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TRANSLATION

The document describes the three main steps of protein initiation - initiation, elongation, and termination. It explains that initiation begins with a specific amino acid and tRNA binding to the small ribosomal subunit. Elongation then occurs through the stepwise binding of aminoacyl-tRNAs and formation of peptide bonds. Translocation moves the ribosome down the mRNA after each cycle.

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20 views16 pages

TRANSLATION

The document describes the three main steps of protein initiation - initiation, elongation, and termination. It explains that initiation begins with a specific amino acid and tRNA binding to the small ribosomal subunit. Elongation then occurs through the stepwise binding of aminoacyl-tRNAs and formation of peptide bonds. Translocation moves the ribosome down the mRNA after each cycle.

Uploaded by

khushboo bhardwaj
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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INITIATION:-

+ STAGE 1:- A Specific Amino Acid Initiates Protein Synthesis.


Prokaryotes- Formylmethionine attached to t RNAfMet
+ Protein synthesis begins at the amino-terminal end and proceeds by the
stepwise addition of amino acids to the carboxyl-terminal end of the growing
polypeptide.
+ The AUG initiation codon specifies an amino-terminal methionine residue.
+ methionine has only one codon, (5')AUG, all organisms have two tRNAs for
methionine. One when (5')AUG is the initiation codon for protein synthesis.
The other is used to code for a Met residue in an internal position in a
polypeptide.
+ The two types of tRNA specific for methionine are designated tRNA Met and
tRNA fMet . The amino acid incorporated in response to the (5')AUG
initiation codon is N-formylmethionine (fMet). It arrives at the ribosome as
+ Methionine + tRNA fMet + ATP → Met-tRNA fMet + AMP + Ppi
by the Met-tRNA synthetase .
+ N 10 -Formyltetrahydrofolate + Met-tRNA fMet → tetrahydrofolate
by transformylase transferase.
Met-tRNA fMet inserts methionine in interior positions in polypeptides.
In eukaryotic cells, all polypeptides synthesized by cytosolic ribosomes begin
with a Met residue (rather than fMet), but, again, the cell uses a specialized
initiating tRNA that is distinct from the tRNA Met used at (5')AUG codons at
interior positions in the mRNA.
+
The Three Steps of Initiation
INITIATION IN PROKARYOTES:-
+ The initiation of polypeptide synthesis in bacteria requires (1) the 30S ribosomal subunit, (2)
the mRNA coding for the polypeptide to be made, (3) the initiating fMet-tRNA fMet , (4) a set
of three proteins called initiation factors (IF1, IF2, and IF3), (5) GTP, (6) the 50S ribosomal
subunit, and (7) Mg 2+ .

STEP 1:-
+ 30S ribosomal subunit binds two initiation factors, IF1 and IF3.
+ Factor IF3 prevents the 30S and 50S subunits from combining prematurely.
+ The mRNA then binds to the 30S subunit.
+ The initiating (5')AUG is guided to its correct position by the Shine-Dalgarno sequence in the
mRNA.
+ The sequence base-pairs with a complementary pyrimidine-rich sequence near the 3' end of the
16S rRNA of the 30S ribosomal subunit .
+ This mRNA-rRNA interaction positions the initiating (5')AUG sequence of the mRNA in the
+ Bacterial ribosomes have three sites that bind tRNAs, the aminoacyl (A) site, the
peptidyl (P) site, and the exit (E) site.
+ The A and P sites bind aminoacyl-tRNAs, whereas the E site binds only
uncharged tRNAs that have completed their task on the ribosome.
+ Factor IF1 binds at the A site and prevents tRNA binding at this site during
initiation.
+ The initiating (5')AUG is positioned at the P site, the only site to which fMet-
tRNA fMet can bind .
+ The fMet-tRNA fMet is the only aminoacyl-tRNA that binds first to the P site;
during the subsequent elongation stage, all other incoming aminoacyl-tRNAs
bind first to the A site and then subsequently to the P and E sites.
+ The E site is the site from which the “uncharged” tRNAs leave during elongation.
+ Both the 30S and the 50S subunits contribute to the characteristics of the A and P
sites, whereas the E site is largely confined to the 50S subunit.
STEP 2:-
+ The complex consisting of the 30S ribosomal subunit, IF3, and mRNA is
joined by both GTP-bound IF2 and the initiating fMet-tRNA fMet . The
anticodon of this tRNA now pairs correctly with the mRNA’s initiation
codon.
STEP 3:-
+ this large complex combines with the 50S ribosomal subunit;
simultaneously, the GTP bound to IF2 is hydrolyzed to GDP and Pi, which
are released from the complex. All three initiation factors leave the
ribosome at this point.
+ Completion of the steps produces a functional 70S ribosome called the
initiation complex, containing the mRNA and the initiating fMet-tRNA
fMet .
Initiation in Eukaryotic Cells
ELONGATION:-. EF- Tu, EF-Ts , EF-G
Elongation Step 1: Binding of an Incoming Aminoacyl-tRNA
+ In the first step, the appropriate incoming aminoacyl-tRNA binds to a
complex of GTP-bound EF-Tu.
+ The resulting aminoacyl-tRNA–EF-Tu–GTP complex binds to the A site of
the 70S initiation complex.
+ The GTP is hydrolyzed and an EF-Tu–GDP complex is released from the
70S ribosome.
+ The bound GDP is released when the EF-Tu–GDP complex binds to EF-Ts,
and EF-Ts is released when another molecule of GTP binds to EF-Tu,
recycling it.
Elongation Step 2: Peptide Bond Formation
+ A peptide bond is now formed between the two amino acids bound by their
tRNAs to the A and P sites on the ribosome.
+ This occurs by transfer of the initiating N-formylmethionyl group from its
tRNA to the amino group of the second amino acid, now in the A site.
+ The α-amino group of the amino acid in the A site acts as a nucleophile,
displacing the tRNA in the P site to form a peptide bond.
+ The reaction produces a dipeptidyl-tRNA in the A site, and the now
“uncharged” (deacylated) tRNA fMet remains bound to the P site. The
tRNAs then shift to a hybrid binding state, with elements of each spanning
two different sites on the ribosome.
+ The peptidyl transferase activity that catalyzes peptide bond formation
resides in the 23S rRNA
Elongation Step 3: Translocation
+ In the final step of the elongation cycle, translocation, the ribosome moves one
codon toward the 3' end of the mRNA .
+ This movement shifts the anticodon of the dipeptidyltRNA, which is still
attached to the second codon of the mRNA, from the A site to the P site, and
shifts the deacylated tRNA from the P site to the E site, from where the tRNA is
released into the cytosol.
+ The third codon of the mRNA now lies in the A site and the second codon lies
in the P site.
+ Movement of the ribosome along the mRNA requires EF-G (also known as
translocase) and the energy provided by hydrolysis of another molecule of GTP.
+ After translocation, the ribosome, with its attached dipeptidyltRNA and mRNA,
is ready for the next elongation cycle and attachment of a third amino acid
residue
The elongation cycle in eukaryotes is similar to that in bacteria. Three
eukaryotic elongation factors (eEF1α, eEF1βγ, and eEF2) have functions
analogous to those of the bacterial elongation factors (EF-Tu, EF-Ts, and EF-
G, respectively).

THANK YOU

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