ArticleThe Journal of biological chemistry2010
Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed, 57 citations in OpenAlex.
- Coordination between aminoacylation and editing to protect against proteotoxicity.Nucleic acids research · 2023Article
- Impedance Matching and the Choice Between Alternative Pathways for the Origin of Genetic Coding.International journal of molecular sciences · 2020Article
- Aminoacyl-tRNA synthetases.RNA (New York, N.Y.) · 2020Review
- Progress and challenges in aminoacyl-tRNA synthetase-based therapeutics.The Journal of biological chemistry · 2019Review
- 11th IUBMB Focused Meeting on the Aminoacyl-tRNA Synthetases: Sailing a New Sea of Complex Functions in Human Biology and Disease.Biomolecules · 2018Article
- The pimeloyl-CoA synthetase BioW defines a new fold for adenylate-forming enzymes.Nature chemical biology · 2017Article
- Aminoacyl-tRNA synthetases.Methods (San Diego, Calif.) · 2017Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Naturally Occurring Isoleucyl-tRNA Synthetase without tRNA-dependent Pre-transfer Editing.The Journal of biological chemistry · 2016Article
- A Human Disease-causing Point Mutation in Mitochondrial Threonyl-tRNA Synthetase Induces Both Structural and Functional Defects.The Journal of biological chemistry · 2016Article
- 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
- 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
- Translational fidelity maintenance preventing Ser mis-incorporation at Thr codon in protein from eukaryote.Nucleic acids research · 2013Article
- Rational design and directed evolution of a bacterial-type glutaminyl-tRNA synthetase precursor.Nucleic acids research · 2012Article
- The mechanism of pre-transfer editing in yeast mitochondrial threonyl-tRNA synthetase.The Journal of biological chemistry · 2012Article
- Kinetic partitioning between synthetic and editing pathways in class I aminoacyl-tRNA synthetases occurs at both pre-transfer and post-transfer hydrolytic steps.The Journal of biological chemistry · 2012Article
- Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignment.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Amino-acid-dependent shift in tRNA synthetase editing mechanisms.Journal of the American Chemical Society · 2011Article
- The α-amino group of the threonine substrate as the general base during tRNA aminoacylation: a new version of substrate-assisted catalysis predicted by hybrid DFT.The journal of physical chemistry. A · 2011Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
Abstract
Aminoacyl-tRNA synthetases hydrolyze aminoacyl adenylates and aminoacyl-tRNAs formed from near-cognate amino acids, thereby increasing translational fidelity. The contributions of pre- and post-transfer editing pathways to the fidelity of Escherichia coli threonyl-tRNA synthetase (ThrRS) were investigated by rapid kinetics. In the pre-steady state, asymmetric activation of cognate threonine and noncognate serine was observed in the active sites of dimeric ThrRS, with similar rates of activation. In the absence of tRNA, seryl-adenylate was hydrolyzed 29-fold faster by the ThrRS catalytic domain than threonyl-adenylate. The rate of seryl transfer to cognate tRNA was only 2-fold slower than threonine. Experiments comparing the rate of ATP consumption to the rate of aminoacyl-tRNA(AA) formation demonstrated that pre-transfer hydrolysis contributes to proofreading only when the rate of transfer is slowed significantly. Thus, the relative contributions of pre- and post-transfer editing in ThrRS are subject to modulation by the rate of aminoacyl transfer.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.