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