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TRANSLATE20b.swf

This is the info page for
Flash #166625

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Text
Polyribosomes

Polyribosomes

Polyribosomes

Ribosome Cycle

Ribosome Cycle

Ribosome Cycle

A strand of mRNA is translated in the 5' to
3' direction from the start codon to the
stop codon.

Translation Overview

Translation Overview

tRNA Charging

tRNA Charging

Initiation

Initiation

Elongation

Elongation

Termination

Termination

Small Ribosome Subunit
The small subunit of the ribosome
contains the decoding center in which
charged tRNAs are read the codon units of
the mRNA.

Roll over for
more info Ë

tRNA
tRNA is the adaptor between a codon and
an amino acid. Each tRNA is charged with
a particular amino acid and each
recognizes a particular codon.

Large Ribosome Subunit
The large subunit of the ribosome contains
the peptidyl transferase center, which is
responsible for the formation of peptide
bonds.

IF3
Initiation Factor 3 (IF3) facilitates initiation
by binding to the small subunit and
preventing it from reattaching prematurely
to the large subunit.

IF2
Initiation Factor 2 (IF2) is a GTPase. It
interacts with IF1, fMet­tRNA and the
small ribosome subunit. IF2 facilitates
association of fMET­tRNA and prevents
binding of other charged tRNAs to the
small subunit.

IF1
Initiation Factor 1 (IF1) facilitates initiation
by preventing tRNA from binding to the A
site of the small ribosome subunit.

EF­TU
Elongation Factor­TU (EF­Tu) is a GTPase
that is responsible for recruiting charged
aminoacyl tRNA to the A site of the
ribosome. EF­Tu can only bind to a
charged tRNA when it is associated with
GTP and releases the charged tRNA in
conjunction with the hydrolysis of GTP only
when there is a correct codon-anticodon
match.

EF­G
Elongation factor G (EF-G) is a GTPase that
is responsible for translocating the
ribosome one codon unit along the mRNA
after each peptidyl transferase reaction.
GTP-bound EF-G binds to the A site of the
ribosome. Hydrolysis of GTP triggers the
movement of the ribosome relative to the
mRNA, thereby shifting the peptidyl tRNA
from the A site back to the P site.

Class II RF
The class II release factor causes the
class I RF to dissociate from the ribosome
after the polypeptide chain is released.

Class I RF
Class I Release Factors recognize stop
codons and trigger hydrolysis of the acyl
bondlinking the completed polypeptide
chain to the tRNA in the P site.

RRF
Ribosome Recycling Factor (RRF) mimics
tRNA by occupying the vacant A site after
polypeptide release. It helps release the P
and E site tRNAs by recruiting EF­G to the
ribosome. Once the tRNAs are released it
dissociates from the ribosome.

Translation

mRNA

5'

3'

Start Codon

Stop Codon

5'

3'

Small Ribosomal Subunit

Charged tRNA

Translation begins with the binding of a free
small subunit and a charged tRNA to the
mRNA with the charged tRNA positioned over
the start codon.

Large Ribosomal Subunit

A large ribosomal subunit is recruited by the
mRNA/small subunit complex creating an
intact ribosome that is poised for translation.

Protein synthesis begins by the transfer of the
amino acid on the first charged tRNA to the
amino acid on the next incoming charged tRNA.

Protein synthesis continues with the
translocation of the ribosome to the next
codon on the mRNA and the transfer of the
growing polypeptide chain to the amino acid
on the next incoming charged tRNA.

As each codon goes by the newly synthesized
polypeptide grows.

Upon reaching a stop codon the peptide chain
is released and the subunits dissociate.

After dissociation, the small and large subunits
can re-associate at the start codon of the same
or a different mRNA and carry out another round
of protein synthesis. This cycle of association
and dissociation can be repeated multiple times
and is known as the ribosome cycle.

A ribosome is only capable of synthesizing a single
peptide strand at a time. A single mRNA can,
however, be translated simultaneously by a queue
of multiple ribosomes, each at a different stage of
completion of the growing polypeptide chain.

An mRNA that is being translated by multiple
ribosomes is known as a polysome.

Polyribosomes enable mulitiple polypeptides to be
generated from a single mRNA simultaneously.

Transfer to the tRNA

Transfer to the tRNA

Transfer to the tRNA

tRNA
tRNA is the adaptor between a codon
and an amino acid. Each tRNA is charged
with a particular amino acid and each
recognizes a particular codon.

Small Ribosomal Subunit
The small subunit of the ribosome
contains the decoding center in which
charged tRNAs are read the codon units of
the mRNA.

EF­G
Primase is an RNA polymerase that
generates an oligoribonucleotide that is
extended by DNA polymerase III.

IF­3
Blah, blah, blah....

EF­TU
lhjasdfjaljksdhfb a;dflh amn a;lkj a
jkanzvnm v0w0u n lkjad

Roll over for
more info Ë

Adenylylation

Adenylylation

Adenylylation

tRNA charging occurs in two steps,
adenylylation and transfer of the adenylylated
amino acid to tRNA. Adenylylation occurs when
an amino acid and ATP react. The amino acid is
adenylylated and pyrophosphate is released.

A

OH

O
­

O

­
O

P

3'

R

NH
2

C

H

Amino Acid

ATP

Adenylylated Amino Acid

Pyrophosphate

R

tRNA charging takes place when the
adenylylated amino acid reacts with tRNA,
which results in the release of AMP.

ACC

ACC

OH

tRNA

O

3'

AMP

High-energy Bond

CH
2

3

2

Both steps of tRNA charging are catalyzed by the
same enzyme (not depicted here), which is
called aminoacyl tRNA synthetase. Cells typically
have 20 synthetases, one for each amino acid.

Binding of mRNA and Initiator to the Small Subunit

Binding of mRNA and Initiator to the Small Subunit

Binding of mRNA and Initiator to the Small Subunit

Initiation Factors and the Initiation Complex

Initiation Factors and the Initiation Complex

Initiation Factors and the Initiation Complex

Creation of the First Peptide Bond

Creation of the First Peptide Bond

Creation of the First Peptide Bond

The ribosome is composed of large and
small subunits and has three binding sites
for tRNA called E, P, and A.

Small Subunit

Large Subunit

A

P

E

The A site binds charged tRNA.
The P site binds peptidyl tRNA.
The E site binds tRNA that had discharged the
growing polypeptide chain in the P site and is
about to be released from the ribosome.

In the initiation step of translation, mRNA binds
to the small subunit of the ribosome together
with a special charged tRNA called the initiator.
The initiator tRNA is charged with the unusual
amino acid N-formyl methionine (fMet).

UAC

UAC

fMet

UCCUC

5'

3'

AGGAG

AUG

Ribosome
Binding
Sequence

fMet­tRNA

CH
2

NH

S

CH
3

The small subunit aligns itself on the mRNA
by base pairing between the ribosome
binding site in the message and a
complementary sequence near the 3' end of
the RNA component (called the 16S RNA) of
the small subunit.

Meanwhile, the charged initiator tRNA enters
what will become the P site of the ribosome
by base pairing between the start codon (AUG)
and the anticodon of the tRNA.

The preceding events are driven by three
initiation factors called IF1, IF2 and IF3.

A

P

E

A

P

E

Initiation factor 3 (IF3) attaches to the small
subunit. It binds in the area of the E site
preventing premature attachment of the
large subunit.

IF3

Initiation factor 1 (IF1) attaches to the small
subunit in the area of the A site blocking the
attachment of tRNA.

IF1

P

GTP

GTP

Initiation factor 2 is a GTPase. It interacts
with IF1, the small subunit and fMet­tRNA.

IF2

Once all the initiation factors are in place,
the small subunit can attach to the initiator
tRNA and mRNA.

fMet-tRNA

IF3 is released after the initiator and mRNA are
assembled on the small subunit, allowing the
large subunit to attach.

Binding of the large subunit leads to the
hydrolysis of GTP by IF2, reducing its affinity
for the ribosome and the initiator tRNA. This,
in turn, leads to the release of both IF2 and
IF1 from the ribosome.

GDP

GDP

The fully assembled ribosome with empty E
and A sites is known as the initiation
complex and is ready to accept a charged
tRNA into the A site and carry out the
formation of the first peptide bond.

O

O

NH
2

C

H

Aminoacyl-tRNA

An aminoacyl-tRNA with the correct anticodon
for the codon in the A site is recruited to the
A site by elongation factor EF-Tu (not shown
but introduced below).

Next, the ribosome catalyzes peptide bond
formation between the incoming amino acid
of the charged tRNA in the A site and the
fMet amino acid attached to the initiator
tRNA in the P site by bringing the 3’ ends of
the two charged tRNAs into close proximity.

The amino group of the A site aminoacyl­tRNA
attacks the carbonyl group of the fMet­tRNA,
creating the first peptide bond.

OH

N

Elongation involves repeated cycles of the introduction
a charged tRNA into the A site, transfer of the growing
polypeptide chain in the P site to the amino acyl tRNA
in the A site, translocation of the ribosome along the
mRNA by one codon unit, and release of an uncharged
tRNA from the E site.

Introduction of Charged tRNA into the A site

Introduction of Charged tRNA into the A site

Introduction of Charged tRNA into the A site

Translocation

Translocation

Translocation

Peptidyl Transferase Reaction

Peptidyl Transferase Reaction

Peptidyl Transferase Reaction

Overview

Overview

Overview

As polypeptide elongation takes place,
aminoacyl­tRNAs are escorted to the A site
by elongation factor EF­Tu.

Peptidyl tRNA

Aminoacyl­tRNA

Polypeptide Chain

EF­Tu

Factor Binding Center

EF­Tu is a GTPase and is only able to bind
to the aminoacyl­tRNA when it is associated
with GTP.

EF­Tu­GTP

GTP-containing EF-Tu binds to aminoacyl-tRNA
and escorts it to the A site of the ribosome.
The GTPase is activated when EF-Tu contacts
the factor binding center and when a proper
codon­anticodon match is made.

EF­Tu hydrolyzes its GTP and exits the ribosome
leaving the aminoacyl­tRNA in the A site.

In a cycle catalyzed by elongation factor EF-Ts
(not shown) , GDP is replaced by a fresh
molecule of GTP, re-generating GTP-containing
EF-Tu, which is poised to bind to a fresh
molecule of charged tRNA.

Peptide bond formation is catalyzed by the transfer
of the growing polypeptide chain in the P site to the
incoming aminoacyl tRNA in the A site. This is
called the peptidyl transferase reaction, and it is
catalyzed by an RNA enzyme (ribozyme) in the large
subunit of the ribosome (not shown).

N

As described above for the formation of the first
peptide bond, the peptidyl transferase reaction
takes place by attack of the amino group of the
aminoacyl tRNA in the A site on the carbonyl
group of the peptidyl tRNA in the P site.

Peptidyl-tRNA

In the process of bond formation, the growing
polypeptide chain is transferred from the
peptidyl-tRNA to the aminoacyl­tRNA.

Translocation of the ribosome along the
mRNA is catalyzed by elongation factor EF-G,
which, like EF-Tu, is a GTPase.

EF­G

GTP hydrolysis by GTP-containing EF-G causes the
ribosome to advance one codon unit along the
mRNA, thereby shifting the peptidyl tRNA from the
previous peptidyl transferase reaction back to the
P site and shifting the deacylated tRNA in the P site
to the E site, where it exits the ribosome.

After translocation, EF-G-GDP dissociates
from the ribosome and its cargo of GDP is
replaced by a fresh molecule of GTP.

Cycles of peptide bond formation and translocation
continue until a stop codon is reached.

E­site tRNA

Ribosome Dissociation

Ribosome Dissociation

Ribosome Dissociation

Polypeptide Release

Polypeptide Release

Polypeptide Release

The stop codon is recognized by release
factors (RFs), which cause the release of the
now complete polypeptide chain from the
peptidyl-tRNA in the P site.

Class I RF

A class I release factor recognizes the stop
codon with a peptide anticodon at one end of the
molecule (highlighted in blue). A domain at the
other end of the release factor (green) triggers
the hydrolysis of the acyl bond to the tRNA. 

Next, a class II release factor triggers the
release of the class I release factor from the
ribosome in a process involving the exchange
of GTP for GDP on the factor and its
subsequent hydrolysis.

Class II RF

A final series of events involving a ribosome
recycling factor (RRF), EF-G and IF-3 causes
the discharge of the mRNA and deacylated
tRNAs from the ribosome and the dissociation
of the ribosome into its subunits, with IF-3
bound to the small subunit.

Deacylated tRNA

RRF

EF­G­GTP

The IF3-bound small subunit is now poised
to initiaite a new cycle of protein synthesis.

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Special Tags

Protect (24)Timeline Frame 10 bytes ""

Labels

"ribosome Cycle"Frame 1
"polyribosomes"Frame 2044
"adenylylation"Frame 2828
"tRNAcharging"Frame 3120
"Ribo binding site"Frame 3845
"assembly start"Frame 4967
"end assembly"Frame 6575
"first bond start"Frame 6576
"elongation start"Frame 7344
"elongation2 start"Frame 8620
"PTR start"Frame 9524
"elongation3 start"Frame 10278
"elongation4 start"Frame 10857
"termination start"Frame 12025




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Created: 18/10 -2018 18:15:57 Last modified: 18/10 -2018 18:15:57 Server time: 26/04 -2024 17:04:32