ArticleNucleic acids research2011
Role of tRNA amino acid-accepting end in aminoacylation and its quality control.
Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Automated prototyping of genetic codes.Nature · 2026Article
- 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
- Human lysyl-tRNA synthetase evolves a dynamic structure that can be stabilized by forming complex.Cellular and molecular life sciences : CMLS · 2022Article
- Article
- LeuRS can leucylate type I and type II tRNALeus in Streptomyces coelicolor.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
- Editing activity for eliminating mischarged tRNAs is essential in mammalian mitochondria.Nucleic acids research · 2018Article
- Vibrio natriegens as a fast-growing host for molecular biology.Nature methods · 2016Article
- A Human Disease-causing Point Mutation in Mitochondrial Threonyl-tRNA Synthetase Induces Both Structural and Functional Defects.The Journal of biological chemistry · 2016Article
- C-terminal Domain of Leucyl-tRNA Synthetase from Pathogenic Candida albicans Recognizes both tRNASer and tRNALeu.The Journal of biological chemistry · 2016Article
- 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
- Recent developments of engineered translational machineries for the incorporation of non-canonical amino acids into polypeptides.International journal of molecular sciences · 2015Review
- 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
- An orthogonal ribosome-tRNA pair via engineering of the peptidyl transferase center.Nature chemical biology · 2014Article
- Coexistence of bacterial leucyl-tRNA synthetases with archaeal tRNA binding domains that distinguish tRNA(Leu) in the archaeal mode.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
- Leucine-specific domain modulates the aminoacylation and proofreading functional cycle of bacterial leucyl-tRNA synthetase.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
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7 authors.
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Abstract
Aminoacyl-tRNA synthetases (aaRSs) are remarkable enzymes that are in charge of the accurate recognition and ligation of amino acids and tRNA molecules. The greatest difficulty in accurate aminoacylation appears to be in discriminating between highly similar amino acids. To reduce mischarging of tRNAs by non-cognate amino acids, aaRSs have evolved an editing activity in a second active site to cleave the incorrect aminoacyl-tRNAs. Editing occurs after translocation of the aminoacyl-CCA₇₆ end to the editing site, switching between a hairpin and a helical conformation for aminoacylation and editing. Here, we studied the consequence of nucleotide changes in the CCA₇₆ accepting end of tRNA(Leu) during the aminoacylation and editing reactions. The analysis showed that the terminal A₇₆ is essential for both reactions, suggesting that critical interactions occur in the two catalytic sites. Substitutions of C₇₄ and C₇₅ selectively decreased aminoacylation keeping nearly unaffected editing. These mutations might favor the regular helical conformation required to reach the editing site. Mutating the editing domain residues that contribute to CCA₇₆ binding reduced the aminoacylation fidelity leading to cell-toxicity in the presence of non-cognate amino acids. Collectively, the data show how protein synthesis quality is controlled by the CCA₇₆ homogeneity of tRNAs.
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