Hydrolysis of non-cognate aminoacyl-adenylates by a class II aminoacyl-tRNA synthetase lacking an editing domain

Aminoacyl-tRNA synthetases, a group of enzymes catalyzing aminoacyl-tRNA formation, may possess inherent editing activity to clear mistakes arising through the selection of non-cognate amino acid. It is generally assumed that both editing substrates, non-cognate aminoacyl-adenylate and misacylated t...

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Bibliographic Details
Published in:FEBS letters 2007-10, Vol.581 (26), p.5110-5114
Main Authors: Gruic-Sovulj, Ita, Rokov-Plavec, Jasmina, Weygand-Durasevic, Ivana
Format: Article
Language:English
Subjects:
aaRS
Adenosine Monophosphate - chemistry
Aminoacyl-adenylate hydrolysis
aminoacyl-tRNA synthetase with amino acids representing Ser, Gln, Phe, Pro, Thr, Ala, Val and Leu thus for seryl-, glutaminyl-, phenylalanyl-, prolyl-, threonyl-, alanyl-, valyl- and leucyl-tRNA synthetase
Binding Sites
Cysteine - chemistry
Escherichia coli
Escherichia coli Proteins - chemistry
Escherichia coli Proteins - genetics
Hydrolysis
Kinetic proofreading
PPi
Pre-transfer editing
Protein Structure, Tertiary
pyrophosphate
RNA Editing
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - genetics
Sc-, Ec- and Tt-SerRS
SerHX
Serine - analogs & derivatives
Serine - chemistry
serine hydroxamate
Serine-tRNA Ligase - chemistry
Serine-tRNA Ligase - genetics
Seryl-tRNA synthetase
seryl-tRNA synthetase from Saccharomyces cerevisiae, Escherichia coli and Thermus thermophilus, respectively
Substrate Specificity
Thermus thermophilus
Threonine - chemistry
tRNA-independent pre-transfer editing
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Summary:Aminoacyl-tRNA synthetases, a group of enzymes catalyzing aminoacyl-tRNA formation, may possess inherent editing activity to clear mistakes arising through the selection of non-cognate amino acid. It is generally assumed that both editing substrates, non-cognate aminoacyl-adenylate and misacylated tRNA, are hydrolyzed at the same editing domain, distant from the active site. Here, we present the first example of an aminoacyl-tRNA synthetase (seryl-tRNA synthetase) that naturally lacks an editing domain, but possesses a hydrolytic activity toward non-cognate aminoacyl-adenylates. Our data reveal that tRNA-independent pre-transfer editing may proceed within the enzyme active site without shuttling the non-cognate aminoacyl-adenylate intermediate to the remote editing site.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2007.09.058