Cell Membranes

One universal feature of all cells is an

outer limiting membrane called the plasma
membrane.
In addition, all eukaryotic cells contain
elaborate systems of internal membranes
which set up various membrane-enclosed
compartments within the cell.
Cell membranes are built from lipids and
proteins.

Chapter 3: STRUCTURES and FUNCTIONS of the

CELL

Anatomy of a Cell

Plasma Membrane
phospholipid bilayer
specializations:
microvilli
membrane junctions: tight
junctions,
desmosomes
gap junctions

 The plasma membrane serves as the

interface between the machinery in
the interior of the cell and the
extracellular fluid (ECF) that bathes all
cells.

 The lipids in the plasma membrane are chiefly

phospholipids like phosphatidyl ethanolamine
and cholesterol. Phospholipids are amphiphilic
with the hydrocarbon tail of the molecule being
hydrophobic; its polar head hydrophilic. As the
plasma membrane faces watery solutions on both
sides, its phospholipids accommodate this by
forming a phospholipid bilayer with the
hydrophobic tails facing each other.

functions of plasma membrane

protects cellular contents

makes contact with other cells

contains channels, transporters...
mediates the entry and exit of
substances

FLUID MOSAIC MODEL

Integral Membrane Proteins

Many of the proteins associated with the
plasma membrane are tightly bound to it.
Some are attached to lipids in the bilayer.

Integral Membrane Proteins

In others - the transmembrane proteins the polypeptide chain actually traverses
the lipid bilayer. The figure shows a
transmembrane protein that passes just
once through the bilayer and another that
passes through it 7 times. All G-proteincoupled receptors (e.g., receptors of
peptide hormones, and odors each span
the plasma membrane 7 times.

Integral Membrane Proteins

In all these cases, the portion within the
lipid bilayer consists primarily of
hydrophobic amino acids. These are
usually arranged in an alpha helix so that
the polar -C=O and -NH groups at the
peptide bonds can interact with each other
rather than with their hydrophobic
surroundings.

Integral Membrane Proteins

Those portions of the polypeptide that
project out from the bilayer tend to have a
high percentage of hydrophilic amino
acids. Furthermore, those that project into
the aqueous surroundings of the cell are
usually glycoproteins, with many
hydrophilic sugar residues attached to the
part of the polypeptide exposed at the
surface of the cell.

Integral Membrane Proteins

Some transmembrane proteins that span
the bilayer several times form a
hydrophilic channel through which certain
ions and molecules can enter (or leave) the
cell

Peripheral Membrane Proteins

These are more loosely associated with the
membrane. They are usually attached
noncovalently to the protruding portions of
integral membrane proteins.

Peripheral Membrane Proteins

These are more loosely associated with the
membrane. They are usually attached
noncovalently to the protruding portions of
integral membrane proteins.

Membrane proteins are often restricted in

their movements.
A lipid bilayer is really a film of oil. Thus we
might expect that structures immersed in it
would be relatively free to float about. For
some membrane proteins, this is the case.
For others, however, their mobility is
limited:

Membrane proteins are often restricted in

their movements.
Some of the proteins exposed at the
interior face of the plasma membrane are
tethered to cytoskeletal elements like
actin microfilaments.
Some proteins are the exterior face of the
plasma membrane are anchored to
components of the extracellular matrix like
collagen.

Membrane proteins are often restricted in

their movements.
Integral membrane proteins cannot pass
through the tight junctions found between
some kinds of cells (e.g., epithelial cells).

 Cytoplasm

cellular contents between plasma

membrane & nucleus
2 components:
cytosol

organelles

Cytoplasmic Structures & Organelles

Cytoskeleton: protein filaments

microfilaments
intermediate filaments
microtubules
maintains shape, general
organization & cell integrity
responsible for movement of cell

 Cytoplasm
cellular contents between plasma
membrane & nucleus
2 components:
cytosol

organelles

 Cytoskeleton
protein filaments
microfilaments
intermediate filaments
microtubules

maintains shape , gen. organization &

cell integrity
responsible for movements of cell

 Centrosome

pericentriolar area plus paired

centrioles
9 + 0 array of microtubules

The Centrosome
The centrosome is
located in the cytoplasm attached to the outside
of the nucleus.
Just before mitosis, the centrosome duplicates.
The two centrosomes move apart until they are on
opposite sides of the nucleus.
As mitosis proceeds, microtubules grow out from
each centrosome with their plus ends growing
toward the metaphase plate. These clusters of
microtubules are called spindle fibers.

The Centrosome
microtubules growing in
vitro from an isolated
centrosome. The
centrosome was supplied
with a mixture of alpha
and beta tubulin
monomers. These
spontaneously
assembled into
microtubules only in the
presence of centrosomes.

Spindle fibers have three destinations:

Some attach to one kinetochore of a dyad with
those growing from the opposite centrosome
binding to the other kinetochore of that dyad.
Some bind to the arms of the chromosomes.
Still others continue growing from the two
centrosomes until they extend between each
other in a region of overlap.

serve as centers for organizing

microtubules

for forming the mitotic spindle

for formation and regeneration of cilia and
flagella

Centrioles
Each centrosome contains a pair of
centrioles.
Centrioles are built from a cylindrical array
of 9 microtubules, each of which has
attached to it 2 partial microtubules.

Centrioles
When a cell enters the cell cycle, and
proceeds from G1 to S phase, each centriole
is duplicated. A "daughter" centriole grows
out of the side of each parent centriole.
Thus centriole replication like DNA
replication (which is occurring at the same
time) is semiconservative.

Centrioles
Once formed, most of the functions of the
centrosomes can be accomplished without
centrioles. However,
Centrioles appear to be needed to organize the
centrosome in which they are embedded.
Sperm cells contain a pair of centrioles; eggs
have none. The sperm's centrioles are absolutely
essential for forming a centrosome which will
form a spindle enabling the first division of the
zygote to take place.
Centrioles are also needed to make cilia and
flagella.

Centrioles
Once formed, most of the functions of the
centrosomes can be accomplished without
centrioles.
However, Centrioles appear to be needed to
organize the centrosome in which they are
embedded.
Sperm cells contain a pair of centrioles; eggs
have none. The sperm's centrioles are absolutely
essential for forming a centrosome which will
form a spindle enabling the first division of the
zygote to take place.
Centrioles are also needed to make cilia and
flagella.

 Cilia and Flagella

motile cell surface projections
9 + 2 array of microtubules
basal body

cilia ensure steady flow of fluid along the

cells surface
flagella move the entire cell

 Both cilia and flagella have the same basic

structure. If the cell has
many short ones, we call them cilia or
only one or a few long ones, we call them
flagella.

 Each cilium (or flagellum) is made of

a cylindrical array of 9 evenly-spaced
microtubules, each with a partial
microtubule attached to it. This gives the
structure a "figure 8" appearance when
view in cross section.
2 single microtubules run up through the
center of the bundle, completing the socalled "9+2" pattern.
The entire assembly is sheathed in a
membrane that is simply an extension of
the plasma membrane.

 Motion of cilia and flagella is created by the

microtubules sliding past one another
Link. This requires:
motor molecules of dynein, which link
adjacent microtubules together, and
the energy of ATP.
Each cilium or flagellum grows out from,
and remains attached to, a basal body
embedded in the cytoplasm. Basal bodies
are identical to centrioles and are, in fact,
produced by them.

 Ribosome
composed of rRNA and many ribosomal
proteins
high content of ribonucleic acid
2 subunits : 40 S & 60 S
2 forms of ribosomes:
free ribosomes
bound ribosomes
synthesize proteins

 Endoplasmic Reticulum
membranous network of flattened sacs
and tubules
2 forms;
rough ER
smooth ER
synthesize proteins for secretion
forms new membranes
synthesize CHO, phospholipids, fats &
steroids
for detoxification

 Golgi Complex
flattened membranous sacs called
cisterns
modifies, sorts packages and transport
products received from ER
forms secretory vesicles
forms peroxisomes

 Lysosomes
membrane enclosed vesicle
40 different kinds of hydrolytic enzymes
pH 5

phagocytosis
autophagy
autolysis

 Peroxisomes
formed by division of pre existing
peroxisomes
contain enzymes that can oxidize
organic substances
Peroxisomes are also called
microbodies.
oxidize amino acids and fatty acids
oxidize toxic substances
contains catalase that decomposes
H2O2

 Peroxisomes
Peroxisomes
Peroxisomes are about the size of
lysosomes (0.51.5 m) and like them are
bound by a single membrane.
They also resemble lysosomes in being
filled with enzymes.

 Peroxisomes
Peroxisomes
The enzymes and other proteins destined
for peroxisomes are synthesized in the
cytosol. Each contains a peroxisomal
targeting signal (PTS) that binds to a
receptor molecule that takes the protein
into the peroxisome and then returns for
another load.

 Peroxisomes
Peroxisomes
Two peroxisomal targeting signals have
been identified:
a 9-amino acid sequence at the N-terminal
of the protein;
a tripeptide at the C-terminal.

 Peroxisomes
Peroxisomes
Each has its own receptor to take it to the
peroxisome. Some of the functions of the
peroxisomes in the human liver:
Breakdown (by oxidation) of excess fatty
acids.
Breakdown of hydrogen peroxide (H2O2), a
potentially dangerous product of fatty-acid
oxidation. It is catalyzed by the enzyme
catalase. [Link to further discussion]

 Peroxisomes
Peroxisomes
Participates in the synthesis of cholesterol.
One of the enzymes involved, HMG-CoA
reductase, is the target of the popular
cholesterol-lowering "statins".
Participates in the synthesis of bile acids.
Participates in the synthesis of the lipids
used to make myelin.
Breakdown of excess purines (AMP, GMP) to
uric acid.

Lysosomes and Peroxisomes

Lysosomes
Lysosomes are roughly spherical bodies
bounded by a single membrane. They are
manufactured by the Golgi apparatus

Lysosomes and Peroxisomes

Lysosomes
They contain over 3 dozen different kinds of
hydrolytic enzymes including
proteases
lipases
nucleases
polysaccharidases

Lysosomes and Peroxisomes

Lysosomes
The pH within the lysosome is about pH 5,
substantially less than that of the cytosol
(~pH 7.2). All the enzymes in the lysosome
work best at an acid pH. This reduces the
risk of their digesting their own cell if they
should escape from the lysosome

Lysosomes and Peroxisomes

Lysosomes
At one time, it was thought that lysosomes
were responsible for killing cells
scheduled to be removed from a tissue; for
example, the resorption of its tail as the
tadpole metamorphoses into a frog. This is
incorrect. These examples of programmed
cell death (PCD) or apoptosis take place by
an entirely different mechanism

Lysosomes and Peroxisomes

Lysosomes
Materials within the cell scheduled for digestion
are first deposited within lysosomes. These may
be:
other organelles, such as mitochondria, that have
ceased functioning properly and have been
engulfed in autophagosomes
food molecules or, in some cases, food particles
taken into the cell by endocytosis
foreign particles like bacteria that are engulfed
by neutrophils

Lysosomes and
Peroxisomes
Lysosomes

Lysosomes and Peroxisomes

Lysosomes
Lysosomal Storage Diseases
Lysosomal storage diseases are caused by the
accumulation of macromolecules (proteins,
polysaccharides, lipids) in the lysosomes
because of a genetic failure to manufacture an
enzyme needed for their breakdown. Neurons of
the central nervous system are particularly
susceptible to damage.
Most of these diseases are caused by the
inheritance of two defective alleles of the gene

Lysosomes and Peroxisomes

Lysosomes
Lysosomal Storage Diseases
Examples:
Tay-Sachs disease and Gaucher's disease both
caused by a failure to produce an enzyme needed
to break down sphingolipids (fatty acid
derivatives found in all cell membranes).

Lysosomes and Peroxisomes

Lysosomes
Lysosomal Storage Diseases
Examples:
Mucopolysaccharidosis I (MPS-I). Caused by a
failure to synthesize an enzyme (-L-iduronidase)
needed to break down proteoglycans like heparan
sulfate. In April 2003, the U.S. Food and Drug
Administration approved a synthetic version of
the enzyme, laronidase (Aldurazyme), as a
possible treatment. This enzyme (containing 628
amino acids) is manufactured by recombinant
DNA technology.

Lysosomes and Peroxisomes

Lysosomes
Lysosomal Storage Diseases
Examples:
However, one lysosomal storage disease, I-cell
disease ("inclusion-cell disease"), is caused by a
failure to "tag" (by phosphorylation) all the
hydrolytic enzymes that are supposed to be
transported from the Golgi apparatus to the
lysosomes. Lacking the mannose 6-phosphate
(M6P) tag, they are secreted from the cell instead.

Lysosomes and Peroxisomes

Lysosomes
Secretory Lysosomes
In some cells, lysosomes have a secretory
function releasing their contents by
exocytosis.
Cytotoxic T cells (CTL) secrete perforin from
lysosomes.

Lysosomes and Peroxisomes

Lysosomes
Mast cells secrete some of their many mediators
of inflammation from modified lysosmes.
Melanocytes secrete melanin from modified
lysosomes.
The exocytosis of lysosomes provides the
additional membrane needed to quickly seal
wounds in the plasma membrane.

 Mitochondria
shoe or sausage-shaped organelles
bounded by two membranes
powerhouse / energy currency
generate ATP

 Nucleus
spherical / oval shaped
most prominent
surrounded by a nuclear envelope
controls cellular structure
directs cellular activities

The Nucleus
The nucleus is the hallmark of eukaryotic
cells; the very term eukaryotic means
having a "true nucleus". The Nuclear
Envelope

The Nucleus
Chromatin
The nucleus contains the chromosomes
of the cell. Each chromosome consists
of a single molecule of DNA complexed
with an equal mass of proteins.

The Nucleus
Chromatin
Collectively, the DNA of the nucleus with its
associated proteins is called chromatin. Most
of the protein consists of multiple copies of 5
kinds of histones. These are basic proteins,
bristling with positively charged arginine and
lysine residues. (Both Arg and Lys have a
free amino group on their R group, which
attracts protons (H+) giving them a positive
charge.) Just the choice of amino acids you
would make to bind tightly to the negativelycharged phosphate groups of DNA.

The Nucleus
Chromatin
Chromatin also contains small amounts of a wide variety
of nonhistone proteins. Most of these are transcription
factors (e.g., the steroid receptors) and their association
with the DNA is more transient.

 Chromatin
loose network of bumpy threads
found in the nucleus

forms chromosomes in a dividing cell

 Nucleolus

small, dark-staining round bodies

site for ribosome assembly

Nucleolus
During the period between cell divisions, when
the chromosomes are in their extended state, 1 or
more of them (10 in human cells) have loops
extending into a spherical mass called the
nucleolus. Here are synthesized three (of the
four) kinds of RNA molecules (28S, 18S, 5.8S) used
in the assembly of the large and small subunits of
ribosomes.

Nucleolus
28S, 18S, and 5.8S ribosomal RNA is transcribed
(by RNA polymerase I) from hundreds to
thousands of tandemly-arranged rDNA genes
distributed (in humans) on 10 different
chromosomes. The rDNA-containing regions of
these 10 chromosomes cluster together in the
nucleolus.

FLAGELLA

NUCLEUS

CILIA
PEROXISOME

NUCLEOLUS

CENTRIOLE
SMOOTH ER

LYSOSOME

ROUGH ER

GOLGI
MITOCHONDRIA

FLUID MOSAIC MODEL

Cell Physiology
Membrane Transport
Osmosis
movement of water molecules across a
selectively permeable membrane
from higher concentration to lower
concentration

solvent and water in living systems

Tonicity = tension
isotonic
hypotonic
hypertonic

Tonicity & Its Effects on RBC

Passive Transport Processes

Diffusion
random movement due to intrinsic
kinetic energy
movement is down a concentration
gradient ( downhill)

 Diffusion through the lipid bilayer

passive diffusion of a substance
through the plasma membrane
substances transported:
non-polar hydrophobic solutes
oxygen & carbon dioxide
nitrogen
fatty acids & steroids
fat soluble vitamins
glycerol, small alcohols, NH3

 Diffusion through membrane channels

passive diffusion of a substance down
its electrochemical gradient
through channels
some channels are open all the time
while some are gated
Substances transported:
small inorganic solutes
K+, Na+, Cl- & Ca+2

DIFFUSION THRU MEMBRANE

CHANNELS

 Facilitated Diffusion
passive but mediated transport
transport is down a concentration
gradient
transmembrane proteins act as
transporters
maximum diffusion rate is limited by
number of transporters
transports polar or charged solutes,
glucose, fructose, galactose, urea and
some vitamins

FACILITATED DIFFUSION

 Filtration
movement of water and solutes through
a membrane or capillary wall by
hydrostatic pressure
pressure gradient
transports solute-containing fluid
( filtrate)

Active Transport Processes

mediated transport
energy
against its concentration gradient
transmembrane proteins act as
transporters

 Primary Active Transport

solute pumps
transport of a substance against its
concentration gradient
transmembrane proteins that use ATP
Ex. Na+ & K+ pump
transports Na+, K+, Ca+2, Cl- & other
ions

 Primary Active Transport

a. In primary active transport, energy derived from ATP changes the
shape of a transporter protein, which pumps a substance across a
plasma membrane against its concentration gradient.
b. The most prevalent primary active transport mechanism is the
sodium ion/potassium ion pump

 Secondary Active Transport

coupled transport of 2 substances
energy supplied by a Na+ or H+
concentration gradient
antiporters = opposite direction
symporters = same direction
Substance transported;
antiporters: Ca+2 & H+ out of cells
symporters; glucose, amino acids
into the cell

Secondary Active Transport

a. In secondary active transport, the energy stored in the form of a sodium or
hydrogen ion concentration gradient is used to drive other substances against their
own concentration gradients.
b. Plasma membranes contain several antiporters and symporters powered by the
sodium ion gradient
Digitalis slows the sodium ion-calcium ion antiporters, allowing more calcium to stay
inside heart muscle cells, which increases the force of their contraction and thus
strengthens the heartbeat

 Vesicular Transport
A vesicle is a small membranous sac formed by
budding off from an existing membrane

movement of substances into or out of

the cell in vesicles
ATP
2 Kinds:
1. Endocytosis

2 Exocytosis

 Endocytosis
phagocytosis
transports bacteria, viruses, aged
or dead cells
pinocytosis
transports solutes in extracellular
fluid
In endocytosis, materials move into a
cell in a vesicle formed from the plasma
membrane.

Receptor-mediated
endocytosis is the
selective uptake of
large molecules
and particles by
cells

Phagocytosis is the ingestion of solid particles

Pinocytosis is the ingestion of extracellular fluid

 Exocytosis

transports neurotransmitters,
hormones & digestive enzymes
In exocytosis, membrane-enclosed structures
called secretory vesicles that form inside the cell
fuse with the plasma membrane and release their
contents into the extracellular fluid

CELL DIVISION and CELL CYCLE

 INTERPHASE

 Prophase

 PROMETAPHASE

METAPHASE

 ANAPHASE

 Telophase

Chromatids arrive at
opposite poles of cell, and
new membranes form
around the daughter
nuclei. The chromosomes
disperse and are no
longer visible under the
light microscope. The
spindle fibers disperse,
and cytokinesis or the
partitioning of the cell
may also begin during this
stage.

 Cytokinesis
In animal cells,
cytokinesis results when a
fiber ring composed of a
protein called actin
around the center of the
cell contracts pinching
the cell into two daughter
cells, each with one
nucleus. In plant cells, the
rigid wall requires that a
cell plate be synthesized
between the two daughter
cells.

CELLULAR DIVERSITY

DISORDERS: HOMEOSTATIC
IMBALANCES
A. Cancer is a group of diseases characterized
by uncontrolled cell proliferation.
1. Cells that divide without control develop into a
tumor or neoplasm
2. A cancerous neoplasm is called a malignant
tumor or malignancy. It has the ability to undergo
metastasis, the spread of cancerous cells to other
parts of the body. A benign tumor is a noncancerous
growth.

DISORDERS: HOMEOSTATIC
IMBALANCES
Types of Cancer
1. Carcinomas arise from epithelial cells.
2. Melanomas are cancerous growths of
melanocytes
3. Sarcomas arise from muscle cells or
connective tissues
4. Leukemia is a cancer of blood-forming
organs
5. Lymphoma is a cancer of lymphatic tissue.

DISORDERS: HOMEOSTATIC
IMBALANCES
Growth and Spread of Cancer
1. Cancer cells divide rapidly and
continuously.
2. They trigger angiogenesis, the growths of
new networks of blood vessels.
3. Cancer cells can leave their site of origin
and travel to other tissues or organs, a process
called metastasis.

DISORDERS: HOMEOSTATIC
IMBALANCES
Causes of Cancer
1. Environmental agents can cause cancer growth. A
chemical agent. or radiation that produces cancer is
termed a carcinogen and induces mutations in DNA.
2. Viruses can cause cancer.
3. Cancer-causing genes, or oncogenes, can cause
cancer.
The normal counterparts of oncogenes are called protooncogenes; these are found in every cell and carry out normal
cellular functions until a malignant change occurs via a
mutation.
b. Some cancers may also be caused by genes called antioncogenes or tumor-suppressor genes. These genes may
produce proteins that normally oppose the action of an
oncogene or inhibit cell division.
a.

DISORDERS: HOMEOSTATIC
IMBALANCES
Carcinogenesis is a multistep process
involving mutation of oncogenes and antioncogenes; as many as 10 distinct
mutations may have to accumulate in a cell
before it becomes cancerous

Treatment of Cancer
1. Treatment of cancer is difficult because it
is not a single disease and because all the
cells in a tumor do not behave in the same way.
2. Various treatments include surgery,
chemotherapy, and radiation therapy

PROTEIN SYNTHESIS

PROTEIN SYNTHESIS
DNA - deoxyribonucleic acid
found in the nucleus
controls the function and structures of the cell
genes are segments of DNA
each gene controls the synthesis of one protein
(generally)
proteins are composed of amino acids arranged
in specific sequences - polypeptide chains
each amino acid is synthesised by a set of three
nucleotides called a codon

PROTEIN SYNTHESIS
Steps in Protein Synthesis:

Much of the cellular machinery is devoted

to synthesizing large numbers of diverse
proteins.
1. The proteins determine the physical and
chemical characteristics of cells.
2. The instructions for protein synthesis is
found in the DNA in the nucleus.
3. Protein synthesis involves transcription
and translation

PROTEIN SYNTHESIS

DNA "unzips" - a segment of the double helix

uncoils and separates to allow mRNA to be formed
mRNA leaves the nucleus
mRNA attaches to a ribosome on the endoplasmic
reticulum
each tRNA segment brings a specific amino acid
(present in the cytoplasm) to the mRNA
each tRNA can only link with a specific amino
acid
when all of the sites on the mRNA are occupied by
complementary segments of RNA, the protein folds
to form its specific characteristic shape
some proteins need to go to the Golgi apparatus to
complete their synthesis

PROTEIN SYNTHESIS
Steps in Protein Synthesis:
STEP 1: The first step in protein synthesis is the
transcription of mRNA from a DNA gene in the
nucleus. At some other prior time, the various
other types of RNA have been synthesized using
the appropriate DNA. The RNAs migrate from the
nucleus into the cytoplasm.Prior to the beginning
of the protein synthesis, all of the component
parts are assembled in the ribosome

 Transcription is the
process by which
genetic information
encoded in DNA is
copied onto a strand
of RNA called
messenger RNA
(mRNA), which directs
protein synthesis

PROTEIN SYNTHESIS
Besides serving as the template for the
synthesis of mRNA, DNA also synthesizes
two other kinds of RNA, ribosomal RNA
(rRNA), and transfer RNA (tRNA).
b. Transcription of DNA is catalyzed by RNA
polymerase.
c. Antisense therapy that blocks mRNA has
been approved by the FDA

PROTEIN SYNTHESIS

Translation
1. Translation is the process of reading the
mRNA nucleotide sequence to determine the
amino acid sequence of the protein

PROTEIN SYNTHESIS
STEP 2: Initiation:
In the cytoplasm, protein synthesis is actually
initiated by the AUG codon on mRNA. The AUG
codon signals both the interaction of the
ribosome with m-RNA and also the tRNA with the
anticodons (UAC). The tRNA which initiates the
protein synthesis has N-formyl-methionine
attached. The formyl group is really formic acid
converted to an amide using the -NH2 group on
methionine (left most graphic)

PROTEIN SYNTHESIS

some proteins are exported as enzymes, hormones, etc

some proteins are necessary for the cell's function

some are used to produce membranes or the structures

on membranes

PROTEIN SYNTHESIS
STEP 2: Initiation:
The next step is for a second tRNA to approach the
mRNA (codon - CCG). This is the code for proline.
The anticodon of the proline tRNA which reads
this is GGC. The final process is to start growing
peptide chain by having amine of proline to bond
to the carboxyl acid group of methinone (met) in
order to elongate the peptide

PROTEIN SYNTHESIS
STEP 3: Elongation:
Elongation of the peptide begins as various tRNA's
read the next codon. In the example on the left the
next tRNA to read the mRNA is tyrosine. When the
correct match with the anticodons of a tRNA has
been found, the tyrosine forms a peptide bond
with the growing peptide chain .
The proline is now hydrolyzed from the tRNA. The
proline tRNA now moves away from the ribosome
and back into the cytoplasm to reattach another
proline amino acid.

PROTEIN SYNTHESIS
Step 4: Elongation and Termination:
When the stop signal on mRNA is reached, the
protein synthesis is terminated. The last amino
acid is hydrolyzed from its t-RNA.
The peptide chain leaves the ribosome. The Nformyl-methionine that was used to initiate the
protein synthesis is also hydrolyzed from the
completed peptide at this time.
The ribosome is now ready to repeat the
synthesis several more times.