THE STRUCTURE AND FUNCTION
OF MACROMOLECULES
Polymer principles
And
Macromolecules
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
Polymers principles: The synthesis and breakdown of
polymers.
A)- Carbohydrates
Monosaccharides
(Classifications of Monosaccharides: Types and examples).
Disaccharides
Polysaccharides: Types and examples
A)- Storage Polysaccharides.
B)- Structural Polysaccharides
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1. Cells join رsmaller organic molecules (Monomers) together to form
larger molecules (macromolecules) (Polymers), which may be composed
of thousands of molecules.
2. Macromolecules are organic molecules that weigh more than 100,000
daltons (ATOMIC MASS UNIT).
3. The four major classes of macromolecules are:
a) - Carbohydrates,
b) - Lipids,
c) - Proteins,
d) - Nucleic acids (will be studied later: lectures 19 & 20 and 21)
Monomers are connected by covalent
bonds through a dehydration
reaction اعل زع ال اء.
One monomer provides a hydroxyl
group and the other provides a
hydrogen to form water.
This process requires energy and is
aided by enzymes.
The covalent bonds connecting monomers in a polymer can be disassembled
ـ ُ َ ــرby hydration (hydrolysis) reaction إ ا ا اء ا.
In hydrolysis as the covalent bond is broken, a
hydrogen atom and a hydroxyl group from a split
water molecule attaches where the covalent
bond used to be.
Hydrolysis reactions dominate the digestive
process, guided by specific enzymes.
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Mono-mer Di-mer Poly-mer
Sugars, Carbo = carbon, hydrate = water; Used as an immediate energy source.
The molecular formula is CnH2nOn means that, carbon, hydrogen and oxygen are found
in the ratio = 1:2:1
1. Monosaccharides:
are the simplest form of carbohydrates (simple sugars).
contain a single sugar molecule.
2. Disaccharides:
contain two monosaccharides joined via dehydration
synthesis
3. Polysaccharides:
are polymers of many monosaccharides.
H O H O
C C
H C OH H C OH
OH C H OH C H
H C OH OH C H
Asymmetric C
Asymmetric C H C OH H C OH
H C OH H C OH
H H
An OH group is attached to each carbon except one, which is double bonded to an oxygen (carbonyl).
Fructose
Triose Sugar Pentose Sugar Hexose Sugar
C6H12O6
H
H OH
H O C Ketone sugar
H O
C C O
C
H C OH OH C H
H C OH
H C OH H C OH
H C OH
H
H C OH
H C OH
Glyceraldehyde H C OH
H C OH
H Ribose
H
Aldoses: are the monosaccharides with the carbonyl group
(C=O) at the end of Carbon chain (e.g. Glucose).
Ketoses: are the monosaccharides with the C=O carbonyl
group within داthe Carbon chain (e.g. Fructose).
Triose (3C): e.g.Glyceraldehyde.
Pentose (5C): e.g. Ribose.
Hexose (6C): e.g. Glucose, Fructose and Galactose.
Consist of 2 monosaccharide molecules joined during a
dehydration reaction ا اء ا.
Sucrose (table sugar): consists of Glucose + Fructose.
The covalent bond formed between Glucose & Fructose is called “glycosidic linkage”.
They consist of few hundreds to few thousands
of monosaccharides joined by a dehydration
reaction.
These are of two types:
1- Storage . Provide sugar for cell by hydrolysis اء إ ا.
2- Structural ر. Serve as building materials for the organism.
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A storage polysaccharide of plants (within plastids).
It consists of thousands of glucose molecules.
Thus, it gives glucose when hydrolysed إ ا ا اءby special enzymes in humans. .
Potatoes and grains are the major sources of starch.
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II- Glycogen (in animals) ﭽـ ال ل
Stored in animal cells (e.g. liver and muscle cells in Human).
It is consisted of thousands of glucose molecules.
Thus, it gives glucose when hydrolysed.
I- Cellulose
It is the building material of plant cell wall.
Forms the micro-fibrils and cell wall in plants.
It is consisted of thousands of β glucose molecules.
Humans cannot digest it, but some bacteria and protozoa can (e.g.
in Termites and Cows stomach).
II- Chitin ال
It is the building material of the cuticle ا ُ ـ َ دin insects.
It is consisted of thousands of glucose molecules
with a N atom at one end.
It is used to manufacture the surgical threads.
(Glucose) (Sucrose)
Starch (in plants) Cellulose (in plants)
& &
Glycogen (in animals) Chitin (in insects)
Triose (3C) Pentose (5C) Hexose (6C)
Glyceraldehyde Ribose Glucose
Aldose Ketose
C=O on top C=O within chain
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
2) Proteins (Polypeptides)
The functions of proteins.
The amino acids.
The peptide Bond.
3)Lipids
The functions of lipids.
The structure of fat molecule.
The types of fats.
3
Proteins are polymers of amino acids (constructed from 20 amino
acids).
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
Amino acids ة اض ا ا
- The components of amino acid include a hydrogen atom, a carboxyl
group, an amino group, and a variable رةR group (or side chain).
H H O
General Formula
of the Amino Acid: N C C
H OH Carboxyl
Amino
group
R group
Amino acids ة اض ا ا
Side chain
- Differences in the R groups produce the 20 different amino acids.
Hydrophobic: the amino acids that have hydrophobic R groups (non-polar).
Hydrophilic: the amino acids that have polar R groups, making them
hydrophilic.
Ionized: the amino acids with functional groups that are charged (ionized) at
cellular pH (7). So, some R groups are bases, others are acids.
The peptide bond is formed between the carboxyl
group of one amino acid and the amino group of
the other by dehydration.
Dehydration
Peptide bond
زع ا اء
Amino acids Peptide Polypeptide (Protein)
Amino acids are joined together when a dehydration reaction
removes a hydroxyl group from the carboxyl end of one amino acid
and a hydrogen from the amino group of the other. The resulting
covalent bond is called “peptide bond”.
The repeated sequence (N-C-C) is the polypeptide backbone.
Attached to the backbone are the various R groups.
Polypeptides range in size from a few monomers to thousands.
Hydrophobic (non-polar R group)
Amino
Hydrophilic (polar R group)
acids
Ionized (charged functional groups)
Summary Proteins
Polypeptides
There are four levels of protein structure:
a. Primary Structure ) ( أ
b. Secondary Structure ا
c. Tertiary Structure
d. Quaternary Structure را
It is the general term for compounds which are not soluble in water.
1. Fats store large amounts of energy
2. Phospholipids are major components of cell membranes
3. Steroids include cholesterol and certain hormones 9
Long chains of mostly carbon and hydrogen atoms with a -COOH group at
one end.
When they are part of lipids, the fatty acids resemble long flexible tails.
Glycerol
H H H
Fatty Acid
O H H
H C C C H
OH C C C
H C OH H H
Ester link
H H H
H C OH
H C OH Dehydration
H
In a fat, three fatty acids are joined to a single glycerol by an ester
linkage, را إ رcreating a triacylglycerol.
Thus, the fat molecule is constructed from two kinds of smaller
molecules: glycerol and fatty acids (so, it is not a true polymer)
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The Fatty acid components are saturated when there is no double bond
between the carbons. All Carbn are linked with Hydrogen .
The Fatty acid components are saturated (i.e. there is no double bonds between
the carbons (all C are linked with H).
They have only single C-C bonds in their fatty acids.
They solid at room temp
Include most animal fats
The double bonds are formed by the removal of H atoms.
Are liquid at room temperature.
There is one or more double bonds between carbons in their fatty acids allows for
kinks in the tails
Include most plant fats
They can be synthetically converted to saturated (solid) by adding H
(Hydrogenation َ)ا َ ْد َر ـ.
1- Phospholipids: are the major components of cell membranes
Phospholipids have two fatty acids attached to a glycerol molecule and a
phosphate group at the third position.
The phosphate group carries a negative charge.
The fatty acid tails are HYDROPHOBIC, but the
phosphate group and its attachments form a
HYDROPHILIC head.
Thus, it is AMPHIPATHIC: has both hydrophobic
and hydrophilic regions
2. Steroids: are hydrophobic molecules
some of them are forming hormones
(Sex Hormones)
3. Waxes
have
: areboth hydrophobic
hydrophobic regions and
molecules
used hydrophilic regions
for waterproofing
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Fats Phospholipids Steroids Waxes
The major component Sex Hormones
of the cell membrane & Cholesterol
Saturated Unsaturated
Animal Fats Vegetable Fats
Hydrogenation
َـد َْر ـَــــــــة
2
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
• Describe why viruses are not considered living
organisms.
• Describe the basic structure of viruses.
A virus consists of a nucleic acid surrounded by a
protein coat.
• Viral Genomes.
• Capsids and Envelopes.
• Viruses replicate only in host cells.
• Replicative Cycles of Phages.
The Lytic Cycle.
The Lysogenic Cycle.
• Compare the lytic and lysogenic cycles of virus
replication.
• At the boundary of life, between the macromolecules (which are not
alive) and the prokaryotic cells (which are alive), lie the viruses and
bacteriophages (phages).
• These creatures are parasites responsible for causing many diseases
in living things (HIV in humans, as an example).
• Viruses are found everywhere.
• Viruses consist of a core of nucleic acid, either DNA or RNA, and a
protective coat of protein molecules and sometimes lipids.
• Viruses show none of the expected signs of life.
• Viruses do not respond to stimuli, do not grow, do not do any of the
things we normally associate with life.
• Viruses are not considered "living" organisms. However, they do show
one of the most important signs of life: the ability to reproduce in a
host cell.
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
1- Viruses are much smaller than bacteria
2- Virus is about 20nm in diameter
3- Viruses are not cells
4- A virus is a genome
ا ض ووenclosed in a
protective coat طاء وا
bacteriophages
Genome (DNA/RNA)
Protein coat (capsid) 6
• A protein shell that encloses the viral genome.
• It is rode-shaped, helical, polyhedral or more complex.
• Capsomeres: Are the protein units that form capsid.
Capsomeres
(proteins)
Capsid
Membranous envelop
(viral envelope)
Sometimes further wrapped ُ َ َّفin a membranous
envelope (Viral envelope ) ال طاء ال روس, eg. Influenza virus.7
• Some viruses have viral
envelopes, membranes
cloaking their capsids.
• These envelopes are derived
from the membrane of the host
cell.
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Viral genomes may consist of:
- double-stranded DNA (dsDNA),
- single-stranded DNA (ssDNA),
- double-stranded RNA (dsRNA),
- single-stranded RNA (ssRNA).
depending on the specific type of a
virus.
The viral genome is usually organized
as a single linear or circular molecule
of nucleic acid.
The smallest viruses have only four
genes, while the largest have several
hundred.
Living Cell
Obligate parasitism اار التط ل ا
1-Inters the cell and releases its genome
2- Replicates using host nucleotides
and enzymes Viral RNA
3- Produce a new capsid units using
host cell resources.
Capsid
4- The new viral DNA and proteins Proteins
assemble to form new viruses
• A viral infection begins when
the genome of the virus enters
the host cell.
• Once inside, the viral genome
commandeers its host,
reprogramming the cell to copy
viral nucleic acid and
manufacture proteins.
• The nucleic acid molecules and
capsomeres then self-assemble
into viral particles and exit the
cell.
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• Human Immunodeficiency Virus (HIV), the virus that causes AIDS
(Acquired Immuno-Deficiency Syndrome) is a retrovirus.
• A retrovirus is an RNA virus that is
duplicated in a host cell using the
reverse transcriptase enzyme to
produce DNA from its RNA genome.
The DNA is then incorporated into
the host's genome by an integrase
enzyme. The viral particle includes:
1) an envelope with glycoproteins,
2) a capsid containing
two identical RNA strands as its genome
3) Two copies of reverse transcriptase.
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Video: plays in LMS
Source: http://highered.mcgraw-hill.com/sites/dl/free/0072437316/120060/ravenanimation.html
• Viruses that infect bacteria,
are called bacteriophages or
phages.
• It has a 20-sided capsid-head
that encloses their DNA and
protein tail piece that attaches
the phage to the host and
injects the phage DNA inside.
• Phages reproduce by Lytic
Cycle ( )د رة ــــةand/or
Lysogenic cycle ( ) د رة ة أ ا ا.
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Phages reproductive cycles within bacteria:
Virus
Bacteria
1)- lytic cycle (ـلل ة )الدورة الت,
The phage reproductive cycle results in the death of the host.
In the last stage, the bacterium lyses (breaks open) and releases
the phages produced within the cell to infect others.
• Virulent phages اتلة روسات reproduce only by a lytic cycle.
Phage T4
(virulent viruses)
ت روس
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The phage genome replicates without Temperate
destroying the host cell. virus
ـ ــروس
ر ت
• Temperate phages, like phage lambda ()ג,
may use both lytic and lysogenic cycles.
• Within the host, the virus’ circular
DNA engages in either the lytic or lysogenic cycle.
• During a lytic cycle, the viral genome immediately turns
the host cell into a virus-producing factory, and the cell
soon lyses and releases its viral products.
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18
Video: plays in LMS
Many tail fibres Only 1 tail fibre
(virulent virus) Temperate virus
&
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Most viruses of eukaryotes attack specific tissues. eg. Human cold viruses
infect only the cells lining the upper respiratory tract, and AIDS virus binds
only to certain white blood cells (Immune system).
- DNA enclosed in a protein coat (sometimes, membranous envelope also)
- Can be crystallised تالور
- They lack ت دenzymes for metabolism
- Have no ribosomes for making their own proteins
- Reproduce only within a living host cell (obligate parasitism )تط ل إ اار.
- Each type of a virus infects a limited range of host cells (host range ) د ا صااة
Viruses are host specific
• a protein on the surface of
the virus has a shape that
matches a molecule in the
plasma membrane of its
host, allowing the virus
recognize the host cell.
2
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
The Cell: Discovery of the Cell
The Cell Theory.
Types of cells.
The two min Domains of Living Organisms
(Prokaryotes and Eukaryotes ).
Similarities between Prokaryotic and Eukaryotic Cells
Differences between Prokaryotic and Eukaryotic Cells
3
The first person to see
cells was Robert Hooke in
1665.
He was looking at a thin slice
of cork through a microscope
He found what he described as
"tiny rooms" that he called
cells
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
In 1838, the German botanist Matthias Schleiden
concluded that all plants were composed of cells
In 1839, Theodor Schwann concluded the same thing
for animals
In 1855, Rudolf Virchow noted that all cells come from
other cells
The cell theory states that:
1) all living organisms are made of one or more cells,
2) cells are the basic units of structure and function, and
3) cells come only from pre-existing cells.
A cell is the smallest unit that can carry
on all of the processes of life
ة ا اة
بدا ة ا اة
Bacteria and related All other forms
micro-organisms of life
ا ات د ة ب ة ب ا اب ترا
Domains of life
A)- Prokaryota
Contains 2 Kingdoms:
1. Archaea,
2. Bacteria (Eubacteria),
B)- Eukaryota
Contains 4 Kingdoms:
1. Fungi
2. Protista
3. Plantae
4. Animalia
All cells are surrounded by a plasma membrane اء ب ز .
The semi-fluid substance ا ادة ب ا ا ةwithin the cell is called
“cytosol”, ت ب ز اcontaining the cell organelles ة ات ا ِ .
All cells contain chromosomes which have genes in the form of DNA.
All cells have tiny organelles رة ات called “Ribosomes” that
make proteins.
1. Eukaryotes have a nucleus, while prokaryotes do not.
2. Eukaryotes have membrane-bound organelles, while prokaryotes do
not.
3. Eukaryotic cells are, on average, ten times the size of prokaryotic cells.
4. The DNA of eukaryotes is much more complex and therefore much
more extensive than the DNA of prokaryotes.
5. Prokaryotes have a cell wall composed of peptidoglycan. Many types of
eukaryotic cells also have cell walls, but none made of peptidoglycan.
6. The DNA of prokaryotes floats freely inside the cell; the DNA of
eukaryotes is held within its nucleus and associated with histones
(proteins)
7. Eukaryotes undergo mitosis and meiosis; prokaryotes divide by binary
fission (simple cell division)
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Prokaryotes Eukaryotes
Nucleus
Endoplasmic reticulum
Plasma membrane Golgi apparatus
Ribosomes Lysosomes
Cytosol Vacuoles
Cell wall Mitochondria
Cytoskeleton
What are Prokaryotes?
Prokaryotes are single-celled (Unicellular)
organisms that do not have a membrane-bound true
nucleus, and can live in nearly every environment on
earth.
Although tiny, prokaryotes differ greatly in their
genetic traits, their modes of nutrition, however,
their habitats are similar.
Based on genetic differences, prokaryotes are
grouped into two Major Domains: Domain Archaea
and Domain Bacteria.
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
Archaea are extremophiles, “ ُ ب ظر ف
”ا ا ةof extreme environments and can
be classified into:
a)- Extreme halophiles ة ُ ب:
live in such saline places as the
Great Salt Lake and the Dead Sea.
Some species require an extremely
salty ة د دة اenvironment to grow.
b)- Extreme thermophiles رارة ُ بlive in
hot environments.
The optimum temperatures for
most thermophiles are 60 - 80°C.
1
2
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
2)- Bacteria
Structure of the bacterial cell.
Shapes of bacteria.
The Gram’s stain.
Reproduction of bacteria.
Major Nutritional Modes.
3
Bacteria occur in many shapes and sizes. Bacteria are of four shapes: rod-
shaped, sphere-shaped, spiral-shaped, or filamentous-shaped.
ا داب
اة ب
ا ر ب ز ات
اء ب ز
ا دار ا
ة ا ب
اط ا
Plasma Cell Wall Capsule
membrane
Ribosomes Nucleoid Cytoplasm
(Cytosol)
Bacteria have one of three basic shapes:
A. Spiral shaped bacteria in the form of spirilla (singular, spirillum)
or vibrio (comma like).
B. Sphere-shaped bacteria are called cocci (singular, coccus). An
example of cocci is Micrococcus luteus. Cocci are single or
aggregate cells in different shapes.
C. Rod-shaped bacteria are called bacilli (singular, bacillus). An
example of bacilli is Escherichia coli. Bacilli are single or
aggregate cells in different shapes also.
It is a tool for identifying ت ر فbacteria, based on differences in
their cell walls.
A)- Gram-positive (Gram +ve) bacteria:
Their cell walls have large amounts ة رةof peptidoglycans
that react with Gram’s stain (appear violet-stained ا ُ )تـ.
B)- Gram-negative (Gram -ve) bacteria:
their cell walls have no or small amount of
peptidoglycan. So, they do not react (or very weakly react) with
Gram’s stain (appear red-stained ر )تصب با
Gram Stain
Most species of bacteria are classified into two categories
based on the structure of their cell walls as determined by
a technique called the Gram stain.
Gram-positive bacteria have a thick layer of
peptidoglycan in their cell wall, and they appear violet
under a microscope after the Gram-staining procedure.
Gram-negative bacteria have a thin layer of
peptidoglycan in their cell wall, and they appear reddish-
pink under a microscope after the Gram-staining
procedure.
Gram +ve bacteria: have Large amount of peptidoglycan
that stained violet.
Gram –ve bacteria: Have small amount or no peptidoglycan
stained red.
Most Gram-negative species are pathogenic (رضة ) more
threatening ( )أ ر ط رةthan gram-positive species.
Gram-negative bacteria are commonly more resistant (ا ة )أ ر
than gram-positive ones to antibiotics ادات ا ات ة .
Many prokaryotes (bacteria)
secrete a sticky
protective layer called
capsule outside
the cell wall.
Capsule has the
following functions ظا:
1. Adhere ت تbacterial cells to their substratum ا ط.
2. Increase bacterial resistance ا ا ةto host defenses ا ة ا ا.
3. Stick ) )تbacterial cells together when live in colonies.
4. Protect تbacterial cell.
In all prokaryotes, the functions of the cell wall are as
follow:
1. maintains ت افظthe shape of the cell,
2. affords physical protection ة اةاط ت فر ا
3. prevents the cell from bursting ( )إ ارin a hypotonic
environment ض ز ا ا ب ة ذات ا تر ز ا.
Most bacterial cell walls contain peptidoglycan
(a polymer of modified sugars cross-linked by short polypeptides).
The walls of Archaea lack ( )تـ ـتـ ـدpeptidoglycan.
ا ب تر ا ات ار
Prokaryotes reproduce ()تـتـ ا ر
only asexually (ا ) by
binary fission ()ا ـا ا ـ ا ا ب ط.
A single cell produces a
colony of offspring.
Video: plays in LMS
Nutrition refers to how an organism obtains
energy and a carbon from the environment to build
the organic molecules of its cells.
• Prokaryotes are grouped (ص ٍ ـَت
ُ ) into four
categories ( )أ اعaccording to how they obtain
energy and carbon
Phototrophs (ة ا ت ذ ة )ض: Organisms that obtain energy from light.
Chemotrophs (ة ا ت ذ ة ا ): Organisms that obtain energy from
chemicals in their environment.
Autotrophs ()ذات ة ا ت ذ ة: Organisms that use CO2 as a carbon source.
Heterotrophs () ت دد ا ت ذ ة: Organisms that use organic nutrients as
a carbon source.
Photoautotrophs (ة )ذات ة ا ت ذ ة ا:
use light energy as an energy source, and CO2 as a carbon source to
synthesize ( )تorganic compounds.
Chemoautotrophs )ا ة )ذات ة ا ت ذ ة ا:
use chemical inorganic substances as an energy source, and CO2 as a carbon
source.
Photoheterotrophs (ة ) ت دد ا ت ذ ة ا:
use light as an energy source, and organic substances as carbon sources.
Chemoheterotrophs (ا ة ) ت دد ا ت ذ ة ا:
use organic substances as a source for both energy and carbon.
B- Eukaryotic Cell
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
• Eukaryotic Cell Organization.
• Introduction: Internal membranes
compartmentalize the eukaryotic cell.
• Plant & Animal Cells: Similarities and
Differences.
• The Cell Organelles:
1. The nucleus.
Nucleolus.
2. Ribosomes
Types of Ribosomes
3
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
• An eukaryotic cell has internal membranes, which partition
the cell into compartments.
• These membranes also participate in metabolism as many
enzymes are built into membranes.
• The general structure of a biological membrane is a double
layer of phospholipids and diverse proteins.
• Each type of membrane has a unique combination of lipids
and proteins for its specific functions.
For example, those in the membranes of mitochondria function in cellular
respiration.
7
• Similarities
Both are eukaryotic cells
Both contain similar organelles
Both are surrounded by cell membrane
• Differences
Plants have
• Cell wall – provides strength & rigidity and is
not found in animal cells.
• Have chloroplasts that is photosynthetic and
are not found in animal cells.
Animals have
• Lysosomes, centrioles and flagella are not
found in plants.
• Centrioles have important role in cell division.
• The nucleus contains most of the genes in an eukaryotic cell as it is
the repository for genetic material.
• The nucleus is separated from the cytoplasm by a double membrane
called nuclear envelope.
• It directs activities of the cell.
• The nuclear membrane contains pores that allow macromolecules and
particles to pass through.
• The nuclear membrane is maintaining the shape of the nucleus.
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• The nucleus contains the “chromatin fibers which are made up
of DNA and proteins.
• When the cell prepares to divide, the chromatin fibers coil up
and condensed to be seen as “chromosomes .
• Each eukaryotic species has a characteristic number of
chromosomes.
- A typical human cell has 46 chromosomes, but sex cells or gametes (eggs
and sperms) have only 23 chromosomes.
• The nucleus directs protein synthesis by synthesizing
messenger RNA (mRNA).
The mRNA travels to the cytoplasm and combines with ribosomes
to translate its genetic message into the primary structure of a
specific protein.
• Nucleolus is a dark region involved in production of ribosomes.
• Ribosomes: are RNA-protein complexes composed of two
subunits (large and small) that join and attach to messenger
RNA to carry out protein synthesis.
• So, it is the site of protein synthesis
• Ribosome assembly begins in the nucleolus and is completed
in the cytoplasm.
• In the nucleolus, ribosomal RNA (rRNA) is synthesized and
assembled with proteins to form ribosomal subunits.
• The subunits pass out through the nuclear pores to the cytoplasm
where they combine to form ribosomes.
• Cells that synthesize large quantities of proteins (e.g., pancreas)
have large numbers of ribosomes.
• Types of Ribosomes:-
1) Free ribosomes are suspended in the cytosol and synthesize
proteins that function within the cytosol.
2) Bound ribosomes are attached to the outside of the endoplasmic
reticulum.
These synthesize proteins that are either included into
membranes or for secretion outside the cell.
17
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
3)- The Endomembrane System
a. The endoplasmic reticulum (ER)
Smooth ER.
Rough ER .
b. Golgi apparatus.
c. Lysosomes.
d. Vacuoles.
4)- Other membranous organelles
a. Peroxisome.
b. Mitochondria.
3
• Largest internal membrane, composed of
lipid bilayer
• Serves as a system of channels from the
nucleus
• Functions in storage and secretion
• There are two types of ER those are
different in structure and function.
1. Smooth ER looks smooth because it
lacks ( does not have ) ribosomes.
Rough Smooth
2. Rough ER looks rough because
ribosomes (bound ribosomes) are attached
to its outside.
The smooth ER:
• It is smooth as it lacks the associated ribosomes.
• It is rich in enzymes and plays a role in metabolic processes.
• Its enzymes synthesize lipids (oils, phospholipids and steroids).
including the sex hormones.
• Extensive in the liver, it helps in detoxifying drugs and poisons.
The rough ER:
• It is “rough” because of the associated ribosomes (sites of protein
synthesis)
• It is especially abundant in those cells that secrete proteins such as
digestive glands and antibody-producing cells.
• These secretory proteins are packaged in transport vesicles that
carry them to their next stage.
• Collect, package, and distribute molecules
synthesized at one location in the cell and utilized
at another location
• Many transport vesicles from the ER travel to the
Golgi apparatus for modification of their contents.
• The Golgi body s function is manufacturing,
warehousing, sorting (Packaging), and shipping
materials to outside the cell.
• The Golgi also manufactures polysaccharides.
• It correctly send proteins to their respective address.
• If the Golgi makes a mistake in shipping the proteins to the right address,
certain functions in the cell may stop.
• The Golgi apparatus is more abundant in secretory cells.
• The lysosome is a membrane-
bounded sac of enzymes that
digests macromolecules.
• Lysosomal enzymes work best at pH
= 5 (acidic).
• The lysosomal enzymes are
synthesized by rough ER and then
transferred to the Golgi then to
lysosomes.
1) They hydrolyse proteins, fats, polysaccharides, and
nucleic acids.
2) Can destroy the cell by autodigestion (autophagy).
3) Can fuse with food vacuoles to digest food, (when a
food item is brought into the cell by phagocytosis).
4) Can also fuse with and digest another organelle or
part of the cytosol. This process is called recycling
which renews the organelle and/or the cell.
5. They digest unwanted particles.
6. They help white blood cells to destroy bacteria.
Video: plays in LMS
Source: http://highered.mcgraw-hill.com/olc/dl/120067/bio01.swf
• They are membrane-bound sacs with varied
functions such as storage, digestion, and waste
removal.
• Contain water solution and help plants maintain
shape.
There are different types of vacuoles including:
1. Food vacuoles, from phagocytosis, fuse with
lysosomes for digestion.
2. Contractile vacuoles, found in freshwater
protists (eg. Paramecium) to maintain water
balance (osmoregulation) by pumping excess
water out of the cell.
3. Central vacuoles (in mature plants) store
wastes, maintain the cell shap.
A)- Peroxisomes
• Peroxisomes are similar in appearance to
lysosomes, but the two have different
origins. Lysosomes are generally formed in
the Golgi complex, whereas peroxisomes
self-replicate themselves.
• Contain enzymes for degrading amino acids
and fatty acids. These reactions produce a
toxic hydrogen peroxide; (H2O2) as a
byproduct of cellular metabolism.
1- Hydrogen peroxide (H2O2) is a poison, but the peroxisome has
enzymes that converts H2O2 to water (H2O).
2- Some peroxisomes break fatty acids down to smaller molecules
that are transported to mitochondria as fuel (cellular respiration).
3- They detoxify alcohol and other harmful compounds. Thus, it
exists extensively in the liver cells.
4- Initiate the production of phospholipids, which are typically used
in the formation of membranes.
B)- Mitochondria:
They are rod-shaped organelles that convert oxygen and nutrients
into ATP (adenosine triphosphate) during aerobic respiration.
• Mitochondria are the sites of cellular respiration,
• Generating ATP from the catabolism of sugars,
fats, and other fuels in the presence of oxygen.
• Almost all eukaryotic cells have mitochondria.
• Mitochondria are mobile and move around the cell
along tracks in the cytoskeleton.
• Mitochondria have a smooth outer membrane and a highly folded inner
membrane forming the cristae.
• The inner membrane encloses the mitochondrial matrix, a fluid-filled space
with DNA, ribosomes, and enzymes.
The number of mitochondria present in a cell depends upon the metabolic
requirements of that cell, and may range from a single large mitochondrion to
thousands of the organelles.
The mitochondrion is different
from most other organelles
because it has its own circular
DNA (similar to the DNA of
prokaryotes) and reproduces
independently of the cell in
which it is found.
B- Eukaryotic Cell
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
5)- The Cytoskeleton: structure and function.
Microtubules
Microfilaments
Intermediate filaments
Centrosome
Cilia and Flagella
6)- Cell membrane
3
A network of fibres ا اف بthat provides structural support تدto the
cell. The cytoskeleton also functions in cell motility ت ر اand
regulation.
It is made up of 3 types of fibers
1. Microfilaments
2. Microtubules
3. Intermediate filaments
It has 3 main functions:
1. Provides mechanical support of
the cell and keeps organelles in
their fixed locations.
2. Helps moving materials within
the cell
3. Plays a major role in cell motility
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
Microfilaments
Intermediate
Microtubules Microfilaments filaments
أ ب بات د أ اف د أ اف ت سط
Thick Thin Middle
ر ط
Responsible for cell Support cell Reinforcing the cell
motility, and motility and shape and fixing
separation of transport materials position of
chromosomes during within the cell. organelles.
cell division.
(Actin protein) (Fibrous protein)
(Tubulin protein)
The cytoskeleton is dynamic, dismantling تفin one part and
reassembling تin another to change cell shape.
The cytoskeleton plays a major role in cell motility ر اby
interacting with motor proteins. ا بر ت ا ر.
Motor proteins are able to move along the surface of a suitable
substrate (powered by ATP).
Motor proteins are the driving force behind most active transport of
proteins and vesicles in the cytoplasm.
Cell Movement
In cilia and flagella motor
proteins pull components
of the cytoskeleton past
each other سب.
This is also true in muscle
cells.
Motor proteins are a class of molecular motors that are able to move along the
surface of a suitable substrate. They are powered by the hydrolysis of ATP and
convert chemical energy into mechanical work.
MOTOR PROTEINS "WALKS" ALONG A MICROTUBULE TRACK
Transport
vesicle
ATP ADP+Pi ATP ADP+Pi
Motor proteins
Microtubule
Interactions of motor proteins and the cytoskeleton circulates
materials within the cell.
The cytoskeleton may transmit mechanical signals that
rearrange the nucleoli and other structures.
Motor molecules also
carry vesicles or organelles
to various destinations
تف إ أ اprovided by the
cytoskeleton.
Organelle
Motor
Protein P
Energy
Microtubules functions as tracks بthat guide motor proteins carrying
organelles to their destination ا ا ا ست دف.
They move chromosomes during cell division
Video: Plays in LMS
In many cells, microtubules grow out from a centrosome ا س
ا ر زnear the nucleus.
Centrosome
In animal cells, the centrosome has a pair of centrioles, each
with 9 triplets of microtubules ا ب بات ات ( تس9 + 0 pattern)
arranged in a ring ُ ر ب دا ر ا.
During cell division the
centrioles replicate تت ا ف.
12
Microtubules are the central structural supporting both
cilia ا دابand flagella ا س اط.
Both can move unicellular and small multicellular organisms by
propelling دwater outside the organism.
Movement of cilia & flagella
Cilia usually occur in large numbers on the cell surface.
Flagella usually occur in just one or a few per cell.
Cilia move more like oars ادبفwith alternating power and recovery
strokes.
Flagella have an undulatory movement ر ت.
So, they differ in their beating pattern أس ب ا ر.
cilia
14
Video: Plays in LMS
15
flagellum
16
Video: Plays in LMS
17
Both cilia and flagella have the
same ultrastructure ا ر ب ا د.
Both have a core ر زof
microtubules sheathed by the
plasma membrane.
9-doublets (9 + 2 pattern) ات تس
ب بتا ا اof microtubules arranged
around a pair at the center.
Flexible “wheels of proteins connect
outer doublets to each other and to
the core.
The outer doublets are also
connected by motor proteins.
Thus, the structure of the cilium and
flagellum is different from that of the
centriole. 1
Cilia and flagella are formed of arms of a motor
protein (dynein )بر ا دا.
Dynein arms alternately
grab, move, and release
the outer microtubules.
Protein cross-links limit
sliding and the force is
expressed as bending إ ت اء.
1
http://www.northland.cc.mn.us/biology/biology1111/animations/flagellum.html
The plasma
membrane
functions as a
selective barrier
ا ز إ ت ارthat
allows passage
of oxygen,
nutrients, and
wastes for the
whole volume of
the cell.
20
Composed of a kind of lipids
(phospholipids) and proteins
Lipid layer contains hydrophilic
and hydrophobic regions
Hydrophilic اء ُ ب
Phospholipid
Hydrophobic اء ار
Proteins
Comparison between
Prokaryotes and Eukaryotes
Term Prokaryotes Eukaryotes
Size 1-10 µm in diameter 10-100 µm in diameter
Cell wall Existed In plant cell (not animal cell)
No nuclear envelope but True nucleus exists with
nucleus
Nucleoid nuclear envelope
As fibre in the nucleoid As Chromatin (DNA and
DNA
region (plasmids in some cases) protein)
Specialized
Most of them are absent All are existed
Organells
Cell
By Binary Fission Meiotic and/or Mitotic
division 23
24
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
Cell Membrane Structure:
Cell membrane is mosaics of structure and function.
• The plasma membrane has a unique collection of proteins.
• These proteins may provide a variety of major cell functions.
• Specific proteins facilitate passive transport.
Cell Membrane Functions:
• Selective permeability.
• Passive transport.
A. Diffusion
B. Osmosis
Osmoregulation
C. Facilitated Diffusion.
The plasma membrane separates the living cell from its
nonliving surroundings.
This thin barrier, 8 nm thick, controls traffic into and out
of the cell.
Like other membranes, the plasma membrane is
selectively permeable ُ ِذ إ ت ار ا, allowing some substances
to cross more easily than others.
The most abundant lipids in the cell membrane are
phospholipids.
Phospholipids and most other membrane constituents
are amphipathic molecules.
Amphipathic molecules have both hydrophobic regions and
hydrophilic regions.
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
The lipid molecules in the bilayer طب زدare
arranged as hydrophobic fatty acid tails that
are sheltered from water while the
hydrophilic phosphate groups interact with
water.
Some membrane proteins are amphipathic, Fig. 8.1b
with hydrophobic and hydrophilic regions.
If at the surface, the hydrophilic regions
would be in contact with water.
In this fluid mosaic
model, the hydrophilic
regions of proteins
and heads phospholipids are
in contact with water, while
the hydrophobic regions
are in a non-aqueous ا
environment.
• A membrane is a collage َ َ تـof different proteins embedded
ُ ـ ْ َ ِ سin the fluid matrix of the lipid bilayer.
To work properly
with permeability,
membrane must be
fluid about as fluid
as oil.
B)- The plasma membrane has a unique
collection of proteins.
There are two populations of MEMBRANE PROTEINS.
1. Peripheral protein ( طرhydrophilic) is not embedded in the lipid
bilayer at all. Instead, it is loosely bounded to the surface of the protein,
often connected to the other population of membrane proteins.
2. Integral protein س ُ penetrates the hydrophobic core of the lipid
bilayer, often completely spanning the membrane (a transmembrane
protein). It is amphipathic, because: Integral
proteins
• Where it is in contact with the core, it
has a hydrophobic region.
• Where it is in contact with the aqueous
environment outside the membrane, it
has a hydrophilic region. Hydrophilic
region
Peripheral Hydrophobic
proteins region
Aquaporins (channel proteins): are transport proteins that
function by having a hydrophilic channel that facilitate the
passage of water molecules through the membrane in
certain cells. Without aquaporins, only a tiny fraction of water
molecules would pass through the cell membrane.
Carrier protein (glucose transporter): in the plasma
membrane of red blood cells transports glucose across the
membrane 50,000 time faster than glucose can pass through
on its own.
Nonpolar molecules, such as hydrocarbons, CO2, and O2,
are hydrophobic and can therefore dissolve in the lipid
bilayer of the membrane and cross it easily, without the aid of
membrane proteins.
Thus, the selective permeability of a membrane depends
on both the discriminating barrier of the lipid bilayer and the
specific transport proteins built into the membrane
1- Selective permeability ت ار ا اذ ا
A steady traffic ا ب ر ا تطof small molecules and ions moves across
the plasma membrane in both directions.
For example, sugars, amino acids, and other nutrients enter a muscle
cell and metabolic waste products leave it.
The cell absorbs O2 and expels CO2.
It also regulates concentrations of inorganic ions, like Na+, K+, Ca2+, and
Cl-, by passing them across the membrane.
However, substances do not move across the barrier
indiscriminately ش ا اas membrane is selectively permeable.
Hydrophobic molecules, like hydrocarbons, CO2, and O2, can
dissolve in the lipid bilayer and cross easily as described in the
previous slide.
Ions and polar molecules like H2O and glucose pass through channel
proteins as described in the previous slide.
Thus membrane proteins assist and regulate ظ سا دthe transport
of ions and polar molecules.
CO2
CO2
Nucleus
O2
O2
Selective Permeability
The cell is able to take up تـ ـتـparticular
molecules and exclude ب تـتothers
2- Passive transport ا تا اسب
Involves the movement of molecules across the cell membrane
without the need of energy by the cell.
No ENERGY is required to move substances across membrane
(water, lipids, and other lipid soluble substances).
Rather, the CONCENTRATION GRADIENT represents potential
energy and drives diffusion
Types of Passive transport:
I. Diffusion
II. Osmosis
III. Facilitated Diffusion
I)- Diffusion:
(The passive transport of solutes molecules)
Is the tendency إست دادof molecules of any substance to spread out تشار in the
available space randomly ش ا ا.
• For example, a permeable membrane شاء ذseparating a solution with sugar
molecules from pure water, sugar molecules will cross the barrier randomly.
• The sugar molecules will cross the membrane until both solutions have equal
concentrations of the sugar (dynamic equilibrium )ا ت اد ا د ا.
Lump of sugar
Dynamic equilibrium
• A substance will diffuse from where it is more concentrated to where
it is less concentrated, down its concentration gradient ـ ُ در ا تر ز.
Differences in concentration of dissolved materials in two
solutions can lead to the movement of ions from one to the
other.
• The solution with the higher concentration of solutes is hypertonic.
• The solution with the lower concentration of solutes is hypotonic.
• Solutions with equal solute concentrations are isotonic.
• Osmosis:
Is a passive transport in which water
diffuses across a selectively permeable
membrane from the hypotonic solution
to the hypertonic solution until the
solutions become isotonic.
Osmosis Isotonic Osmosis
Selectively
permeable
membrane
Low conc. of sugar High conc. of sugar
hypotonic hypertonic
• Hypertonic solution: ز ا تر ا
contains high concentration of solute ُ ذابmolecules.
• Hypotonic solution: ز ض ا تر
contains low concentration of solute molecules.
• Isotonic solutions: ت اد
contain equal concentrations of solute molecules.
Biological
Membrane
H2O
Hypertonic Hypotonic
• The cell in a hypertonic environment
will loose water, shrivel ت ش, and
die.
• A cell in a hypotonic solution will
gain تس بwater, swell, and burst.
• Nothing will happen for a cell in an
isotonic solution
Organisms without rigid walls have
osmotic problems in either a
hypertonic or hypotonic environment
and must have adaptations for
osmoregulation to maintain اظ
their internal environment.
Example, Paramecium has a
specialized organelle (the contractile
vacuole), that functions as a pump to
force طردwater out of the cell.
Video: plays in LMS
Behavior of water when a living cell is placed in Hypertonic,
Hypotonic or Isotonic solutions
• Many polar molecules and ions diffuse passively through the lipid bilayer
with the help of transport proteins (gated channels ) ات ُ بَ ب.
• The passive movement
of molecules down its
concentration gradient via a
transport protein is called
facilitated diffusion.
• Many transport proteins
simply provide channels
allowing a specific molecule
or ion to cross the
membrane.
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
B)- Active transport
• Transport of small molecules
• Transport of large molecules (macromolecules).
Exocytosis
Endocytosis
o Phagocytosis
o Pinocytosis
o Receptor-mediated endocytosis
• Some facilitated transport proteins can move solutes against their
concentration gradient, from the side where they are less
concentrated to the side where they are more concentrated.
• This active transport requires metabolic energy via ATP.
• Active transport is critical ا اfor a cell to maintain its internal
concentrations of small molecules.
• Active transport is performed by specific proteins embedded in
the membranes called transport protein (T. protein).
4
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
• The sodium-potassium pump
actively maintains the gradient
of sodium (Na+) and potassium
ions (K+) across the membrane.
Na
– The animal cell has higher
Na Protein
concentrations of K+ and lower
Na molecule
concentrations of Na+ inside Na
the cell.
– The sodium-potassium pump
(T. protein) uses the energy of
one ATP to pump 3 Na+ ions
out and 2 K+ ions in.
1ATP T. protein ATP
Low conc. High conc.
+ 2 + Cellular
of K of K membrane
High conc. Low conc.
of Na
+ 3 of Na+
6
7
http://highered.mcgraw-hill.com/sites/dl/free/0072437316/120060/ravenanimation.html
Two roles of
membrane protein
Both diffusion and facilitated diffusion are forms of passive transport of
molecules down their concentration gradient, while active transport requires an
investment of energy to move molecules against their concentration gradient.
2)- Transport of large molecules (macromolecules)
Large molecules are transported by Exocytosis and endocytosis
Small molecules and water enter or leave the cell
through the lipid bilayer or by transport proteins.
Large molecules, such as polysaccharides,
proteins and lipoprotein particles cross the
membrane by vesicles أ ع.
1. Exocytosis ا راج ا:
A transport vesicle budded from أ
the Golgi apparatus is moved by
the cytoskeleton to the plasma
membrane.
When the two membranes come in
contact ت س, the bilayers fuse د ج
and spill ُ رعthe contents to
the outside.
Transport of large molecules (macromolecules)
2- Endocytosis ا د ا ا:
A cell brings in macromolecules and particulate matter by forming
new vesicles from the plasma membrane and include the
following:
A)- Phagocytosis ا ت ع ا:
• Called “cellular eating”. The cell engulfs تـَ ْ َعa particle by extending pseudopodia أ دا اذ
around it and packaging it تـ ُ اin a large vacuole.
• The contents of the vacuole are digested when the vacuole fuses with a lysosome.
10
11
Transport of large molecules (macromolecules)
B)- Pinocytosis, “ ا رب اcellular drinking”.
A cell creates a vesicle around droplets اطof extracellular fluid
ا سا ا ج د ارج ا.
– This is a non-specific process ر ت ع.
Transport of large molecules (macromolecules)
C)- Receptor-mediated endocytosis: تا ت ا ست ع طر ا د ا ا
It Is called (Selective eating) which is very specific in what substances are being
transported.
• It is triggered تـُستـَحثwhen extracellular substances bind to special receptors
ُ ست ـِ ت ا, on the membrane surface. This triggers the formation of a vesicle
• It enables a cell to take large quantities of specific materials that may be in low
concentrations in the environment.
14
Source: http://highered.mcgraw-hill.com/olc/dl/120068/bio02.swf
(Solute molecules) (Solvent molecules) (T. protein) (T. protein) (Membrane)
Exocytosis Endocytosis
Phagocytosis Pinocytosis Receptor-mediated
endocytosis
Cellular eating Cellular drinking Selective eating
Zoology 109 course
General Animal Biology
For Premedical Student
Zoology Department
Lecture 11: Enzymes
(An introduction to metabolism )
1
1438-1439H
Objectives
• Enzymes speed up metabolic reactions by lowering energy barriers.
– Enzymes and Activation Energy.
– Enzymes are substrate specific.
– The active site is an enzyme’s catalytic center.
– Catalytic Cycle of Enzyme.
• Cellular factors affecting enzyme activity:
– Temperature
– pH.
– Cofactors.
• Enzyme inhibitors
– Competitive inhibition.
– Non-competitive inhibition.
– Some benefits of enzyme inhibitors
AN INTRODUCTION
TO METABOLISM
Enzymes
1. Enzymes speed up metabolic reactions by lowering energy barriers.
2. Enzymes are substrate specific.
3. The ac i e i e i a e e ca al ic ce e .
4. A cell h ical a d che ical e i e affec e e ac i i .
ENZYMES:
A protein with catalytic
properties due to its power
of specific activation
3
Pages 96 - 103
Hydrolysis of sucrose (table sugar)
Dehydration
Glucose + Fructose Sucrose
Hydration (H2O)
Glucose + Fructose
Sucrase
Hydrolysis of sucrose in the presence of Sucrase results
in its two monosaccharide components.
This process include:
1- Breaking the bond between Glucose and Fructose;
2- Then, forming new bonds with H+ and OH- from water
This process consumes ت ت energy (Activation Energy; EA)
Enzymes speed up metabolic reactions
by lowering energy barriers ا ز ا طا ة
A catalyst ا ُ زis a chemical agent that changes the rate of a
reaction without being consumed د أ ُ تby the reaction.
An enzyme is a catalytic protein.
Chemical reactions between molecules involve both bond breaking
and bond forming.
To hydrolyze (hydration) sucrose, the bond between glucose and
fructose must be broken via hydrolysis in the presence of sucrase (the
catalyst).
Sucrase
Enzymes and Activation Energy
Activation Energy:
It is the minimum amount of energy needed to start a reaction. It is
the amount of energy needed for the reaction (between enzyme & substrate)
to complete (to break the bonds).
Raising the temperature for these reactions to complete will either
denature the compounds or kill the cell.
Thus, organisms must therefore use a catalyst ز ا.
Catalyst:
It is a chemical agent that accelerate the reaction without being
consumed by the reaction.
Enzyme is a catalytic protein ز /د ر
Enzyme is a specific ت صصcatalyst for specific reactants
at any time in the cell (e.g. Sucrase for only Sucrose).
Activation energy: is the amount of
energy necessary to push the
reactants over an energy barrier.
At the transition state, the molecules
are at an unstable point.
The difference between free energy
of the products and the free energy
of the reactants is the delta G.
Enzyme can increase the rate of
reactions by lowering EA.
The transition state can then
be reached even at moderate
temperatures.
7
Enzymes are substrate specific
• The substrate ا ا ادة ا ط بis a reactant which binds to an enzyme.
• When a substrate binds to an enzyme, the enzyme catalyzes the
conversion تof the substrate to the product ات ا ا ب ا ة.
Sucrase (catalyst) is an enzyme that binds to sucrose (substrate) and
breaks the disaccharide into fructose and glucose (products).
Enzyme (a catalyst)
Substrate Product (s)
Sucrase
Sucrose + H2O Glucose + Fructose
Specificity of enzyme ت صص ة ا زrefers to the shape of its
Active Site ا ر ز ا طinto which fits ـ ُ ا بthe surface of the
substrate.
The active site is an enzyme s catalytic center
The active site ا ا ا طof an enzymes is the groove ا بon the
surface of the enzyme into which the substrate fits.
The specificity of an enzyme is due to the fit between ا ت ا ب بthe
active site and that of the substrate.
As the substrate binds, the enzyme changes shape to fit the
substrate, bringing chemical groups in position to catalyze the
reaction.
Catalytic Cycle of Enzyme
Active site of enzyme and Catalytic Cycle
Sucrose Sucrase
Glucose
Fructose
H2O
Catalytic Cycle of Enzyme
1- The substrate binds to the active site of enzyme.
2- This forms an Enzyme-Substrate complex (via weak
hydrogen bonds).
3- The active site catalyses the conversion of the
substrate to final products (original components) by
breaking bonds.
4- The resulting products release from the enzyme.
5- The enzyme starts another reaction over and over again.
6- Thus, the enzyme can have a huge metabolic effect in
the catalytic cycle.
A single enzyme molecule can catalyze thousands or more reactions
a second.
Enzymes are unaffected by the reaction and are reusable ـ ُ اد ا ت دا ا.
Most metabolic enzymes ة ا ز ات اcan catalyze a reaction in both
the forward and reverse direction.
The actual direction depends on the relative concentrations of products
and reactants.
Enzymes catalyze reactions in the direction of equilibrium ا ت اد.
Enzymes lower activation energy and speed a reaction.
The rate that a specific number of enzymes converts substrates to
products depends in part on substrate concentrations.
At some substrate concentrations, the active sites on all enzymes are
engaged ة , called enzyme saturation ا ت ب ا ز.
A)- Cellular factors affecting enzyme activity
• Changes in shape of the enzyme molecule influence the reaction
rate.
• Some conditions lead to the most active conformation and lead to
optimal rate of reaction. These factors are:-
1. Temperature: has a major
impact on reaction rate.
As temperature increases,
reaction between substrate
and active sites occur faster.
However, at some point
thermal increase begins to
denature the enzyme.
Each enzyme has an optimal
temperature ُ در ة رارة.
14
2. pH also influences the reaction rate, each enzyme has
an optimal pH falls between pH 6 - 8 for most
enzymes.
• However, digestive enzymes in the
stomach are designed to work best
at pH 2 while those in the intestine
are optimal at pH 8, both matching
their working environments.
3. Cofactors : ا ا ا ا دة
A non-protein helpers for catalytic activity of enzymes. They bind
permanently دا اto the enzyme and include two types:-
a)- Inorganic cofactors, include zinc, iron, and copper.
b)- Organic cofactors, include vitamins or molecules derived
from vitamins.(coenzymes)
B)- Enzyme inhibitors: ُ ـ ِّـبطات ا ز ات
• Inhibitors are chemicals that reduce the rate of enzymic reactions.
• The are usually specific and they work at low concentrations.
• They block the enzyme but they do not usually destroy it.
• Many drugs and poisons are inhibitors of enzymes in the nervous system.
• Competitive inhibition ت ب ط ت ا: the inhibitor binds to the same site as
the substrate, thus prevent the enzymatic reactions.
• Non-competitive inhibition: ت ب ط ت ا
the inhibitor binds somewhere other
than the active site, resulting in
changing enzyme shape. Finally,
16
deactivate ـ ُ دthe active site
Some benefits of enzyme inhibitors
The insecticide DDT is inhibitor for key enzymes
of nervous system in insects results in death.
Many antibiotics (e.g. Penicillin) inhibits
enzymes that help bacteria to make their cell
walls.
In the next lecture we will see that:
Activation and inhibition of enzymes
are essential for metabolic control
Reference
18
Thank you
19
2
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
The Control of Metabolism.
Allosteric Regulation of Enzymes
Allosteric Activation
Allosteric Inhibition
Feedback Inhibition
Cooperativity regulation.
In many cases, the molecules that naturally regulate
enzyme activity behave like reversible noncompetitive
inhibitors.
These molecules often bind weakly to an allosteric site Allosteric
site
which is a specific receptor on the enzyme that is not the
active site.
These molecules can either inhibit or stimulate enzyme
activity.
1)- Allosteric Regulation: ت ر اتظ ا
Most allosterically regulated enzymes
are constructed of two or more
polypeptide chains.
Each subunit has its own active site.
The allosteric sites are often located
where subunits are joined.
The whole protein exists in two
conformational shapes, The active
form, and the inactive form.
a)- Allosteric activators طات:
It stabilizes the conformation that
has a functional active site.
b)- Allosteric inhibitors طات:
It stabilizes the conformation that
lacks an active site.
In many cases, both inhibitors and activators are similar enough in
shape that they compete for the same allosteric sites.
These molecules may be products and substrates of a metabolic pathway.
For example, some catabolic pathways have allosteric sites that are inhibited
when ATP binds, but activated when AMP (adenosine monophosphate) binds.
When ATP levels are low, AMP levels are high, and the pathway is turned on
until ATP levels rise, AMP levels fall and inhibition by ATP occurs.
c)- Feedback inhibition
ا ت ط ا ر ا را:
It is one of the common
methods of metabolic control
in which a metabolic pathway
is turned off by its end
product ا ا ا ا.
Example:
The production of Isoleucine
from Thereonine by
Thereonine deaminase:-
The end product acts as an
inhibitor of an enzyme in the
pathway.
When the product is
abundant ر, the pathway is
turned off, when rare the
pathway is active. 6
Video: plays in LMS
7
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2)- Cooperativity regulation اتظ ات ا
It occurs in enzymes with
multiple catalytic subunits.
Lending a substrate to
one active site stabilizes
favorable conformational
changes at all other
subunits, a process called
cooperativity ا ا.
This mechanism amplifies ـُز دthe response ا اof
enzymes to substrates, making the enzymes accept
additional إ اsubstrates.
Summary of metabolic control
The cell is controlling its metabolism by regulating enzyme activity:
1)- Allosteric Regulation:
Regulatory molecules that bind weakly to an Alosteric site of the enzyme
(Allosteric Enzymes) in order to inhibit or stimulate the enzyme activity
A)- Allosteric activation.
B)- Allosteric inhibition
C)- Feedback inhibition.
2- Cooperativity.
Stabilizes favorable conformational changes at all other subunits to
make the enzyme more efficient.
9
2
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
The Principles of Energy Harvest.
Cellular respiration and fermentation are
catabolic, energy-yielding pathways.
Production of Adenosine Tri-Phosphate (ATP).
Redox reactions release energy when electrons move
closer to electronegative atoms.
Electrons “fall from organic molecules to oxygen
during cellular respiration.
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
O2 H 2O
Food
(Fuel of energy)
Respiration Energy
+
O2 CO2
Cellular Activities
Organic compounds + O2 Energy + CO2 + H2O
• ATP (Adenosine Tri-Phosphate) is the important
molecule in cellular energetics ات إ تاج ا طا ة.
– The attachment of three negatively-charged phosphate groups (P) is
an unstable ت ر ر, energy-storing طا ة ز arrangement.
– Loss of the end phosphate group release energy.
– Thus, it can diffuse to any part of the cell and release energy.
• The price of most cellular work is the conversion of ATP
to ADP and phosphate (P).
• An animal cell regenerates ت د إ تاجATP from ADP by adding P via
the catabolism دof organic molecules.
Adenosine
P P P
+ H2O
Triphosphate
Energy P P P
Adenosine Di-Phosphate
P P P
Organelle
Motor P
Protein
Energy
The transfer of the terminal phosphate group from ATP to
another molecule is phosphorylation ـَ ْـ ـَرة.
This changes the shape
of the receiving molecule
in order to work
(transport, mechanical,
or chemical).
• When the phosphate
group leaves the protein
molecule, it returns to
its original shape.
Redox reactions release energy when electrons
move closer to electronegative atoms
• Catabolic pathways relocate بد أ اthe electrons stored in food molecules,
releasing energy that is used to synthesize تATP.
• Reduction-Oxidation reactions (Redox reactions):
Are reactions that result in the transfer of one or more electrons from one reactant
to another
• Oxidation: Is the loss ـدof electrons. Redox reactions require
• Reduction: Is the addition إ ت ابof electrons. both a donor and acceptor of e.
Oxidation Reduction
(Reducing agent) (Oxidizing agent)
Lose electrons Gain electrons
Lose hydrogen Gain hydrogen
Gain oxygen Lose oxygen
+
Xe- + Y X + Y
Oxidation Reduction
(reducing agent) (oxidizing agent)
Na + Cl Na+ + Cl- Energy
Electrons fall from organic molecules to
oxygen during cellular respiration
• In cellular respiration, glucose and other fuel molecules are oxidized, releasing
energy.
e-
C6H12O6 + 6O2 6CO2 + 6H2O + (ATP + Heat)
Reducing Oxidizing Energy = 686 kcal/mol
agent agent Energy
• Glucose is oxidized, oxygen is reduced, and electrons lose potential energy.
• H is the source of electrons that transfers to O.
• Thus, molecules that have an abundance of رةhydrogen are excellent fuels
because their bonds are a source of electrons that fall closer to oxygen.
• Enzymes lower the barrier of activation energy, allowing these fuels to be
oxidized slowly.
• When H moves to O, it leaves bonds which degenerated to release energy.
• The resulting energy is used by the cell to synthesis ATP .
The fall of electrons ا دار ا رduring respiration is
stepwise رح, by NAD+ and an electron transport chain
• Cellular respiration does not oxidize glucose in a single step that transfers
all the hydrogen in glucose to oxygen at one time.
• Rather, glucose and other fuels are broken down gradually تدر ج اin a series
of steps, each catalyzed by a specific enzyme.
• At key steps ا ط ات ا ا ة, hydrogen atoms move from glucose and
passed first to the coenzyme NAD+ (Nicotinamide Adenine Dinucleotide).
• Dehydrogenase enzymes strip two hydrogen atoms from the fuel (e.g.,
glucose), pass two electrons to NAD+ and release H+.
• This changes the oxidized form, NAD+, to the reduced form
NADH. Thus, NAD+ is oxidizing agent as it accepts electrons.
– NAD+ functions as the oxidizing agent in many of the redox
steps during the catabolism of glucose.
Dehydrogenase
H-C-OH + NAD+ C=O + NADH + H+
• As electrons fall from NADH to oxygen, their energy is
used to synthesize ATP.
Electron transport chain
• Cellular respiration uses an electron transport chain ا تر ات ة
to break َ ـ ُ ـthe fall of electrons to O2 into several steps دة ط ات.
• The electron transport chain, consisting
of several molecules (primarily proteins),
is built into the inner membrane of a
mitochondrion.
• NADH takes electrons from food to the
op of he chain.
• A he bo om , o gen cap re he
electrons and H+ to form water.
• Electrons are passed by the chain until
they are caught by oxygen (the most
electronegative).
Summary of electron Fall steps
- Falling of all H atoms from glucose to O is gradually not at once.
- It occurs in steps, each step is catalyzed by an enzyme.
- H atoms of glucose pass first to the co-enzyme NAD+ to form NADH
- Then from NADH to electron transport chain, and finally to O and
releases energy to form ATP.
Mitochondrion
NAD+ e e
Food H NADH Transport chain Oxygen
Energy
ATP ADP
1
2
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
Cellular Respiration: involves three stages:
1. Glycolysis harvests chemical energy by
oxidizing glucose into to two pyruvates
and produces about 5% of ATP (in cytoplasm).
2. Krebs cycle completes the energy-yielding
oxidation of organic molecules and produces
about 5% of ATP (in mitochondrial matrix).
3. Electron transport chain to synthesis ATP and produces about 90% of ATP
(inner mitochondrial membrane).
Cellular respiration generates many ATP molecules. From
each glucose molecule, it produces (38 ATP molecules).
I- Substrate-level phosphorylation:
• Some ATP is generated in glycolysis and in Krebs cycle by
Substrate-level phosphorylation. Phosphate group is transferred from
an organic molecule (the substrate) to ADP,
forming 10% ATP (4 ATP).
II- Oxidative phosphorylation:
• As electrons passed along the chain,
their energy stored in the mitochondrion
in a form that can be used to synthesize
the rest 90% of the ATP (34 ATP).
• via Oxidative phosphorylation.
4
1- Glycolysis (splitting glucose): harvests chemical
energy by oxidizing glucose to 2-pyruvate molecules
• During glycolysis, glucose (a six carbon-sugar) is split into two molecules (each is
three-carbon sugar).
• These smaller sugars are oxidized and rearranged to form two molecules of pyruvate.
• Each of the 10 steps in glycolysis is catalyzed by a specific enzyme.
• These steps can be divided into two phases:
1)- Energy investment phase: طا إ
ATP is consumed to provides activation
energy by phosphorylating glucose
(this requires 2 ATP per glucose).
2)- Energy payoff phase: إ اج طا
ATP is produced by substrate-level
phosphorylation and NAD+ is reduced to
NADH.
• 4 ATP and 2NADH are produced per
glucose.
• Thus, the net yield from glycolysis is
2 ATP and 2 NADH per glucose.
• Oxygen is not required for glycolysis
Summary of Glycolysis (Splitting of glucose)
It is the process of breaking a glucose into 2 Pyruvates.
It is a source for some ATP & NADH and occurs in the
CYTOSOL (cytoplasm).
It has two phases
1)- Glucose is phosphorylated twice by adding 2 P
coming from 2 ATP (substrate-level-phosphorylation).
2)- Thus, Glucose (6-C) splits into two small sugar molecules (each with 3-C).
4ATP are formed by adding 4P to 4ADP molecules.
The net yield of this process is the formation of 2 NADH,
2 ATP and 2 pyruvate molecules.
2. The Krebs cycle completes the energy-yielding
oxidation of organic molecules (in mitochondrial matrix)
• If O2 is present, pyruvate enters the mitochondrion where enzymes of
the Krebs cycle complete the oxidation of this organic fuel to CO 2.
• As pyruvate enters the mitochondrion which modifies pyruvate
to acetyl-CoA which enters the Krebs cycle in the matrix.
– A carboxyl group is removed as CO2.
– A pair of electrons is
transferred from the
remaining two-carbon
fragments to NAD+ to form
NADH.
– The oxidized fragment,
acetate, combines with
coenzyme A to form
acetyl-CoA.
2. The Krebs cycle completes the energy-yielding
oxidation of organic molecules (in mitochondrial matrix)
It is the process of producing some of the remaining energy (ATP)
from the Pyruvate molecules. It occurs mainly in mitochondrial
matrix if oxygen is present.
It is the main source for preparing most of the cellular NADH (storing
energy molecule), and for producing some more of the cellular ATP.
It includes two cycles :
Pyruvate is converted into acetyle-CoA in the
presence of O2 through 3 steps.
-
a)- C=O group of pyruvate is released as CO2.
e-
b)- The remaining two-C fragments are oxidized (releasing ) into
- transform NAD+ into NADH.
acetate and the resultinge
c)- The coenzyme-A (CoA) transform acetate compound into
acetyle-CoA, which will be ready for Krebs Cycle for further
oxidation.
2 NAD+ 2 NADH + H+
+ CO2 + H2O
CoA
Krebs Cycle
It has eight steps starting with 2 acetyle-
CoA compunds. They are summarized as
shown in the figure: Pre-Krebs
Cycle
• This cycle begins when acetate from each acetyl-
CoA combines with oxaloacetate (4 C atoms) to
form citrate (citric acid).
• Ultimately, the oxaloacetate is recycled and the
acetate is broken down to CO2.
• Each cycle produces one ATP by substrate-level
phosphorylation, three NADH, and one FADH2
(another electron carrier) per acetyl CoA.
Thus, the outcome of the two cycles is
(for the 2 Acetyle-CoA molecules):
2 ATP
6 NADH
Output
2 FADH2
Flavin Adenine Dinucleotide
2
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
Oxidative Phosphorylation and the Electron
Transport Chain
o Electron transport chain (The Pathway of Electron Transport).
o Chemiosmosis (the Oxidative Phosphorylation)
Fermentation and anaerobic respiration: enable
cells to produce ATP without the use of oxygen:
o Types of Fermentation.
o Comparing Fermentation (Anaerobic Respiration) with Aerobic
Respiration
The catabolism of various molecules from food
Only 4 of 38 ATP ultimately produced by respiration of glucose are
derived from substrate-level phosphorylation (2 from glycolysis and 2
from Krebs Cycle).
The vast majority of the ATP (90%) comes from the energy in the
electrons carried by NADH and FADH2.
The energy in these electrons is used in the electron transport
chain to power تدATP synthesis.
Thousands of copies of the electron
transport chain are found in the extensive
surface of the cristae (the inner membrane of
the mitochondrion).
Electrons drop in free energy as they pass
down the electron transport chain.
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
Electrons carried by NADH are transferred to
the first molecule in the electron transport
chain (the flavoprotein; FMN).
The electrons continue along the chain which
includes several Cytochrome proteins and
one lipid carrier.
The electrons carried by FADH2 have
lower free energy and are added to
a later point in the chain.
Electrons from NADH or FADH2 ultimately
pass to oxygen.
The electron transport chain generates no
ATP directly. Rather, its function is to break
the large free energy drop from food to Fig. 9.13
oxygen into a series of smaller steps that
release energy in manageable amounts 5
ات ا.
ATP-synthase, in the cristae actually makes ATP from ADP and Pi.
ATP used the energy of an existing proton gradient to power ATP synthesis.
This proton gradient develops between
the inter-membrane space and the matrix.
This concentration of H+ is the
proton-motive force.
The ATP synthase molecules are the only
place that will allow H+ to diffuse back to
the matrix (exergonic flow of H+).
This flow of H+ is used by the enzyme to
generate ATP in a process called
“Chemiosmosis”.
Chemiosmosis: (osmos = puch)
It is the oxidative phosphorelation that
results in ATP production in the inner 6
membrane of mitochondria.
Energy carried by NADH and FADH2 give a maximum yield
of 34 ATP is produced by oxidative phosphorylation.
7
Video: plays in LMS
During respiration, most energy flows from glucose NADH
electron transport chain proton-motive force ATP.
Some ATP is produced by substrate-level phosphorylation
during glycolysis and the Krebs cycle, but most ATP comes from
oxidative phosphorylation (through electron transport chain).
Energy produced in Glycolysis and Krebs cycle gives a
maximum yield of 4 ATP by substrate-level phosphorylation.
Energy produced in electron transport chain gives a maximum
yield of 34 ATP by oxidative phosphorylation via ATP-synthase.
Substrate-level phosphorylation and oxidative phosphorylation
give a bottom line of 38 ATP.
- Glycolysis occurs in the cytosol and breaks glucose into two pyruvates
- Krebs Cycle takes place within the mitochondrial matrix, and breaks
a pyruvate into CO2 and produce some ATP and NADH.
- Some steps of Glycolysis and Krebs Cycle are Redox in which
dehydrogenase enzyme reduces NAD+ into NADH.
- Some of ATP is produced at these two steps via (substrate-level-
phosphorylation).
- Electron Transport Chain accepts e- from NADH and passes these e-
from one protein molecule to another.
- At the end of the chain, e- combine with both H+ and O2 to form H2O
and release energy.
- These energy are used by mitochondria to synthesis 90% of the cellular
ATP via ATP-synthase, a process called Oxidative Phosphorylation, in
the inner membrane of mitochondria.
Video: plays in LMS
Chemiosmosis: a process via which oxidative phosphorylation
takes place at the end of the Electron Transport Chain to produce
90% of ATP via ATP-synthase.
Or, is the process in which ATP synthesis powered by the flow of H+
back across ATP synthase.
ATP-synthase: an enzyme presents in the inner mitochondrial
membrane and used in making ATP by using H+ (protons).
NAD+: Nicotinamide adenine dinucleotide, which is a co-enzyme
that helps electron transfer during redox reactions in cellular
respiration.
FAD: Flavin adenine dinucleotide, which is an electron acceptor
that helps electron transfer during Krebs Cycle and Electron
Transport Chain in cellular respiration.
Oxidation refers to the loss of electrons to any electron acceptor, not
just to oxygen.
In glycolysis, glucose is oxidized to 2 pyruvate molecules with NAD+ as the
oxidizing agent (not O2).
Some energy from this oxidation produce 2 ATP.
If oxygen is present, additional ATP can be generated when NADH delivers its
electrons to the electron transport chain.
Glycolysis generates 2 ATP when oxygen is absent (anaerobic ا ).
Anaerobic catabolism of sugars can occur by fermentation.
Fermentation can generate ATP from glucose by substrate-level
phosphorylation as long as there is a supply of NAD + (the oxidizing
agent) to accept electrons.
If the NAD+ pool is exhausted إ ـتـ ُ ـِذ, glycolysis shuts down.
Under aerobic واconditions, NADH transfers its electrons to the electron
transfer chain, recycling NAD+.
Under anaerobic conditions, various fermentation pathways generate
ATP by glycolysis and recycle NAD+ by transferring electrons from
NADH to pyruvate.
Alcohol fermentation:
the pyruvate is converted to ethanol in two steps.
First, pyruvate is converted to acetaldehyde
by the removal of CO2.
Second, acetaldehyde is reduced by NADH
to ethanol.
Alcohol fermentation by yeast is used in
wine-making.
Lactic acid fermentation:
the pyruvate is reduced directly by NADH to form
lactate (ionized form of lactic acid).
Lactic acid fermentation by some fungi and
bacteria is used to make cheese and yogurt.
Muscle cells switch from aerobic respiration
to lactic acid fermentation to generate ATP
when lack of O2 (O2 is scarce ) ادر
The waste product, lactate, may cause
muscle fatigue, but ultimately it is 15
converted back to pyruvate in the liver.
Examples of anaerobic respiration:
A)- During exercise our bodies require a lot of energy
The body can only supply a limited amount of oxygen for
cellular respiration.
Energy is not produced at the rate required.
Cells will use anaerobic respiration to release extra energy
This produces lactic acid (a waste product).
B)- We use yeast to make bread
CO2 produced causes bread to rise by creating air pockets
The ethanol (alcohol) produced is evaporating during baking
A. Fats
have more energy per gram than
carbohydrates or proteins.
fatty acid chains are oxidized and broken
into smaller 2 carbon chains.
the 2 carbon chains are converted into
acetyl CoA to enter the Kreb’s cycle.
B. Proteins
must be converted into individual amino
acids.
excess amino acids are converted by
enzymes into intermediated of glycolysis
and Krebs cycle.
amino acids go through deamination
(amino groups are removed)
nitrogenous wastes from the amino
groups are released as wastes.
new compounds enter glycolysis or
Krebs.
Some organisms (facultative Proteins and fats, can also enter the
anaerobes ا ا ت ار ا )ا, respiratory pathways, including
including yeast and many bacteria, glycolysis and the Krebs cycle, like
can survive using either carbohydrates.
fermentation or respiration.
At a cellular level, human muscle
cells can behave as facultative
anaerobes, but nerve cells cannot.
1
2
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
The Key Roles of Cell Division: Introduction
• Cell division distributes identical sets of chromosomes
to daughter cells.
– Cellular Organization of the Genetic Material.
– Distribution of Chromosomes During Eukaryotic Cell Division
• The mitotic phase (M) alternates with interphase in the
cell cycle
– Phases of the Cell Cycle
• The continuity of life from one cell to another
is based on the reproduction of cells via cell
division.
• This division process occurs as part of the
cell cycle (the life of a cell from its origin in the
division of a parent cell until its own division into
two).
• The division of a unicellular ح د الorganism
(e.g. Amoeba) reproduces an entire organism,
increasing the population.
• Cell division is also central to the
development of a multicellular د د ال ا
organism that begins as a fertilized egg or
zygote.
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
Introduction
Multicellular organisms also use cell
division to repair and renew cells that
die normally or by accidents (blood cells
from bone marrow).
Cell division distributes the genetic
material (DNA) to two daughter cells.
Division is different among cells:.
- Skin cells divide frequently.
- Liver cells divide when needed (damage repair).
- Nerve cells and muscle cells never divide.
• A cell s genetic information (genome )ال ك الـis packaged as DNA.
• In prokaryotes, the genome is often a single long DNA molecule.
– In eukaryotes, the genome consists of several DNA molecules.
• A human cell must duplicate about 3m of DNA and separate the two
copies such that each daughter cell ends up with a complete
genome.
• DNA molecules are packaged into chromosomes.
– Every eukaryotic species has a characteristic
number of chromosomes in the nucleus.
– Human somatic cells (body cells) have
46 chromosomes.
– Human gametes ( أ اجsperm or eggs) have
23 chromosomes, half the number in
a somatic cell الج د ال.
• Each eukaryotic chromosome consists
mainly of a long, linear DNA molecule. 6
• Each chromosome has hundreds or thousands
of genes (the units that specify an organism s
inherited characters )الص ات ال را.
• This DNA-protein complex (chromatin) is
organized into a long thin fiber.
• After the DNA duplication, chromatin
condenses to form (chromosome).
• Each duplicated chromosome consists of two
sister chromatids which contain identical
copies of the chromosome s DNA.
• The narrow region where the chromosomal
strands connect is the called centromere.
• Later, the sister chromatids are pulled apart and
repackaged into two new nuclei at opposite
ends of the parent cell during cell division.
• The process of the formation of the two
daughter nuclei is called (mitosis) and is
usually followed by division of the cytoplasm
(cytokinesis ) ا طار ال. It occurs in somatic
cells ال ا الج د.
Chromatid
Chromatin
(DNA + Protein )
Sister chromatids
Centromere
• The mitotic (M) phase of the cell cycle alternates تت ادلwith the much longer
interphase ال رح ال.
– The M phase includes mitosis and
cytokinesis ا طار ال.
– Interphase accounts for 90% of the
cell cycle.
• During interphase the cell prepares for
division by producing cytoplasmic
organelles and copying its chromosomes.
A.Interphase has three sub-phases:
1. The G1 phase (“first gap”): cell is carrying out its everyday activities.
2. The S phase (“synthesis”): genetic material replicates itself, which allows
the cell to contain enough material for 2 cells upon division
3. The G2 phase (“second gap”): cellular organelles are produced to allow for
an adequate amount for the new cell being produced.
B. Division phase (M). The cell starts the division process.
The resulting daughter cells may then repeat the cycle again.
Usually includes five sub-phases راحل ر :
Prophase, الت د
Prometaphase, ت ا لا
Metaphase, ا ت ا
Anaphase, ا صال
Telophase. ا تا
• By late interphase (G2), the
chromosomes have been
duplicated تضا تbut are
loosely packed.
• The centrosomes have been
duplicated and begin to
organize microtubules into
11
an aster (“star”).
1) Prophase, الت دthe chromosomes are
tightly coiled, with sister chromatids joined
together, The nucleoli disappear. The mitotic
spindle begins to form and appears to push
the centrosomes away from each other
towards opposite ends (poles) of the cell.
2) Prometaphase, ل ا ت ا the nuclear
envelope fragments and microtubules from
one pole attach to one of two kinetochores
(special regions of the centromere) while
microtubules from the other pole attach to
the other kinetochore.
3) Metaphase, ا ت اthe spindle fibers push
the sister chromatids until they are all
arranged at the imaginary plane equidistant
between the poles, defining metaphase.
12
• Anaphase, ا صالthe centromeres
divide, result in separating the sister
chromatids. Each is then pulled toward
the pole to which it is attached by
spindle fibers. By the end, the two
poles have equivalent collections of
chromosomes.
• Telophase, ا ت اthe cell continues to
elongate as free spindle fibers from
each centrosome push off each other.
1) Two nuclei begin to form, surrounded by
the fragments of the parent s nuclear
envelope.
2) Chromatin becomes less tightly coiled.
3) Cytokinesis, begins as the division of
the cytoplasm occurs.
13
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It is the division of the cytoplasm
• Cytokinesis typically follows
mitosis.
• Contraction إ اضof the cell
pinches the cell into two new cells
17
18
Mitosis Cytokinesis
G1 S G2
Prophase Prometaphase Metaphase Anaphase Telophase
ال د ا لا ا ا ال ا ا ا
What are type of cells that divide?
They are somatic cells (body cells)
How many cells are produced and are they similar?
Produces 2 genetically identical cells
What abbreviation and name describes the fact that they contain 2
sets of chromosomes?
form diploid (2n) cell
Does the division reduce the number of chromosomes or maintain
the same number?
Maintains the same number of chromosomes in each daughter cell
How many cell divisions are there?
1 cell division
How many steps are there in mitosis?
5 steps
Genes: The units that specify an organism s inherited characters.
Chromatin: A DNA-protein complex which is organized into a long
thin fiber
Chromosome: The package that is formed from a condensed, coiled
and folded chromatin.
Chromatids: Two sister arms (chromatids) formed from each duplicated
chromosome. They contain identical copies of the chromosome s DNA
Centromere: The narrow region at which the chromosomal strands
(Chromatids) are connected together.
Mitosis: Is the division process which forms two daughter nuclei
Cytokinesis: طار ال اIs the division stage of the cytoplasm which
usually follows mitosis.
2
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
The Role of Meiosis in Sexual Life Cycles.
– Fertilization and Meiosis alternate in sexual life cycles.
• Sets of Chromosomes in Human Cells.
• Behavior of Chromosome Sets in the Human Life Cycle.
– Meiosis reduces the number of chromosome sets
from diploid to haploid (Reduction Division).
• The Stages of Meiosis.
• Crossing Over and Synapsis During Prophase-I.
– A Comparison of Mitosis and Meiosis.
A life cycle of an organism is the generation-to-generation
sequence of stages in its reproductive history.
It starts at the conception of an organism until it produces its own
offspring.
In humans, each somatic cell (all cells other than sperm or ovum) has
46 chromosomes.
The homologous chromosome pairs carry genes that control the
same inherited characters.
A karyotype ا ط ا رis a display of the 46 chromosomes
shows 23 pairs of chromosomes, each pair with the same length,
centromere position, and staining pattern.
It is a display of an individual’s chromosomes those are
arranged according to sizes and shapes
5
• An exception to the rule of homologous chromosomes is found in
the sex chromosomes (X and Y chromosomes).
• The pattern of inheritance of these chromosomes determine an
individual’s sex.
– Human females have a homologous pair of X chromosomes (XX).
– Human males have an X and a Y chromosome (XY).
• The other 22 pairs are called autosomes.
• We inherit one chromosome of each homologous pair from each
parent.
– The 46 chromosomes in a somatic cell can be viewed as two sets of 23
(a maternal set or a paternal set).
• Sperm cells or ova (gametes) have only one set of chromosomes -
22 autosomes and an X or a Y.
• A cell with a single chromosome set is called haploid.
– For humans, the haploid number of chromosomes is 23 (n = 23).
• A haploid sperm reaches and fuses with a haploid ovum.
• These cells fuse (Syngamy) resulting in fertilization.
• The fertilized egg (Zygote) now has a diploid set of chromosomes
from the maternal and paternal family lines.
• The zygote and all cells with two sets of chromosomes are diploid
cells 46 (2n = 46).
• As an organism develops from a zygote to a sexually mature adult,
the zygote’s genes are passes on to all somatic cells by mitosis.
• Gametes, which develop in the gonads, are not produced by mitosis.
• Instead, gametes undergo the process of meiosis in which the
chromosome number is halved.
• In the gonads ا ا ل, cells undergo a meiotic division, which yields
four daughter cells, each with half the chromosomes’ number of the
parent cell.
– In humans, meiosis reduces the number of chromosomes from 46 to 23.
• Each of us inherited 23 chromosomes from each parent: one set in
an egg and one set in a sperm during meiosis.
• Gametes ( ا اجeggs or sperms) are produced only in gonads ال ا ل
(ovaries or testes).
• Fertilization fuses two gametes together and doubles the number of
chromosomes to 46 again.
• The fertilized egg undergoes trillions of cycles of mitosis and
cytokinesis to produce a fully developed multicellular human.
• Fertilization restores the diploid condition by combining two haploid sets of
chromosomes.
• Fertilization and meiosis alternate in sexual life cycles.
Gametes, produced by meiosis, are
the only haploid cells.
Gametes undergo no divisions
themselves, but fuse to form a diploid
zygote that divides by mitosis to
produce a multicellular organism
Many steps of meiosis resemble steps in mitosis.
Both are preceded by the replication of
chromosomes.
However, in meiosis, chromosomes replicate
once followed by two consecutive cell divisions,
meiosis I and meiosis II, which results in four
daughter cells.
Each final daughter cell has only half
chromosomes number (haploid).
Meiosis reduces chromosome number by
copying the chromosomes once, but dividing
twice.
The first division (meiosis I) separates homologous
chromosomes.
The second (meiosis II) separates sister 10
chromatids.
1)- interphase the chromosomes are
replicated to form sister chromatids.
2)- Prophase I, the chromosomes condense and
homologous chromosomes pair up to form tetrads.
• Homologous chromosomes attached together
(synapsis).
– Chromatids of homologous chromosomes are
crossed (at chiasmata) and segments of the
chromosomes are exchanged (Crossing Over).
3)- Metaphase I, the tetrads are all arranged at the metaphase plate.
– Microtubules from one pole are attached to the kinetochore of one
chromosome of each tetrad, while those from the other pole are
attached to the other.
4)- Anaphase I,
the homologous
chromosomes separate
and are pulled toward
opposite poles.
5)- Telophase I, movement of homologous
chromosomes continues until there is a
haploid set at each pole.
– Each chromosome consists of linked sister
chromatids.
• Cytokinesis follows
1) Prophase II, a spindle apparatus forms, attaches to kinetochores of
each sister chromatids, and moves them around.
2)- Metaphase II, the sister chromatids are arranged at the metaphase plate.
3)- Anaphase II, the centromeres of sister chromatids separate and the
separated sister chromatids travel toward opposite poles.
14
4)- Telophase II, separated sister
chromatids arrive at opposite poles.
– Nuclei are formed around the
chromatids.
• Cytokinesis separates the
cytoplasm.
• At the end of meiosis, there are four
haploid daughter cells.
Meiosis Division (Reduction Division)
Occurs in two steps
A)- Meiosis I B)- Meiosis II
- Separate homologous - No further replication of
chromosomes. chromosomes.
-Occurs in the newly resulting
- Results in 2 cells with replicated
cells from Meiosis I.
chromosomes.
(4 haploid cells)
It occurs mainly in sex gonads to form Gametes (sperms and ova)
Each of the resulting cells has half number of chromosomes of the
original cell (23 in human). Thus, it is called Reduction Division
Chiasma
Recombinant Chromosomes
• Occurs during prophase I.
• The two homologous chromosomes joint together
very closely.
• Two non-sister chromatids of the homologous
chromosomes are crossed over at a chiasma point
and exchange corresponding segments.
• The resulting chromosomes are called “recombinant
chromosomes”.
• It is important in genetic variation in sexual life cycle.
• Three mechanisms contribute to genetic variation:
1) independent assortment
2) crossing over
3) random fertilization
1)- Independent assortment: of chromosomes contributes to
genetic variability due to the random orientation of tetrads at the
metaphase plate.
– There is a fifty-fifty chance
that a particular daughter cell
of meiosis I will get the maternal
chromosome of a
certain homologous
pair and a fifty-fifty
chance that it will
receive the paternal
chromosome.
19
• Independent assortment alone would
find each individual chromosome in a
gamete that would be exclusively
maternal or paternal in origin.
3)- Crossing over:
Homologous portions of two non-
sister chromatids exchange places,
producing recombinant
chromosomes which combine genes
inherited from each parent.
2- The random fertilization: it adds to
the genetic variation arising from
meiosis.
• Any sperm can fuse with any egg.
20
21
• The chromosomes number is reduced by half in meiosis, but not
in mitosis.
– Mitosis produces daughter cells that are genetically identical to the
parent and to each other.
– Meiosis produces cells that differ from the parent and each other.
• Three events, unique to meiosis, occur during the first division
cycle.
1. During prophase I, homologous chromosomes pair up in a
process called synapsis.
– Later in prophase I, the joined homologous chromosomes are visible as
a tetrad.
– At X-shaped regions called chiasmata, sections of non-sister chromatids
are exchanged.
– Chiasmata is the physical manifestation of crossing over, a form of
genetic rearrangement.
2. At metaphase I homologous pairs of chromosomes, not
individual chromosomes are aligned along the metaphase
plate.
• In humans, you would see 23 tetrads.
3. At anaphase I, it is homologous chromosomes, not
sister chromatids, that separate and are carried to
opposite poles of the cell.
– Sister chromatids remain attached at the centromere until
anaphase II.
• The processes during the second meiotic division are
virtually identical to those of mitosis.
Comparison between Mitosis and meiosis
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
In April 1953, James Watson and Francis Crick shook the scientific world
with an elegant double-helical model ا زد ج ا زج ا ح زfor the structure of
deoxyribonucleic acid or DNA.
Watson and Crick began to work on a model of DNA with two strands, the
double helix ا زد ج ا ح ز.
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
• The amino acid sequence of a polypeptide is programmed by a gene.
• A gene is a small region in the DNA.
• Nucleic acids store and transmit hereditary information ات ا راث ا ع.
• There are two types of nucleic acids: ribonucleic acid (RNA) and
deoxyribonucleic acid (DNA).
• DNA also directs mRNA synthesis, thus, controls protein synthesis.
• Organisms inherit تت ارثDNA from their parents.
– Each DNA molecule is very long and usually consists of hundreds to
thousands of genes.
– When a cell divides ت, its DNA is copied and passed to the next
generation of cells.
• The mRNA interacts with ribosomes to direct the synthesis of amino
acids in a polypeptide (protein)
3 o5 Bases
o P o
o DNA
Basenucleotide Adenine
Phosphate
group
5 CH2 o (A) Purine
4 H H 1
H H Guanine
3 2H
(G)
o Deoxyribose
o P o
o
Base Cytosine
CH2 o (C) Pyrimidine
H H
H
3 H Thymine
5 3 H
(T)
Sugar-phosphate backbone
• The PO43- group of
one nucleotide is
attached to the sugar
of the next nucleotide
in line م ف ف.
• The result is a
“backbone of
alternating تباد
phosphates and
sugars, from which
the bases starts.
3 5
Hydrogen bonds
Cytosine Guanine
Nitrogenous bases
(C) (G)
Thymine Adenine
(T) (A)
Uracil (U)
Pyrimidines Purine
5 3
Sugar-phosphate
backbones
• Adenine (A) would
form 2 hydrogen bonds
only with thymine (T)
• Guanine (G) would form 3
hydrogen bonds only with
cytosine (C).
CH2 o CH2 o
H H
H H H
H H
H H
OH
Deoxyribose sugar Ribose sugar
(O on C2 is missed) (no missed O)
Deoxiribo-Nucleic-Acid Ribo-Nucleic-Acid
Double stranded nucleic acid Single stranded nucleic acid
Bases: A, G, C, T Bases: A, G, C, U
• Nucleic acids are polymers of monomers called nucleotides.
• Each nucleotide consists of three parts: a nitrogen base, a pentose
sugar, and a phosphate group.
• The nitrogen bases (rings of carbon and nitrogen) come in two types:
Purines and Pyrimidines.
• The pentose sugar joined to the nitrogen base is ribose in
nucleotides of RNA and deoxyribose in DNA.
• The only difference between the sugars is the lack صof an oxygen
atom on carbon 2 in deoxyribose.
• Polynucleotides are synthesized by connecting the
sugars of one nucleotide to the phosphate of the next
with a phosphodiester link.
• This creates a repeating backbone of sugar-phosphate
units with the nitrogen bases as appendages.
• The sequence of nitrogen bases along a DNA or mRNA
polymer is unique for each gene.
• Genes are normally hundreds to thousands of
nucleotides long.
• The linear order ا ترت ب ا تتابعof bases in a gene specifies
ُحددthe order of amino acids ( ترت ب ا ح اض اthe monomers of a
protein).
• The flow of genetic information is from DNA
mRNA protein.
– Protein synthesis occurs
in ribosomes.
– In eukaryotes, DNA is
located in the nucleus,
but most ribosomes are
in the cytoplasm with
mRNA as an
intermediary ط.
• An RNA molecule is a single polynucleotide chain (single strand).
• DNA molecules have two polynucleotide strands (double strand)
that spiral around تد ر ح ز اto form a double helix ح ز زد ج.
• The sugar-phosphate
backbones of the two
polynucleotides are on
the outside of the helix.
• Pairs of nitrogenous
bases (one from each
strand) connect the
polynucleotide chains
with hydrogen bonds.
• Most DNA molecules
have thousands to
millions of base pairs
( ز ج ا اعدbP).
• Because of their shapes, only some bases are compatible ت اwith
each other.
– Adenine (A) always pairs with thymine (T) and guanine (G) with
cytosine (C).
• With these base-pairing rules, if we know the sequence of bases on
one strand, we know the sequence on the opposite ا ابstrand.
• The two strands are complementary بعض ا .
• During preparations for cell division each of the strands serves as
a template ا بto order nucleotides into a new complementary
strand.
• This results in two identical copies ت طب ا ص of the original
double-stranded DNA molecule.
– The copies are then distributed ت زعto the daughter cells.
• This mechanism ensures that the genetic information is
transmitted to the new cells.
DNA A G C T A T C
mRNA T
U C G A T
U A G
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
DNA Replication.
Three different models of DNA replication.
DNA Replication: A Closer Look.
During DNA replication, base pairing enables
existing DNA strands to serve as templates for
new complimentary strands.
A large team of enzymes and other proteins carry
out DNA replication:
o The Replication Mechanism.
When a cell copies a DNA molecule, each strand serves as a
template ذجfor ordering nucleotides into a new complimentary
strand ِّ ُ ا جا ب ا.
Nucleotides line up ـ َ ـَراصalong the template strand according to
the base-pairing rules.
The nucleotides are linked to form new strands (complementary).
4
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
Semiconservative replication (the most common and accepted by
Watson and Crick). The double helix replicates each of the daughter
molecules and will have one old strand and one newly made strand.
The other two models are the conservative and the dispersive models
5
1. During DNA replication, base pairing إزد اج ا ا دenables
existing DNA strands to serve as templates ا ب/ذج for
new complimentary strands ِّ ُ ا جا ب ا
2. Several enzymes and other proteins carry out DNA
replication:
Helicase,
Primase,
Polymerase,
Ligase.
The ends of DNA molecules are replicated by a special
mechanism.
A large team of enzymes and other proteins carries
out DNA replication: The Replication Mechanism
It takes E. coli less than an hour to copy each of the 5 million
base pairs in its single chromosome and divide to form two
identical daughter cells.
A human cell can copy its 6 billion base pairs and divide into
daughter cells in only a few hours.
This process is remarkably accurate, with only one error per
billion nucleotides.
A helicase; untwists َ ا اand separates the template
DNA strands at the replication fork.
Single-strand binding proteins; keep the unpaired
template strands apart ص during replication.
The replication of a DNA molecule begins at a special site called
origin of replication ـ ا اwhich is a single specific sequence
of nucleotides that is recognized by the replication enzymes.
Replication enzymes separate the strands, forming a replication
bubble ةا ا.
Replication proceeds in both directions until the entire
molecule is copied.
In eukaryotes, there may be
hundreds or thousands of bubbles
(each has origin sites for replication) per
chromosome.
At the origin sites, the DNA
strands separate forming a
replication bubble with
replication forks ة ا س at each
end.
The replication bubbles elongate
س طas the DNA is replicated and
eventually fuse ا دج ب.
Primase: (an RNA polymerase)
links complementary
ribonucleotides to the DNA
template. The primer, which is a
short segment of RNA ( 10
nucleotides long) is required to
start a new chain.
DNA polymerases: catalyze the
elongation of new DNA at a
replication fork. After formation
of the primer, DNA polymerases
can add deoxyribonucleotides to
the 3 end of the ribonucleotide
chain.
Another DNA polymerase later
replaces the primer
ribonucleotides with
deoxyribonucleotides
complimentary to the template.
9
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DNA polymerases can only add
n cleo ide o he f ee 3 end of a g o ing
DNA strand.
A new DNA strand can only elongate in the
5 ->3 di ec ion.
At the replication fork, one parental strand
(3 -> 5 in o he fo k), the leading strand,
can be used by polymerases as a template
for a continuous complimentary strand.
The other parental strand (5 ->3 into
the fork), the lagging strand, is copied
away from the fork in short segments
(Okazaki fragments ) ـِّطـ َ ص رة.
Okazaki fragments (each about 100-
200 nucleotides) are joined by DNA
ligase ا ز ا رابطto form the sugar-
phosphate backbone of a single DNA 11
strand.
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Step 1
Helicases: Enzymes that separate the DNA strands
Helicase move along the strands and breaks the hydrogen bonds
between the complimentary nitrogen bases
Replication Fork: the Y shaped region that results from the separation
of the strands
Step 2
DNA Polymerase: enzymes that add complimentary nucleotides.
Nucleotides are found floating freely inside the nucleus
Covalent bonds form between the phosphate group of one nucleotide
and the deoxyribose of another
Hydrogen bonds form between the complimentary nitrogen bases
Step 3
DNA polymerases finish replicating the DNA and fall off.
The result is two identical DNA molecules that are ready to move to new
cells in cell division.
Semi-Conservative Replication: this type of replication where one strand
is from the original molecule and the other strand is new
Each strand is making its own new strand.
DNA synthesis is occurring in two different directions
One strand is being made towards the replication fork
and the other is being made away from the fork. The
strand being made away from the fork has gaps.
Gaps are later joined by another enzyme, DNA ligase
The strands in the double helix are anti-parallel
ا جا اد از.
The sugar-phosphate backbones run in
opposite directions.
Each DNA strand has a 3 end with a free OH
group attached to deoxyribose and a 5 end with a
free phosphate group attached to
deoxyribose.
The 5 -> 3 direction of one strand runs counter
to ُ ا س ـthe 3 -> 5 direction of the other strand.
The two DNA-strands separate forming replication bubbles.
Each strand functions as a template for synthesizing new
complementary & lagging strands via primers, polymerase and ligase.
5 3
T A C T G A C
A G A G
T C T Primer
3 Complementary
5
Polymerase Templates
(leading) strand
Ligase
T A C T G A C
3 5
Lagging strand Okazaki
(complementary) fragments
1
2
ا ـَـــ ْء
3
ا ا
4
16
Fig. 16.15, Page 298
Helicase: untwists the double helix to separate the DNA strands by forming
replication bubbles.
Replication enzymes: separates DNA strands, forming a replication bubble .
Replication bubble: formed at the origin sites of replication as DNA strands
separate, and hence, replication forks formed at each end.
Replication site: it is also called origin of replication which is a single specific
sequence of nucleotides that is recognized by the replication enzymes
and at which replication starts.
Primer: is a short piece of RNA (10 nucleotide long) which is synthesised
by primase and used to initiate the leading strands of the new DNA.
DNA-polymerase: builds up the new DNA strand by adding nucleotides to
the primer (from 5 to 3 end).
Leading strand: the elongation strand (5 3 into the fork) that initiate the
new DNA after recognizing the sequence of the primer by special proteins.
Lagging strand: Is the other parental strand (5 3 into the fork), is copied
away from the fork in short segments (Okazaki fragments).
Okazaki fragments: the newly formed segments (5 3 , away from the fork)
then, form the lagging strand when connected by ligase towards the fork.
DNA-ligase: joins the Okazaki fragments of the newly formed bases to form
the new lagging DNA strand.
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
• Types of RNAs.
• mRNA transcription and translation are the two main
processes that link gene to protein.
• Transcription is the DNA-directed synthesis of mRNA:
– Synthesis of mRNA Transcript.
• RNA Polymerase Binding and Initiation of Transcription.
• Elongation of the mRNA Strand.
• Termination of Transcription
• The genetic codes (nucleotide triplets) specify the
amino acids.
• Eukaryotic cells modify mRNA after transcription.
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
RNA transcription إ خand translation تر ةare the two
main processes that link gene to protein
• The information content of DNA is in the form of specific sequences
of nucleotides along the DNA strands.
• The DNA inherited by an organism leads to specific traits by
dictating the synthesis of proteins.
• Proteins are the links between genotype and phenotype.
– For example, Mendel’s dwarf pea plants lack a functioning copy of the
gene that specifies the synthesis of gibberellins (which stimulate the
normal elongation of stems).
• Genes provide the instructions for making specific proteins.
• The bridge between DNA and protein synthesis is RNA.
• The specific sequence of hundreds or thousands of nucleotides in
each gene carries the information for the primary structure of a
protein, the linear order of the 20 possible amino acids.
• During RNA transcription خ ا, a DNA strand provides a template
for the synthesis of a complementary RNA strand.
• Transcription of a gene produces a messenger RNA (mRNA)
molecule.
• During mRNA translation ( التر ةat ribosomes), the information
contained in the order of nucleotides in mRNA is used to determine
تـُحددthe amino acid sequence ترت بof a polypeptide.
• The basic mechanisms of RNA transcription and translation are
similar in eukaryotes and prokaryotes, while the process of RNA
transcription and translation are not similar as following:
a) In prokaryotes:
They lack nuclei, thus transcription and
translation are coupled ـُت ز ا.
Translation of mRNA by the ribosome
starts while the transcription is still
in progress.
b) While In a eukaryotes:
All mRNA transcription occurs within the
nucleus, while the translation occurs
mainly by ribosomes in the cytoplasm.
In addition, the primary mRNA is
modified in various ways during mRNA
processing ت زbefore it leaves to the
cytoplasm.
• In conclusion: genes program (control)
protein synthesis via genetic mRNA.
Transcription Translation
DNA mRNA Protein
8
• Triplets ة ات of nucleotide bases are the smallest units that can code
for all amino acids.
• In the triplet code three consecutive تتالbases specify تحددan amino acid.
• The genetic instructions for a polypeptide
chain are written in DNA as a series of
three-nucleotidewords (triplets).
• During transcription, one DNA strand
(the template strand) provides an
mRNA template.
• The complementary mRNA molecule
is synthesized according to
base-pairing rules, except that
uracil is the complementary base
to adenine.
• During translation, blocks
of three nucleotide bases (codons ) رة,
(ة ال ا د ة )ال رة بارةare
decoded ك ال رةinto a sequence تتاب
of amino acids.
• During translation, the codons are
read in the 5’->3’ direction along the
mRNA.
• The codon UUU coded for the amino
acid phenylalanine.
• The codon AUG not only codes for
the amino acid methionine but also
indicates the start of translation.
• A specific codon indicates a specific
corresponding amino acid, but the
amino acid may be the translation of
several possible codons.
• The reading frame and subsequent
codons are read in groups of three
nucleotide bases (codon).
• In summary, genetic information
is encoded as a sequence of
base triplets (codons) which is
translated into a specific amino
acid during protein synthesis.
• mRNA is transcribed خfrom the template strand of a gene.
• RNA polymerase separates the DNA strands at the suitable point and
bonds ربطthe RNA nucleotides as they base-pair along the DNA
template.
• Like DNA polymerases, RNA polymerases can add nucleotides only
to the 3’ end of the growing polymer.
• Specific sequences of nucleotides along the DNA mark where gene
transcription begins and ends.
– RNA polymerase attaches and initiates transcription at the promotor
ال ُ َح ـز, at the beginning of the transcription unit (gene) on the DNA.
– The terminator ط ة ال ا ةends the transcription.
• Bacteria have a single type of RNA polymerase that synthesizes all
RNA molecules.
• In contrast, eukaryotes have three RNA polymerases (I, II, and III) in
their nuclei.
– RNA polymerase II is used for mRNA synthesis.
• Transcription
can be separated
into three stages:
1- initiation ا دء
2- elongation ا ا,
3- termination اء ا.
• The promotor contains
the starting point for
the transcription of a
gene.
• The promotor also
includes a binding site
for RNA polymerase.
• Thus, RNA-
polymerase can
recognize and bind
directly to the
promotor region.
12
• As RNA polymerase moves along the DNA, it untwists the double
helix, 10 to 20 bases at a time.
• The enzyme adds
nucleotides to the
3’ end of the
growing strand.
• Behind the point
of RNA synthesis,
the double helix
re-forms and the
RNA molecule
moves away.
• Transcription proceeds
until after the RNA
polymerase transcribes
a terminator sequence
in the DNA.
B)- The Processing of mRNA:
Eukaryotic cells modify RNA after transcription
• Enzymes in the eukaryotic nucleus modify pre-mRNA before the
genetic messages are dispatched to the cytoplasm.
1. At the 5’ end of the pre-mRNA molecule, a modified form of
guanine is added, the 5’ cap which function as:
a) protect mRNA from hydrolytic ُ ح لenzymes.
b) a translation start point for ribosomes.
2. At the 3’ end, an enzyme adds 50 to 250 adenine
nucleotides, the poly(A) tail.
3. The poly(A) tail facilitates the export of mRNA from the nucleus.
1) Transcription begins when the enzyme RNA polymerase binds to DNA at
a promoter region.
2) The enzyme separates the DNA strands by breaking the hydrogen bonds,
and then uses one strand of DNA as a template from which nucleotides
are assembled into a strand of mRNA.
3) RNA polymerase pairs up free floating mRNA nucleotides with DNA
template and joins the nucleotides together to form the backbone of the
new mRNA strand.
4) When mRNA hits a termination sequence, it separates from the DNA.
5) mRNA editing occurs in the nucleus: before the mRNA leaves the
nucleus, it is called pre-mRNA and it gets “edited. Parts of the pre-
mRNA that are not involved in coding for proteins are called introns and
are cut out. The remaining mRNA pieces are called exons (because they
are expressed) and are spliced (combine) back together to form the
mRNA.
6) Then the final mRNA leaves the nucleus through the nuclear pores and
enters the cytoplasm headed to the ribosomes.
16
Bubble
3 5
T A C T G A C
C T C A TRNA UT G
A A CT UG G
A C A C T
C
polumerase
G A G A A T G A C T G T G A
A T G A C T G
Promoter
Ribosome
Protein
Codons (ة )الـ رة الـor triplet code: it is a block of three consecutive تتال
nucleotide bases that specify تحددa particular amino acid.
Start codon: a codon that specifies the start of mRNA translation.
Stop codon: a codon that specifies the end of mRNA translation.
RNA polymerases: RNA transcription enzyme that first separates the DNA
strands at the suitable point then start to add nucleotides to the 3’ end of the
growing RNA polymer until completed.
Transcription unit (the gene): a specific sequences of nucleotides along
the DNA that marks where mRNA transcription begins and ends.
Promotor ال ُ َح ـز: a specific short sequence on DNA at which RNA
polymerase attaches and initiates transcription at the beginning of the
transcription unit.
Terminator ط ة ال ا ة: a specific short sequence on DNA at which mRNA
transcription ends (the end of the gene).
2
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
• The Synthesis of Protein.
• Translation is the mRNA-directed synthesis of a polypeptide
Molecular Components of Translation.
• The Structure and Function of Transfer RNA (tRNA).
• Role of Ribosomes in protein synthesis .
Translation occurs in three stages:
1. initiation of translation
2. elongation of the polypeptide chain
3. termination of translation
Polyribosomes.
• Mutations
Point mutations
1. Base-pair substitution
2. Frame-shift mutation (Insertions and deletions)
• In the process of
translation, a cell sends a
series of codons along a
mRNA molecule.
• Transfer RNA (tRNA)( )ا ا
transfers amino acids
from the cytoplasm to a
ribosome.
• The ribosome adds each
amino acid carried by
tRNA to the growing end
of the polypeptide chain.
4
• During translation, each type of
tRNA links the mRNA codon with
the appropriate amino acid.
• Each tRNA arriving at the
ribosome carries a specific
amino acid at one end and has a
specific nucleotide triplet, an
anticodon, at the other end.
• The anticodon base-pairs with a
complementary codon on mRNA.
If the codon on mRNA is
UUU, a tRNA with an AAA
anticodon and carrying
phenyalanine will bind to it.
• Codon by codon, tRNAs
deposit amino acids in the
prescribed order and the
ribosome joins them into a
polypeptide chain.
5
• tRNA molecules: are transcribed
from DNA in the nucleus.
• Once it reaches the cytoplasm,
each tRNA is used repeatedly for
the following functions:-
1) to pick up its relevant amino acid
in the cytosol,
2) to deposit the amino acid at the
ribosome
3) to return to the cytosol to pick up
another copy of that amino acid.
• The anticodons ا رة ا ُ ا ةof some
tRNAs recognize more than one
codon.
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
• Ribosomes: the protein making machine
facilitate the coupling of the tRNA anticodons with
mRNA codons.
Each ribosome has a large and a small subunit formed in the
nucleolus.
The ribosome is composed of proteins and ribosomal RNA
(rRNA), the most abundant RNA in the cell.
• rRNA is transcribed in the nucleus, then bind to special
proteins to form the ribosomal subunits in the nucleolus.
• The subunits exit the nucleus via nuclear pores.
• The large and small subunits join to form a functional ribosome
only when they attach to an mRNA molecule.
Each ribosome has a binding site for mRNA and three
binding sites for tRNA molecules.
1) The Peptidyle (P) site holds the tRNA carrying the growing
polypeptide chain.
2) The Acceptor (A) site carries the tRNA with the next amino acid.
3) The Exit (E) site at which the discharged tRNA leave the
ribosome.
8
• Translation occurs in three stages:
1- initiation ا دءof translation
2- elongation ا طا ا اof the polypeptide chain
3- termination ا اof translation
1. Initiation:
brings together mRNA, a tRNA (with the first amino acid) and the two ribosomal
subunits (large & small).
First, a small ribosomal subunit binds with mRNA and a special initiator tRNA, which carries
methionine and attaches to the start codon.
Initiation factors bring in the large subunit such that the initiator tRNA occupies the P site.
Methionine
Guanosine
triphosphate
2. Elongation:
Consists of a series of three step cycles as each amino acid is added to
the proceeding one in 3 steps:-
a) Codon recognition ا رات ا ت رف, an elongation factor assists hydrogen
bonding between the mRNA codon under the A site with the
corresponding anticodon of tRNA carrying the appropriate ا ا بamino
acid [This step requires the hydrolysis of two guanosine triphosphate (GTP)].
b) Peptide bond formation: an rRNA molecule catalyzes the formation of
a peptide bond between the polypeptide in the P site with the new amino
acid in the A site. This step separates
the tRNA at the P site from the
growing polypeptide chain and
transfers the chain, now one
amino acid longer, to the tRNA
at the A site.
c) Translocation ت ر ا اof tRNA:
the ribosome moves the tRNA with
the attached polypeptide from
the A site to the P site.
3. Termination:
Occurs when one of the three stop codons reaches the A site.
• A release factor ا ُ ررbinds to the stop codon and hydrolyzes the bond
between the polypeptide and its tRNA in the P site.
• This frees the polypeptide and the translation complex disassembles ت.
Fig. 17.19
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• A ribosome requires less than a minute to translate an average-sized
mRNA into a polypeptide.
• Multiple ribosomes, polyribosomes, may trail along the same mRNA.
• Thus, a single mRNA is used to make many copies of a polypeptide
simultaneously.
1
1) mRNA attaches to a ribosome at the AUG, which is
the start codon. This begins translation.
2) The transfer RNA (tRNA) bonds with the correct
amino acid and becomes “charged. (in the
cytoplasm)
3) The tRNA carries the amino acid to the ribosome.
2
Each tRNA has an anticodon whose bases are
complementary to a codon on the mRNA strand.
The tRNA brings the correct amino acid to the
ribosome.
4) The ribosome moves along the mRNA and adds
more amino acids to the growing polypeptide or
protein
5) The process continues until the ribosome reaches
one of the three stop codons on the mRNA, and
then the ribosome falls off the mRNA.
6) The result is a polypeptide chain or protein that is 3
ready for use in the cell.
• Mutation is a change in the genetic material of a cell.
• These include large-scale mutations in which long segments of DNA are
affected (e.g., translocations, duplications, and inversions).
I.Point mutation ة ط رة:
is a chemical change in just one base pair of a gene.
• If these occur in cells producing gametes, they may be transmitted to future
generations (offspring).
For e.g., sickle-cell disease is
caused by a mutation of a
single base pair in the gene
that codes for one of the
polypeptides of hemoglobin.
A change in a single
nucleotide from T to A in the
DNA template leads to an
abnormal protein. 16
• It is a point mutation that results in
replacement of a pair of
complimentary nucleotides with
another nucleotide pair.
a) Silent mutation: some base-pair
substitutions (point mutation) have little
or no impact ت ر اon protein function
which lead to switches from one amino
acid to another with similar properties.
Other base-pair substitutions cause a
detectable change ظ ت رin a protein
which impacts ؤ رthe function.
b) Missense mutations: a point mutation
that still code for an amino acid but
change the resulting protein.
c) Nonsense mutations: change an amino
acid codon into a stop codon, nearly
always leading to a nonfunctional protein
17
ر ظ بر ت.
Frame-shift إزا mutation.
• It is a mutation in which
additions or losses of nucleotide
pairs occurs and causes a
Frame-Shift إزا ةMutation.
These have a disastrous ار
effect on the resulting protein
• When frame-shift occurs, all the
nucleotides downstream of the
deletion or insertion will be
improperly grouped into new
codons.
The result will be extensive
missense, ending sooner or later
in nonsense - premature
termination ف ب ر تر ة. 18
• Mutations can occur in a number of ways.
Errors can occur during DNA replication, DNA repair, or DNA recombination.
These can lead to base-pair substitutions, insertions, or deletions, as well as
mutations affecting longer stretches of DNA.
These are called spontaneous mutations.
• Mutagens ُ ـببات ا ط رات:
are chemical or physical agents that interact with ا DNA to cause
mutations.
1. Physical agents include high-energy radiation like X-rays and ultraviolet
light ة ا ة ف ا ب.
2. Chemical agents may operate in several ways.
Some chemicals are base analogues that may be substituted into DNA, but that
pair incorrectly during DNA replication.
Other mutagens interfere with DNA replication by inserting into DNA and
distorting the double helix.
Still others cause chemical changes in bases that change their pairing
properties.
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
G eg Mendel Di c e ie .
Mendel used the scientific approach to
identify two laws of inheritance:
The Law of Segregation.
Useful Genetic Terminology.
The Testcross.
3
Gregor Mendel (the father of
genetics), Czech geneticist 1822
1884.
Gregor Johann Mendel was born
on July 22, 1822, in what is now
Hyncice, Czech Republic. He
entered a monastery in what is
now Brno, Czech Republic, and
performed a famous and
important series of breeding
experiments while at the
monastery. Mendel died on
January 6, 1884, in Brno.
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
Around 1857, Mendel began breeding
garden peas to study inheritance راثة.
Because they are available in many
varieties with distinct heritable ُ ت ارث
characters اتwith different genes.
Each pea plant has male (stamens)
and female (carpel) sexual organs.
In nature, pea plants typically
self-fertilize ت ح ذات, (fertilizing ova with
their own pollens).
However, Mendel could also move
pollens حب ب ا احfrom one plant to
another to cross-pollinate ُـ حplants.
5
Mendel Re l and C ncl i n
Recessive and Dominant Traits
Mendel concluded that inherited characteristics
are controlled by factors that occur in pairs.
In his experiments on pea plants, he found that
one factor in a pair masked the other, Thus:
The trait that masked the other was called
the dominant trait.
The trait that was masked was called the
recessive trait.
In a breeding experiment, Mendel would cross-pollinate
( ت ح طhybridize ) َجtwo contrasting تبا, true-breeding
pea varieties أ اع.
The true-breeding parents are the P (Parental generation) and
their hybrid offspring ا ُ ج اare the F1 (1st Filial generation) .
Mendel would then allow the F1 (1st Filial generation) hybrids
to self-pollinate to produce an F2 generation.
It was mainly Mendel s quantitative analysis تحof F2
plants that revealed the two fundamental laws of
heredity:
A)- The law of segregation.
B)- The law of independent assortment.
Mendel expected that the F1 hybrids
from a cross ت حbetween purple-
flowered and white-flowered pea
plants would have pale purple flowers
ب ج با ت.
Instead, the F1 hybrids all have
purple flowers, just a purple like their
parents.
This cross produced a 3 purple to 1
white ratio of traits in the F2 offspring,
Mendel reasoned that the heritable
factor for white flowers was present
in the F1 plants, but it did not affect
flower color.
Thus, purple flower is a dominant color
) ( ة ا دةand white flower is a recessive
color )( ة ُ ت ح ة.
Focuses on only a single character via monohybrid crosses ة ا تزا ج أحاد ا
Mendel found similar 3 : 1 ratios of two traits among F2
offspring when he conducted crosses for six other
characters, each represented by two different varieties
ت ت ت .
For example, when Mendel crossed two true-breeding
varieties, one of which produced round seeds تد رة ُ بذ ر,
the other of which produced wrinkled seeds ُ َجعدة بذ ر, all
the F1 offspring had round seeds, but among the F2
plants, 75% of the seeds were round and 25% were
wrinkled (see second law in the next lecture).
11
Mendelian inheritance reflects rules of probability for the
behaviour of genes (alleles).
Alleles segregate تbecause of the distribution of homologous
chromosomes to different gametes in meiosis.
For each character, an organism inherit two alleles (one from each
parent).
Red colour
gene (allele)
Homologous
chromosomes
White colour
gene (allele)
If the two alleles differ, one of them will be Dominant, and the other
is Recessive.
The two alleles (genes) for a character are separated (segregated)
into separate gametes (summarized as Mendel s law of segregation)
and aggregated again by fertilization.
Mendel s law of segregation accounts
for the 3:1 ratio in the F2 generation.
The F1 hybrids will produce two
classes of gametes, half with the
purple-flower allele and half with the
white-flower allele.
During self-pollination, the gametes
of these two classes unite randomly.
This can produce four equally likely
combinations of sperm and ovum.
A Punnett square predicts the results
of a genetic cross between individuals
of known genotype ا طرز ا ـ.
A Punnett square analysis of the
flower-color example demonstrates
Mendel s model.
Mendel s model accounts for the 3:1
ratio in the F2 generation
PP X pp Pp X Pp
Heterozygous
Homozygous
P p P p
P p
Dominant
allele Pp Recessive
allele PP Pp Pp pp
100% Purple
3 Purple : 1 White
F1 generation F2 generation 14
Phenotype:
Is the organism s appearance ا طرز ا ظ ر.
(Colour)
Genotype:
Is the organism s genetic makeup
ا طرز ا ـ.
PP ت ا ل ال نات
An organism having a pair of
identical alleles
ت ا ن ال نات
(Genetic make up)
An organism having a pair of two
different alleles
15
For flower color in
peas, both PP and Pp
plants have the same
phenotype (purple) but
different genotypes
(homozygous and
heterozygous).
The only way to
produce a white
phenotype is to
be homozygous
recessive (pp)
for the flower-
color gene.
It is not possible to predict the
genotype of an organism with a
dominant phenotype.
The organism must have one
dominant allele, but it could be
homozygous dominant or
heterozygous.
Test cross:
is breeding a
homozygous recessive
with dominant phenotype,
but unknown genotype,
can determine the identity
of the unknown allele.
Q: What is the result of Cross
hybridization of purple X white
17
colored flowers ?
The Law of Segregation
The law of segregation states that a pair of factors is segregated, or
separated, during the formation of gametes.
Dominant character (allele) ال فة ال ا دة
Is fully expressed in the organism s appearance.
Recessive character (allele) ال فة ال ُ تن ة
Has no noticeable effect ت ر ر ل ظon the organism s appearance.
Homozygous ُ ت ا ل ال نات
An organism with two identical alleles for a character.
Heterozygous ُ تلف ال نات
An organism with two different alleles for a character.
Phenotype الطرز ال ظ ر
A description of an organism s traits (feature ) ظ ر.
Genotype الطرز ال ن
A description of an organism s genetic makeup.
Albinism
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
The Law of Independent Assortment.
Recessively Inherited Disorders.
• Cystic Fibrosis.
• Tay-Sachs disease.
• Sickle-Cell Disease.
Dominantly Inherited Disorders.
• Achondroplasia.
• Huntington s disease.
Multifactorial Disorders.
3
• Mendel s experiments that followed the inheritance of flower color or
other characters focused on only a single character via monohybrid
crosses ا تزا ج أحاد ا صف.
• He conducted other experiments in which he followed the inheritance
of two different characters (a dihybrid cross )ا تزا ج ا ا صف.
• In one dihybrid cross experiment, Mendel studied the inheritance of
seed color and seed shape.
The allele for yellow seeds (Y) is dominant compared to the allele for
green seeds (y).
The allele for round seeds (R) is dominant compared to the allele for
wrinkled seeds (r)
• Mendel crossed true-breeding plants that had yellow & round seeds
(YYRR) with true-breeding plants that has green & wrinkled seeds
(yyrr).
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
• The two pairs of alleles segregate independently of each other.
The presence of one specific allele for one trait has no impact تأ رon
the presence of a specific allele for the second trait.
• When a sperm and ova (each
with four classes of alleles)
combine, there would be 16
equally probable ways in which
the alleles can combine
in the F2 generation.
• These combinations produce
four distinct phenotypes in a
9:3:3:1 ratio.
• This was consistent with
Mendel re l .
• Each character appeared to be
inherited independently.
It is a mating between two parent plants different in two characters.
Y
YY RR X yy rr
R
YR y r
y
Y y Rr
r
F1 Yellow Round
Yy Rr X Yy Rr
YR Yr yR yr
YR YYRR
Yellow Round
Yr YYrr
Yellow Wrinkled
yR yyRR
Green Round
yr yyrr
Green Wrinkled
F2: % of Phenotype ?
• Thousands of genetic disorders أ راض را, including disabling ا ا
or deadly hereditary diseases ا راض ا را ا ُ ت, are inherited as
simple recessive traits صفات را ُ ت ح.
• These range from the relatively mild Albinism
(albinism ا، )اto life-threatening
(cystic fibrosis).
Heterozygotes have a normal phenotype because
one normal allele produces enough of the
required factors (for the normal trait).
• A recessively inherited disorder
shows up ظ رonly in the individuals who
inherit homozygous recessive allele from parents.
• Thus, individuals who lack the disorder are either
homozgyous dominant or heterozygous.
• Heterozygous member may have no clear phenotypic
effects, but is a carrier who may transmit a recessive allele to their offspring.
• Most people with recessive disorders are born from carrier parents with normal
phenotypes.
Two carriers have a 1/4 chance of having a child with the disorder, 1/2 chance of a carrier,
and 1/4 free.
1. Cystic fibrosis ( ) ا ت ف ا: a lethal recessive disorder
One in 25 people is a carrier.
The normal allele codes for a membrane protein that transports Cl- between
cells and the environment.
If these proteins are absent, there are abnormally high extracellular levels of
chloride that causes the mucus coats of certain cells to become thicker
and stickier زجthan normal.
This mucus build-up in the pancreas, lungs, digestive tract, and elsewhere
favoring bacterial infections.
Without treatment, affected children die before five, but with treatment can live
past their late 20 s. ( رض وراث ت ّح حدث عجز ترّ ع ا دد ارج ةCystic Fibrosis) ات ا
. ا راز ا ثر ص رة رة ع و ا ث رة ا ج
، و دى ذا ا رض ثر ع اج زة حددة،ا رد تعت د ع اعراض ا راد ا صا ا ت ا
وا ت اثر ا ج، وا ض، اج زة ا ت ت اول اثار ا ت ا،ا ع ج
وا صع ات ا تزا دة ع ء ا تصاص ا تا ات وا اد ا ذ،ا عراض ا رى وت ا راض ا رة
. صع ات ع ا ص، ا ج از ا ض و ا ضا ة إ ذ
،ا رة ا ث ث ات ا ع ر و ت ث ر ا صا ا ت ا، جد ع ج ت ا
و ث را ا ن ز ا زرع ا رة
2. Tay-Sachs disease ( ت )ا ه ا: a lethal recessive
disorder.
It is caused by a dysfunctional enzyme ر ا إز
that fails to break down specific brain lipids.
The symptoms begin with seizures ح, blindness,
and degeneration of motor and mental
performance a few months after birth.
Inevitably, the child dies after a few years.
3. Sickle-cell disease ا اد ا ج رض.
It is caused by the substitution of a single amino acid in
hemoglobin.
When oxygen levels in
the blood of an affected
individual are low,
sickle-cell hemoglobin
crystallizes into long
rods.
This deforms red blood
cells into a sickle shape.
Doctors can use regular
blood transfusions to
prevent brain damage
and new drugs to
prevent or treat other
problems.
• The two alleles are codominant as both normal and abnormal
hemoglobins are synthesized.
Although most harmful alleles are recessive, many human
disorders are due to dominant alleles.
1. Achondroplasia, a form of dwarfism ا ز,
has an incidence of one case in 10,000 people.
Heterozygous individuals have the dwarf phenotype.
Those who are not achodroplastic dwarfs are
homozygous recessive for this trait.
• Lethal dominant alleles are much less common
than lethal recessives because if a lethal
dominant kills an offspring before it can mature
and reproduce, the allele will not be passed on
to future generations.
2- Huntington s disease: a degenerative ر ض
ُ disease of the nervous system.
The dominant lethal allele has
no obvious phenotypic effect
until an individual is about 35
to 45 years old.
• The deterioration of the nervous
system is irreversible and
inevitably fatal ُ ت.
• Huntington's disease results in
an eventual loss of both mental
and physical control.
• The disease is also known as
Huntington's chorea (means
"dance-like movements ) refers to
the uncontrolled motions.
• Autosome - Any chromosome other than a sex
chromosome
• Genetic disorders caused by genes on autosomes
are called autosomal disorders
Some genetic disorders are autosomal dominant
• An individual with AA has the disorder
• An individual with Aa has the disorder
• An individual with aa does NOT have disorder
Other genetic disorders are autosomal recessive
• An individual with AA does NOT have disorder
• An individual with Aa does NOT have disorder, but is a carrier
• An individual with aa DOES have the disorder
16
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
A)- Sex Chromosomes.
Chromosomal systems of sex determination.
Sex-linked genes exhibit unique patterns of inheritance.
Inheritance of Sex-Linked Genes.
human Sex-linked disorders.
Duchenne muscular dystrophy.
Hemophilia.
Color blindness.
B)- Alterations of chromosomal number or structure cause some
genetic disorders:
Abnormal Chromosomal Number.
Alterations of Chromosomal Structure.
3
In human and other mammals, there are
two varieties of sex chromosomes, X & Y.
An individual who inherits two X
chromosomes usually develops as a female.
An individual who inherits an X and a Y
chromosome usually develops as a male.
This X-Y system of mammals is not the
only chromosomal mechanism of
determining sex.
Other options include the X-0 (in locust)
system, the Z-W system (in birds), and the
haplo-diploid system (in bees).
In Human, the SRY gene (Sex-determining
Region of the Y chromosome) modifies
embryonic gonads into testes.
Females lack the SRY gene, thus, the
embryonic gonads develop into ovaries.
In the X-Y system, Y and X chromosomes behave as
homologous chromosomes during meiosis.
In reality, they are only partially homologous and rarely
undergo crossing over
In both testes (XY) and ovaries (XX), the two sex
chromosomes segregate during meiosis and each
gamete receives one.
Each egg receives an X chromosome.
Half the sperm receive an X chromosome and half receive a Y
chromosome.
Because of this, each conception has about a fifty-fifty
chance of producing a particular sex.
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
The sex chromosomes, especially the X
chromosome, have genes for many
characters unrelated to sex.
These sex-linked genes ات رت ط ا س
follow the same pattern of inheritance
as the white-eye locus in Drosophila.
If a sex-linked trait is due to a recessive
allele, a female have this phenotype
only if homozygous.
Heterozygous females will be carriers.
1. Duchenne muscular dystrophy: ا ض ت
affects one in 3,500 males born in the United States.
Affected individuals rarely live past their early 20s.
This disorder is due to the absence of an X-linked gene for a
key muscle protein, called dystrophin.
The disease is characterized by a weakening ض فof the
muscles and loss of coordination فـ ـْد ا ت از.
2. Hemophilia: ا ز ف ا دis a sex-linked recessive
trait defined by the absence of one or more clotting
factors ت ط ا.
These proteins normally slow and then stop bleeding.
Individuals with hemophilia have prolonged bleeding ز ف ست ر
because a firm clot ت طforms slowly.
Individuals can be treated with intravenous injections of the
missing protein.
This gene is transmitted to offspring via the mothers.
Thus, Sons borne from hemophilic woman should be exempted
ُستfrom circumcision ا تا.
3. Color blindness: ا ا is a disorder inherited as a
recessive sex-linked character and affect both males and females.
A color blind female (XaXa) may be born to a color blind father (XaY)
and a carrier mother (XAXa)
Because males have only one X chromosome
(hemizygous), any male receiving the recessive allele
from his mother will express the trait.
Therefore, males are far more likely to inherit sex-
linked recessive disorders رضthan are females.
Alterations of chromosomes number or
structure cause some genetic disorders
Physical and chemical disturbances, as well as errors during
meiosis, can damage chromosomes in major ways or alter
their number in a cell.
A. Chromosomal deletions/translocations
Homologous chromatids may break and rejoin at incorrect
places, thus, one chromatid will loose more genes than it
receives.
B. Abnormal Chromosomal Number (Aneuploidy) ا ذوذ ا روم م
Result from non-disjunction of homologous chromosomes
during gametes production in one parent.
An abnormal number of a particular chromosome, is a
condition known as “Aneuploidy”.
Alterations of chromosome number or structure
cause some genetic disorders
Some organisms have more than two complete
chromosomal sets in all somatic cells.
The general term for this chromosomal alteration is
polyploidy م ا دد ا روم
Examples: triploidy (3n) and tetraploidy (4n) are specific
terms indicate three or four chromosomal sets, respectively.
Polyploidy is fairly common in the plant kingdom
Summary: Chromosomal number abnormality
Aneuploidy: results from the fertilization of gametes in
which non-disjunction occurred
Offspring with this condition have an abnormal number of a
particular chromosome
Polyploidy: is a condition in which an organism has
more than two complete sets of chromosomes:
Triploidy (3n) is three sets of chromosomes
Tetraploidy (4n) is four sets of chromosomes
12
Chapter 12
Summary: Alterations of Chromosome Structure
Breakage of a chromosome can lead to four
types of changes in chromosome structure:
1. Deletion: removes a chromosomal fragment
2. Duplication: repeats a segment
3. Inversion: reverses orientation of a segment
within a chromosome
4. Translocation: moves a segment from one
chromosome to another
14
a)- Aneuploidy in autosomes ( ات ا ذات ا ر )ا ت دد
Down syndrome trisomy in autosomes (3n)
Is due to three copies of chromosome 21 (2n + 1).
Although chromosome 21 is the smallest human chromosome, it
severely alters ُ رan individual s phenotype in specific ways.
Upward slant to eyes.
Small ears that fold over at the top.
Small, flattened nose.
Small mouth, making tongue appear large.
Short neck.
Small hands with short fingers.
In addition, down syndrome always involves
some degree of mental retardation, from mild to
severe. In most cases, the mental retardation is
mild to moderate.
The frequency of Down syndrome increases
with the age of the mother.
( ات ا ا ر )ا ت دد
1)- Klinefelter s syndrome: trisomy (3n) in sex chromosomes (2n + 1).
Disorder occurring due to nondisjunction of the X chromosome.
The Sperm containing both X and Y combines with an egg containing the X, results
in a male child.
The egg may contribute the extra X chromosome.
(a)- An XXY male,
occurs once in every 2000 live births.
These individuals have male sex organs,
but are sterile.
There may be feminine characteristics ص ات أ,
but their intelligence is normal.
(b)- An XYY male, tend to somewhat taller than average
2)- Triple X syndrome: a trisomy female (XXX), which occurs once
in every 2000 live births, produces healthy females.
3)- Turner s syndrome, a monosomy female (X0),
Occurs once in every 5000 births, produces phenotypic, but
immature females س ا ر اض.
Turner syndrome is associated
with underdeveloped ovaries,
short stature.
Bull neck, and broad chest.
Individuals are sterile, and lack
expected secondary sexual
characteristics.
Mental retardation typically not
evident.
Abnormal Chromosomal Number (Aneuploidy)
Autosomes Sex Chromosomes
Klinefelter s Turner s
Down trisomy syndrome
syndromes female (XXX)
syndrome (X0)
Females
(XXY) (XYY)
Males
It can also cause human disorders.
Deletions زف, even in a heterozygous state, cause severe physical
and mental problems.
1. Cri-du-chat ط ارض اء ا, (“cry of the cat”)
results from a specific deletion in chromosome 5.
- Is due to a missing part of chromosome 5
These individuals are mentally retarded, have a
small head with unusual facial features, and a cry
like the mewing of a distressed cat.
This syndrome is fatal in infancy ا طor
early childhood.
2. Myelogenous,
[leukemia (CML)].
Caused by chromosomal
translocations since a
fragment of chromosome 22
switches places with a
small fragment from the tip
of chromosome 9.
2
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
Objectives
CHEMICAL SIGNALS (Hormones) IN ANIMALS
• Function and Secretion of Hormones.
• Classes of Hormones and Mechanism of Chemical Signaling.
1)Pituitary gland:
1) Follicle-stimulating hormone (FSH) and luteinizing hormone (LH)
2) Thyroid-stimulating hormone (TSH)
3) Adrenocorticotropic hormone (ACTH)
4) Prolactin
5) Growth hormone (GH)
6) Melanocyte-stimulating hormone (MSH).
7) Endorphins.
8) Oxytocin
9) Antidiuretic hormone (ADH)
2) Pineal gland 3
• Hormones: are substances secreted by
cells that act to regulate the activity of
other cells in the body.
– Hormones affect all cells in the body
and are made and secreted by
endocrine glands.
• Endocrine glands: are ductless organs
that secret hormones either into the
bloodstream or the fluid around cells.
• The endocrine glands can be found
through out the body and are collectively
known as the endocrine system.
• Endocrine glands, such as the pancreas,
can also be exocrine glands.
– Exocrine glands: secrete substances
through ducts to specific locations
inside and outside the body.
Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
• Nervous and endocrine systems are the main internal
communication and regulation systems.
• The animal hormone-secreting cells constitute the endocrine
system.
• Secretory cell: is the site that secrets hormone into blood stream
and regulates communicating messages within the body.
• Target cell: is the site that is reached by the hormone to which it
responds.
• Complete changes in the body is regulated by hormones (e.g.
metamorphosis in insects).
• Types of hormones: are [Polypeptide H., Amino acid derivatives H
or Steroid H.].
Hormones can be grouped into two types based on their structure. Hormones
can either be amino acid-based hormones or steroid hormones.
– Amino acid based-hormones (protein hormones) are made of amino
acids, either a single modified amino acid or a protein made of 3-200
amino acids, and are water soluble.
– Steroid hormones are lipid hormones that body makes from cholesterol
and are fat soluble.
• Similar to steroid hormones are thyroid hormones.
I): Protein hormones:
Bind to a receptor protein on the surface of the target cell which
will trigger signal transduction pathway.
6
II) Steroid hormones:
Penetrate the cell and bind to a receptor protein inside the target cell. This
also will trigger signal transduction pathway (for triggering mRNA
transcription for synthesizing a specific protein).
• Estrogen, progesterone, vitamin D and NO.
– Usually, the intracellular receptor activated by a hormone is a
transcription factor.
8
Source: http://highered.mcgraw-hill.com/sites/dl/free/0072437316/120060/ravenanimation.html
• Tropic hormones: )ة ذة (ا ات ا ا ر
Target other endocrine glands and are important to
understanding chemical coordination.
• Many endocrine organs contain specialized nerve cells called
neurosecretory cells that secret hormones.
• The hormone epinephrine has two functions:
– As a hormone of the endocrine system.
– As a signal in the nervous system.
• Feedback is common in regulation of the activity of both
endocrine and nervous systems (homeostasis):
– Calcitonin and parathyroid hormones play an important role in maintaining
the concentration of the blood calcium constant.
– They are secreted from thyroid and parathyroid glands respictively.
• Hormones regulate the development of invertebrates (e.g. insects)
Tropic hormones
(دد ا )ا ر
Target other endocrine
glands and are
important to
understanding
chemical coordination.
• Human has 9
endocrine glands.
11
Fig. 45.5, Page 960
The hypothalamus and the pituitary gland,
control the initial release of many hormones
for the endocrine system.
The hypothalamus is the area of the brain
that coordinates many activities of the
nervous and endocrine systems.
The pituitary gland has two parts, anterior
and posterior. It stores and releases
hormones that are produced (synthesized)
by the hypothalamus. Hypothalamus
The neurosecretory cells of hypothalamus
produce hormones that function as:
Anterior
Posterior pituitary
a) Releasing hormones stimulate the anterior pituitary
pituitary (adenohypophysis) to secrete hormones.
b) Inhibiting hormones prevent the anterior
pituitary from secreting hormones.
A)- Anterior pituitary hormones. Gigantism
1) Growth hormone (GH): a protein.
• Stimulates growth and metabolism.
• Secretion is regulated by hypothalamic hormones.
• Acts directly on boon tissues or acts via growth factors.
o Gigantism: ال ملexcessive GH during development.
o Acromegaly: excessive GH production during adulthood.
o Hypopituitary dwarfism ال زم: childhood GH deficiency.
2) Prolactin (PRL): a protein.
Stimulates milk production and secretion from mammary gland ة ال دد ا.
This secretion is regulated by hypothalamic hormones.
A)- Anterior pituitary hormones.
3) Gonadotropins (Gonotropic ل )م ذ للم ا: glyocoproteins.
Follicle-stimulating hormone (FSH).
• Stimulates production of sperms and ova.
• Secretion is regulated by hypothalamic hormones.
Luteinizing hormone (LH) ال ُم ذ ل ن ال م ا ر.
• Stimulates ovaries and testes.
• Secretion is regulated by hypothalamic hormones.
4) Thyroid-stimulating hormone (TSH): a glycoprotein.
• Stimulates thyroid gland.
• Secretion is regulated by thyroxine in blood.
• Secretion is also regulated by hypothalamic hormones.
5) Adrenocorticotropic hormone (ACTH): a peptide
• Stimulates adrenal cortex secretion of glucocorticoids
• Secretion is regulated by glucocorticoids and hypothalamic hormones.
6) Melanocyte-stimulating hormone (MSH): a peptide.
• May play a role in fat metabolism.
7) Endorphins: peptides.
• Inhibit pain perception.
• Effects mimicked by heroin and other opiate drugs.
Melanocyte-
stimulating H.
Adrenocorticotropic
Also called gonadotropin 15
hormones ر ات ال ا ل
B)- Posterior pituitary hormones.
1. Oxytocin: a peptide.
• Stimulates contraction of the uterus and mammary glands.
• Secretion is regulated by the nervous system.
2. Antidiuretic hormone (ADH): ُم اد درار ال لa peptide.
• Promotes retention of
water by the kidneys
(in Kidney tubules).
• High level decreases
urination and vice versa.
• Secretion regulated by
water/salt balance.
Both ADH and Oxytocin are
synthesized by the hypothalamus,
then stored in and released by the
posterior pituitary. Antidiuretic H
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It is a small mass of tissue near the center of the mammalian
brain and is involved in biorhythms.
– The pineal gland secretes the hormone, melatonin, an
amine.
• Involved in biological rhythms associated with reproduction.
• Secretion is regulated by light/dark cycles.
Pineal gland
Pituitary gland
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Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings
3
• The thyroid gland of mammals consists
of two lobes located on the ventral
surface of the trachea. It contains 4
small Parathyroid glands. It plays role in
Thyroid
maintaining normal blood pressure, releasing H.
heart rate and digestion ..etc.
• Thyroid glands secretes 3
hormones:
I. Tri-iodothyronine [(T3), 3 I
atoms]: amino acid derivative. Thyroid
stimulating H.
II. Thyroxine [(T4), 4 I atoms]:
amino acid derivative.
– Stimulates and maintain metabolic
processes.
– Secretion is regulated by TSH
hormones. 4
III. Calcitonin: a peptide.
Lowers blood Ca2+ levels.
Its secretion regulated by calcium in blood.
a) Hyperthyroidism:
It is the excessive secretion of thyroid hormones causes:
• high body temperature, sweating, weight loss, Irritability, high blood pressure.
b) Hypothyroidism:
It is an insufficient ل لamount of thyroid hormones because of the
deficiency of I in human diet (causes Goiter).
Infants: cretinism. د ا ة
Adults: weight gain, lethargy ال ل, cold intolerance.
Goiter م ال دة : often is associated with iodine
deficiency ن ص.
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• PTH is secreted by The four parathyroid glands which are
embedded in the surface of the thyroid gland. It functions as:
– Raises blood Ca2+ levels.
– Secretion is regulated by calcium in the blood.
– Causes osteoclasts ف د ال ال ومto break down bone, releasing Ca2+ into
the blood.
– Stimulates the kidneys to reabsorb د إم صاصCa2+.
– Stimulates kidneys to convert vitamin D to its active form, which
stimulate intestine to absorb Ca2+.
– PTH and calcitonin are antagonistic م اد نhormones. Thus PTH and
calcitonin regulate blood calcium level (important role in homeostasis).
• Hypoparathyroidism (tetany):
It is a lack of PTH which causes:
– Ca2+ levels in the blood drop.
– Convulsive شنcontractions of the 6
skeletal muscles.
• The pancreas has both endocrine and exocrine functions.
– Exocrine function: secretion of bicarbonate ions and digestive
enzymes.
– Endocrine function: insulin and glucagon are secreted by beta and
alpha cells of islets of Langerhans وب ن رانز.
1. Insulin: a protein secreted by beta cells.
• Lowers blood glucose levels.
– Stimulates all body cells (except brain cells) to take up glucose.
– Slows glycogenolysis ( بط ء لل ال ل و نa source of glucose).
– Inhibits gluconeogenesis و ف و ن ال لو وز.
• Secretion is regulated by glucose in blood (negative feedback).
– Hypoinsulinism: diabetes mellitus ن ص اإلن ول ن.
• Hereditary factors امل وراand play a role in its development.
• High blood sugar levels – sugar is excreted in the urine.
• Symptoms: excessive urination رة ال بولand excessive thirst ال طش.
a) Type I diabetes mellitus (insulin-dependent diabetes).
• Autoimmune disorder.
• Usually appears in childhood الطفولة.
• Treatment: insulin injections.
b) Type II diabetes mellitus (non-insulin-dependent diabetes).
• Usually due to target cells having a decreased responsiveness to
insulin لة اإل ابة ل ن ول ن.
• Usually occurs after age 40 – risk increases with age.
• Accounts for over 90% of diabetes cases.
2. Glucagon: a protein secreted by alpha cells.
• Raises blood glucose levels.
– Stimulates glycogenolysis لل ال ل و نin the liver and skeletal
muscle to produce glucose.
– Secretion is regulated by glucose in blood (negative feedback).
Hormonal control of glucose
homeostasis in mammals blood
• The adrenal glands are located adjacent to the kidneys.
– The adrenal cortex ال رةis the outer portion.
– The adrenal medulla is the inner portion.
I- Adrenal medulla المر ز.
– Developmentally and functionally related to the nervous system.
– It produces the following hormones (in response to stress):
a) Epinephrine (adrenaline ) رمون ال لب.
b) Norepinephrine (noradrenaline).
They are amino acid derivatives (synthesized from tyrosine)
and function as:
• Raises blood glucose level and blood fatty acid level.
• Increases heart rate and stroke volume and dilates bronchioles.
• Shunts blood away from skin, digestive organs, and kidneys,
and increases blood flow to heart, brain, and skeletal muscle.
II- Adrenal cortex: reacts to stress.
• Secretion of corticosteroids (a family of steroid hormones) is
regulated by the nervous system in response to stress for example:
a) Glucocorticoids.
• Raises blood glucose level.
• Secretion is regulated by ACTH (Adrenocorticotropic
hormone).
• Abnormally high doses are administered as medication to
suppress the inflammation response.
b) Mineralocorticoids (example: aldosterone, which affects salt and
water balance).
• Promotes re-absorption of Na+ and excretion of K+ in kidneys.
• Their secretion regulated by K+ in blood.
C) Sex hormones.
• Androgens are secreted by the adrenal cortex may account for the
female sex drive.
• The adrenal cortex also secretes small amounts of estrogens and
progesterone.
a) Testes hormones:
– Testosterone): steroids.
• Supports sperm formation.
• Promote development and maintenance of male sex characteristics.
• Secretion is regulated by FSH and LH.
b) Ovaries hormones:
1) Estrogens: steroids.
• Stimulate uterine lining growth.
• Promote development and maintenance of female sex
characteristics.
• Secretion is regulated by FSH and LH.
2) Progesterone: steroids.
• Promotes uterine lining growth.
• Secretion is regulated by FSH and LH.
Secretes Thymosin: a peptide.
It stimulates T lymphocytes.
Protein hormones affect target cells via
receptors on the membrane protein
Steroid hormones enter the target cells
and trigger protein synthesis via
receptors in the nucleus.
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Table 45.1 (continued)