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Translation in prokaryotes
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Translation in Prokaryotes
It is the process of synthesis of protein by encoding information on
mRNA.
Protein synthesis requires mRNA, tRNA, aminoacids, ribosome and
enzyme aminoacyl tRNA synthase

Various protein factors involved in protein

synthesis

Factors Translation steps Functions

IF-1 Initiation Helps to stabilize 30S ribosomal

subunit

IF-2 Initiation Binds fmet-tRNA with 30S subunit

mRNA complex; bind GTP and
hydrolyse

IF-3 Initiation Binds 30S subunit with mRNA

EF-TU Elongation Binds GTP; bring Aminoacyl-tRNA

to A-site of ribosome

EF-TS Elongation Generates EF-TU

EF-G Elongation Helps in translocation of ribosome

RF-1 Termination Helps to dissociates polypeptide

from tRNA ribosome complex;
speci"c for UAA and UAG

RF-2 Termination Helps to dissociates polypeptide;

speci"c for UGA and UAA

RF-3 Termination Stimulates RF-1 and RF-2

Steps in translation:

1. Activation of aminoacids:

The activation of aminoacids take place in cytosol.

The activation of aminoacids is catalyzed by their aminoacyl tRNA
synthetases.
All the 20 aminoacids are activated and bound to 3’ end of their speci"c
tRNA in the presence of ATP and Mg++.
The N-formylated methionine is chain initiating aminoacid in bacteria
whereas methionine is chain initiating aminoacid in eukaryotes.
Methionine is activated by methionyl-tRNA synthetase. For N-
formylmethionine two types of tRNA are used ie. tRNAmet and tRNAfmet.
Similarly, all 2o aminoacids are activated (amino acyl-AMP enzyme
complex) and then bound to their speci"c tRNA forming Aminoacyl tRNA.

2. Initiation:

In the "rst step, initiation factor-3 (IF-3) binds to 30S ribosomal unit.
Then mRNA binds to 30S ribosomal subunit in such a way that AUG codon
lie on the peptidyl (P) site and the second codon lies on aminoacyl (A) site.

The tRNA carrying formylated methionine ie. FMet–tRNAFMet is palced at P-

site. This speci"city is induced by IF-2 with utilization of GTP. The IF-1
prevent binding of FMet–tRNAFMet is in A-site.
Shinedalgrno sequence in the mRNA guide correct positioning of AUG
codon at P-site of 30S ribosome.

After binding of FMet–tRNAFMet on P-site, IF-3, IF-2 and IF-1 are released so
that 50S ribosomal unit bind with 30S forming 70S sibosome. The exit site
is located in 50S.

3. Elongation:

i. Binding of AA-tRNA at A-site:

The 2nd tRNA carrying next aminoacid comes into A-site and recognizes
the codon on mRNA. This binding is facilitated by EF-TU and utilizes GTP.
After binding, GTP is hydrolysed and EF-TU-GDP is releasd
EF=TU-GDP then and enter into EF-TS cycle.

ii. Peptide bond formation:

The aminoacid present in t-RNA of P-site ie Fmet is transferred to t-RNA of

A-site forming peptide bond. This reaction is catalyzed by
peptidyltransferase.
Now, the t-RNA at P-site become uncharged

iii. Ribosome translocation:

After peptide bond formation ribosome moves one codon ahead along
5’-3’ direction on mRNA, so that dipeptide-tRNA appear on P-site and next
codon appear on A-site.
The uncharged tRNA exit from ribosome and enter to cytosol.
The ribosomal translocation requires EF-G-GTP (translocase enzyme)
which change the 3D structure of ribosome and catalyze 5’-3’ movement.
The codon on A-site is now recognized by other aminoacyl-tRNA as in
previous.
The dipeptide on P-site is transferred to A-site forming tripeptide.
This process continues giving long polypeptide chain of aminoacids.

4. Termination:

The peptide bond formation and elongation of polypeptide continues

until stop codon appear on A-site.
If stop codon appear on A-site it is not recognized by t-RNA carrying
aminoacids because stop codon donot have anticodon on mRNA.
The stop codon are recognized by next protein called release factor (Rf-1,
RF-2 and RF-3) which hydrolyses and cause release of all component ie
30s, 50S, mRNA and polypeptide separates.
RF-1 recognisaes UAA and UAg while RF-2 recognises UAA and UGA while
RF-3 dissociate 30S and 50S subunits.
In case of eukaryotes only one release actor eRF causes dissociation.

Post translation modi!cation:

The newly formed polypeptide may not be biologiy functional so it undergoes
several folding and processing known as post translation modi"cation.

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1. Amino terminal and carboxyl terminal

modi!cation:

The N-formylmethionine in case of bacteria is removed from polypeptide

chain and some carboxyl terminal are also removed by enzymatic action
to make functional protein. In case of eukaryotic protein, amino terminal
is N- acetylated.

2. Loss of signal sequences:

In some protein the amino terminal end is cleaved by speci"c peptidase

so that protein loss its signaling property.

3. Modi!cation of individual aminoacids:

The aminoacids may be phosphorylated, acetylated for modi"cation

4. Attachment of carbohydrate side chain:

Carbohydrate side chain is added to make protein functional. Eg,

glycoprotein. Lipoprotein

5. Addition of isoprenyl group:

In some protein, isoprenyl group is added so to make protein active.

References
1. https://courses.lumenlearning.com/microbiology/chapter/protein-
synthesis-translation/
2. https://www.khanacademy.org/science/biology/gene-expression-central-
dogma/translation-polypeptides/a/the-stages-of-translation
3. https://en.wikipedia.org/wiki/Prokaryotic_translation
4. http://vle.du.ac.in/mod/book/print.php?id=13622&chapterid=30273
5. http://www.biologydiscussion.com/cell/prokaryotes/translation-in-
prokaryotes-genetics/38022
6. http://www.sparknotes.com/biology/molecular/translation/section3.rhtml

Translation in Prokaryotes

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! PROTEIN SYNTHESIS PROTEIN SYNTHESIS STEPS

" PREVIOUS
TRANSLATION IN PROKARYOTES
Di!erence between
Prokaryotic and 1
Eukaryotic cell
COMMENT NEXT #
Di!erence between
Prokaryotic and
Dr Dipan Adhikari Eukaryotic translation
JULY 14, 2017 AT 11:54 PM

Really informative and lucidly written

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