1/1
The Mechanism of Pre-transfer Editing in Yeast Mitochondrial Threonyl-tRNA Synthetase
journal contribution
posted on 2013-11-22, 00:00 authored by Jiqiang Ling, Kaitlyn M. Peterson, Ivana Simonović, Dieter Söll, Miljan SimonovićBackground: The mechanism of pre-transfer
editing by which aaRSs regulate translational
fidelity is not well understood.
Results: Yeast mitochondrial ThrRS, MST1,
hydrolyzes seryl adenylate at the aminoacylation
active site more rapidly than the cognate
threonyl adenylate.
Conclusion: MST1 discriminates against serine
and reduces mischarging of threonine tRNA by
employing pre-transfer editing.
Significance: The mechanism of misactivation
and pre-transfer editing of serine by ThrRS is
provided.
Funding
This work was supported by a grant GM22854 from the National Institute of General Medical Sciences (to D.S.), and by grants from the National Institute of General Medical Sciences and the American Cancer Society, Illinois Division, Inc. (to M.S.).
History
Publisher Statement
This research was originally published in Journal of Biological Chemistry. Ling JQ, Peterson KM, Simonovic I, Soll D, Simonovic M. The Mechanism of Pre-transfer Editing in Yeast Mitochondrial Threonyl-tRNA Synthetase. Journal of Biological Chemistry. Aug 2012;287(34):28518-28525. © the American Society for Biochemistry and Molecular BiologyPublisher
American Society for Biochemistry and Molecular BiologyLanguage
- en_US