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The Mechanism of Pre-transfer Editing in Yeast Mitochondrial Threonyl-tRNA Synthetase

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posted on 2013-11-22, 00:00 authored by Jiqiang Ling, Kaitlyn M. Peterson, Ivana Simonović, Dieter Söll, Miljan Simonović
Background: 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 Biology

Publisher

American Society for Biochemistry and Molecular Biology

Language

  • en_US

issn

0021-9258

Issue date

2012-08-01

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    Keywords

    Proofreadingtranslational quality controlX-ray crystallography

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