ArticleThe Journal of biological chemistry2012
Kinetic partitioning between synthetic and editing pathways in class I aminoacyl-tRNA synthetases occurs at both pre-transfer and post-transfer hydrolytic steps.
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 28 papers.
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Who cites it
28 citing papers in PubMed, 55 citations in OpenAlex.
- The ZN domain acts as a dynamic switch coordinating multiple-step aminoacylation in bacterial leucyl-tRNA synthetase.Nucleic acids research · 2026Article
- Mechanisms and kinetic assays of aminoacyl-tRNA synthetases.FEBS letters · 2025Review
- Time-Dependent Inhibition of Leucyl-tRNA-Synthetase (LeuRS): Insight into Target Vulnerability.ACS infectious diseases · 2025Article
- Kinetic characterization of amino acid activation by aminoacyl-tRNA synthetases using radiolabelled γ-[FEBS open bio · 2025Article
- Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip.Communications biology · 2022Article
- Negative catalysis by the editing domain of class I aminoacyl-tRNA synthetases.Nucleic acids research · 2022Article
- A Leucyl-tRNA Synthetase Urzyme: Authenticity of tRNA Synthetase Catalytic Activities and Promiscuous Phosphorylation of Leucyl-5'AMP.International journal of molecular sciences · 2022Article
- The energy cost and optimal design of networks for biological discrimination.Journal of the Royal Society, Interface · 2022Article
- A novel fluorescent reporter sensitive to serine mis-incorporation.RNA biology · 2022Article
- Bypassing the requirement for aminoacyl-tRNA by a cyclodipeptide synthase enzyme.RSC chemical biology · 2021Article
- Fine-Tuning of Alanyl-tRNA Synthetase Quality Control Alleviates Global Dysregulation of the Proteome.Genes · 2020Article
- Self-protective responses to norvaline-induced stress in a leucyl-tRNA synthetase editing-deficient yeast strain.Nucleic acids research · 2017Article
- Article
- Discovery and Investigation of Natural Editing Function against Artificial Amino Acids in Protein Translation.ACS central science · 2017Article
- Proteome-wide measurement of non-canonical bacterial mistranslation by quantitative mass spectrometry of protein modifications.Scientific reports · 2016Article
- Elongation Factor Tu Prevents Misediting of Gly-tRNA(Gly) Caused by the Design Behind the Chiral Proofreading Site of D-Aminoacyl-tRNA Deacylase.PLoS biology · 2016Article
- 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
- EF-Tu dynamics during pre-translocation complex formation: EF-Tu·GDP exits the ribosome via two different pathways.Nucleic acids research · 2015Article
- MD Simulations of tRNA and Aminoacyl-tRNA Synthetases: Dynamics, Folding, Binding, and Allostery.International journal of molecular sciences · 2015Review
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
Comprehensive steady-state and transient kinetic studies of the synthetic and editing activities of Escherichia coli leucyl-tRNA synthetase (LeuRS) demonstrate that the enzyme depends almost entirely on post-transfer editing to endow the cell with specificity against incorporation of norvaline into protein. Among the three class I tRNA synthetases possessing a dedicated post-transfer editing domain (connective peptide 1; CP1 domain), LeuRS resembles valyl-tRNA synthetase in its reliance on post-transfer editing, whereas isoleucyl-tRNA synthetase differs in retaining a distinct tRNA-dependent synthetic site pre-transfer editing activity to clear noncognate amino acids before misacylation. Further characterization of the post-transfer editing activity in LeuRS by single-turnover kinetics demonstrates that the rate-limiting step is dissociation of deacylated tRNA and/or amino acid product and highlights the critical role of a conserved aspartate residue in mediating the first-order hydrolytic steps on the enzyme. Parallel analyses of adenylate and aminoacyl-tRNA formation reactions by wild-type and mutant LeuRS demonstrate that the efficiency of post-transfer editing is controlled by kinetic partitioning between hydrolysis and dissociation of misacylated tRNA and shows that trans editing after rebinding is a competent kinetic pathway. Together with prior analyses of isoleucyl-tRNA synthetase and valyl-tRNA synthetase, these experiments provide the basis for a comprehensive model of editing by class I tRNA synthetases, in which kinetic partitioning plays an essential role at both pre-transfer and post-transfer steps.
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