The Mechanism of Pre-transfer Editing in Yeast Mitochondrial Threonyl-tRNA Synthetase
journal contributionposted on 22.11.2013 by Jiqiang Ling, Kaitlyn M. Peterson, Ivana Simonović, Dieter Söll, Miljan Simonović
Any type of content formally published in an academic journal, usually following a peer-review process.
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.