ArticleThe Journal of biological chemistry2012
The mechanism of pre-transfer editing in yeast mitochondrial threonyl-tRNA synthetase.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Mammalian mitochondrial translation infidelity leads to oxidative stress-induced cell cycle arrest and cardiomyopathy.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Nitrosative stress inhibits aminoacylation and editing activities of mitochondrial threonyl-tRNA synthetase by S-nitrosation.Nucleic acids research · 2020Article
- Cross-editing by a tRNA synthetase allows vertebrates to abundantly express mischargeable tRNA without causing mistranslation.Nucleic acids research · 2020Article
- Rewiring protein synthesis: From natural to synthetic amino acids.Biochimica et biophysica acta. General subjects · 2017Review
- The pimeloyl-CoA synthetase BioW defines a new fold for adenylate-forming enzymes.Nature chemical biology · 2017Article
- Multiple Quality Control Pathways Limit Non-protein Amino Acid Use by Yeast Cytoplasmic Phenylalanyl-tRNA Synthetase.The Journal of biological chemistry · 2016Article
- The crystal structure of yeast mitochondrial ThrRS in complex with the canonical threonine tRNA.Nucleic acids research · 2016Article
- Trans-oligomerization of duplicated aminoacyl-tRNA synthetases maintains genetic code fidelity under stress.Nucleic acids research · 2015Article
- The tRNA A76 Hydroxyl Groups Control Partitioning of the tRNA-dependent Pre- and Post-transfer Editing Pathways in Class I tRNA Synthetase.The Journal of biological chemistry · 2015Article
- Protein mistranslation protects bacteria against oxidative stress.Nucleic acids research · 2015Article
- Article
- A minimalist mitochondrial threonyl-tRNA synthetase exhibits tRNA-isoacceptor specificity during proofreading.Nucleic acids research · 2014Article
- Mistranslation of the genetic code.FEBS letters · 2014Review
- Determinants for tRNA-dependent pretransfer editing in the synthetic site of isoleucyl-tRNA synthetase.Biochemistry · 2014Article
- The physiological target for LeuRS translational quality control is norvaline.The EMBO journal · 2014Article
- Mechanism of oxidant-induced mistranslation by threonyl-tRNA synthetase.Nucleic acids research · 2014Article
- Emergence and evolution.Topics in current chemistry · 2014Review
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Authors and funding
5 authors.
Funding
Abstract
Accurate translation of mRNA into protein is a fundamental biological process critical for maintaining normal cellular functions. To ensure translational fidelity, aminoacyl-tRNA synthetases (aaRSs) employ pre-transfer and post-transfer editing activities to hydrolyze misactivated and mischarged amino acids, respectively. Whereas post-transfer editing, which requires either a specialized domain in aaRS or a trans-protein factor, is well described, the mechanism of pre-transfer editing is less understood. Here, we show that yeast mitochondrial threonyl-tRNA synthetase (MST1), which lacks an editing domain, utilizes pre-transfer editing to discriminate against serine. MST1 misactivates serine and edits seryl adenylate (Ser-AMP) in a tRNA-independent manner. MST1 hydrolyzes 80% of misactivated Ser-AMP at a rate 4-fold higher than that for the cognate threonyl adenylate (Thr-AMP) while releasing 20% of Ser-AMP into the solution. To understand the mechanism of pre-transfer editing, we solved the crystal structure of MST1 complexed with an analog of Ser-AMP. The binding of the Ser-AMP analog to MST1 induces conformational changes in the aminoacylation active site, and it positions a potential hydrolytic water molecule more favorably for nucleophilic attack. In addition, inhibition results reveal that the Ser-AMP analog binds the active site 100-fold less tightly than the Thr-AMP analog. In conclusion, we propose that the plasticity of the aminoacylation site in MST1 allows binding of Ser-AMP and the appropriate positioning of the hydrolytic water molecule.
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