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Proofreadingandediting Mechanism During Translation.: Roll No.:12 M.Sc. Zoology 1 Semester

The document summarizes various proofreading and editing mechanisms used during translation to ensure accurate protein synthesis. It discusses how tRNAs and mRNAs are quality controlled, how tRNA synthetases accurately select cognate tRNAs and amino acids using a double sieve mechanism, and how transfer RNA (tmRNA) helps solve the problem of incomplete mRNA in prokaryotes by tagging unfinished proteins for degradation. The conclusion states that proofreading and editing occurs at every step of translation to minimize errors and maintain the fidelity of genetic information being translated into proteins.

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699 views11 pages

Proofreadingandediting Mechanism During Translation.: Roll No.:12 M.Sc. Zoology 1 Semester

The document summarizes various proofreading and editing mechanisms used during translation to ensure accurate protein synthesis. It discusses how tRNAs and mRNAs are quality controlled, how tRNA synthetases accurately select cognate tRNAs and amino acids using a double sieve mechanism, and how transfer RNA (tmRNA) helps solve the problem of incomplete mRNA in prokaryotes by tagging unfinished proteins for degradation. The conclusion states that proofreading and editing occurs at every step of translation to minimize errors and maintain the fidelity of genetic information being translated into proteins.

Uploaded by

Paresh
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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PROOFREADING AND EDITING

MECHANISM DURING TRANSLATION.


By
Yengkhom Paresh Kumar
Roll no. :12
M.Sc. Zoology 1st Semester
Under the supervision of
Ma’am O. Sangita Devi
INTRODUCTION
• Proofreading and editing mechanisms are used throughout
protein synthesis to ensure faithful translation of genetic
information.
• Various quality control mechanisms are employed to assure the
fidelity of translation.
ACCURACY IS MAINTAINED AT EVERY STEP.

• The maturation of tRNAs and mRNAs is monitored,


as is the identity of amino acids attached to tRNAs.

• The exact matching of tRNA with their


corresponding cognate amino acids is checked.

• Accuracy is further enhanced during the selection


of aminoacyl tRNAs on the ribosome and their
base pairing with the mRNA.
QUALITY CONTROL DURING SELECTION
t OF
t RNA SYNTHETASES.
RNAS BY
• The structural diversity presented by the different combination of
bases in tRNAs ensures that the cognate molecules can be
specifically selected by the aminoacyl tRNA.

• The enzyme contains three nucleotide binding pockets,each of


which is complementary in shape and charge to the nucleotide
in the anticodon.

• Competition between enzymes for their cognate tRNAs


enhance accuracy of tRNA selection
QUALITY CONTROL DURING CHARGING OF
t
RNA
• Charging of tRNAs with correct amino acids is important.

• There is difficulty in discriminating similar amino acids, amino


acids being considerably less complex in structure .

• These selection of cognate amino acids is performed by


tRNA synthetases in a two step mechanism which presents a
double sieve model.

• The molecular mechanism underlying the proofreading


activity is best demonstrated in the recognition of isoleucine
versus valine by isoleucyl-tRNA synthetase.
DOUBLE SIEVE MECHANISM
tRNA
1st Sieve is coarse excluding amino
acids too big
synthetase
• It excludes amino acids larger than the cognate amino
contains two acids but unable to exclude the closely similar and
distinct smaller amino acids .
catalytic sites • Amino acids are activated at the Active site.
Viz; Active
site and 2nd Sieve is fine, degrades amino acids
Editing site too small.
that presents • The Editing site allows acess to closely related amino
acids but excluding Athe cognate one.
a double
• The non-cognate amino acids are hydrolysed at the
sieve during editing site.
substrate • Enzyme transfers the activated amino acid to its cognate
selection. tRNA.
tRNA synthetase showing its catalytic
sites and aminoacylation of tRNA.
tm RNA SOLVES THE PROBLEM OF
m
INCOMPLETE RNA IN PROKARYOTES
• tmRNA contains two functional domains ; one that mimics a part of
tRNA and the other that of an mRNA.

• When a bacterial ribosome translates an incomplete mRNA, the


tmRNA enters the A-site of the ribosome mimicking a tRNA and itself
gets translated encoding a short polypeptide.

• The translation of its mRNA domain adds a special amino acid tag to
the C-terminus of the protein.

• This tag is a recognition sequence of a number of proteases that will


degrade the entire protein.
CONCLUSION
• The cell places a high priority on ensuring that translation
produces proteins that accurately reflects the corresponding
genetic information.

• Proofreading and Editing activities can be seen at every step


where errors might accumulate. These mechanisms share a
common feature which is to prevent naturally occurring
mistakes.

These phenomenal activities answers how a cell manage to


make few errors during protein synthesis.
THANK YOU
THANK YOU

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