ArticleThe Journal of biological chemistry2010
tRNA-dependent pre-transfer editing by prokaryotic leucyl-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 34 papers.
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Who cites it
34 citing papers in PubMed, 52 citations in OpenAlex.
- Bioprospecting Chromobacterium violaceum for bioremediation: an alternative to environmental lead pollution.World journal of microbiology & biotechnology · 2026Article
- Deciphering the interaction of benzoxaborole inhibitor AN2690 with connective polypeptide 1 (CP1) editing domain ofJournal of biosciences · 2020Article
- The G3-U70-independent tRNA recognition by human mitochondrial alanyl-tRNA synthetase.Nucleic acids research · 2019Article
- A natural non-Watson-Crick base pair in human mitochondrial tRNAThr causes structural and functional susceptibility to local mutations.Nucleic acids research · 2018Article
- Self-protective responses to norvaline-induced stress in a leucyl-tRNA synthetase editing-deficient yeast strain.Nucleic acids research · 2017Article
- Acetylation of lysine ϵ-amino groups regulates aminoacyl-tRNA synthetase activity inThe Journal of biological chemistry · 2017Article
- Translational Quality Control by Bacterial Threonyl-tRNA Synthetases.The Journal of biological chemistry · 2016Article
- Multiple Quality Control Pathways Limit Non-protein Amino Acid Use by Yeast Cytoplasmic Phenylalanyl-tRNA Synthetase.The Journal of biological chemistry · 2016Article
- Proteome-wide measurement of non-canonical bacterial mistranslation by quantitative mass spectrometry of protein modifications.Scientific reports · 2016Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Degenerate connective polypeptide 1 (CP1) domain from human mitochondrial leucyl-tRNA synthetase.The Journal of biological chemistry · 2015Article
- Modulation of Aminoacylation and Editing Properties of Leucyl-tRNA Synthetase by a Conserved Structural Module.The Journal of biological chemistry · 2015Article
- Identification of lethal mutations in yeast threonyl-tRNA synthetase revealing critical residues in its human homolog.The Journal of biological chemistry · 2015Article
- A minimalist mitochondrial threonyl-tRNA synthetase exhibits tRNA-isoacceptor specificity during proofreading.Nucleic acids research · 2014Article
- Mistranslation of the genetic code.FEBS letters · 2014Review
- A bridge between the aminoacylation and editing domains of leucyl-tRNA synthetase is crucial for its synthetic activity.RNA (New York, N.Y.) · 2014Article
- Syn5 RNA polymerase synthesizes precise run-off RNA products.Nucleic acids research · 2014Article
- Aminoacylation and translational quality control strategy employed by leucyl-tRNA synthetase from a human pathogen with genetic code ambiguity.Nucleic acids research · 2013Article
- The Yin and Yang of tRNA: proper binding of acceptor end determines the catalytic balance of editing and aminoacylation.Nucleic acids research · 2013Article
- Leucine-specific domain modulates the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase.Nucleic acids research · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To prevent genetic code ambiguity due to misincorporation of amino acids into proteins, aminoacyl-tRNA synthetases have evolved editing activities to eliminate intermediate or final non-cognate products. In this work we studied the different editing pathways of class Ia leucyl-tRNA synthetase (LeuRS). Different mutations and experimental conditions were used to decipher the editing mechanism, including the recently developed compound AN2690 that targets the post-transfer editing site of LeuRS. The study emphasizes the crucial importance of tRNA for the pre- and post-transfer editing catalysis. Both reactions have comparable efficiencies in prokaryotic Aquifex aeolicus and Escherichia coli LeuRSs, although the E. coli enzyme favors post-transfer editing, whereas the A. aeolicus enzyme favors pre-transfer editing. Our results also indicate that the entry of the CCA-acceptor end of tRNA in the editing domain is strictly required for tRNA-dependent pre-transfer editing. Surprisingly, this editing reaction was resistant to AN2690, which inactivates the enzyme by forming a covalent adduct with tRNA(Leu) in the post-transfer editing site. Taken together, these data suggest that the binding of tRNA in the post-transfer editing conformation confers to the enzyme the capacity for pre-transfer editing catalysis, regardless of its capacity to catalyze post-transfer editing.
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