ArticleNucleic acids research2014
Distinct tRNA recognition strategies used by a homologous family of editing domains prevent mistranslation.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
- Strategies for detecting aminoacylation and aminoacyl-tRNA editingIsrael journal of chemistry · 2024Article
- Article
- The role of tRNA identity elements in aminoacyl-tRNA editing.Frontiers in microbiology · 2024Review
- Distinct localization of chiral proofreaders resolves organellar translation conflict in plants.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Structural basis of tRNAPro acceptor stem recognition by a bacterial trans-editing domain.Nucleic acids research · 2023Article
- HumanThe Journal of biological chemistry · 2020Article
- Stoichiometry of triple-sieve tRNA editing complex ensures fidelity of aminoacyl-tRNA formation.Nucleic acids research · 2019Article
- Article
- Quality control by trans-editing factor prevents global mistranslation of non-protein amino acid α-aminobutyrate.RNA biology · 2018Article
- A genomically modified Escherichia coli strain carrying an orthogonal E. coli histidyl-tRNA synthetase•tRNABiochimica et biophysica acta. General subjects · 2017Article
- Translational fidelity and mistranslation in the cellular response to stress.Nature microbiology · 2017Review
- Conformational and chemical selection by aProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Specificity and catalysis hardwired at the RNA-protein interface in a translational proofreading enzyme.Nature communications · 2015Article
- The identity of the discriminator base has an impact on CCA addition.Nucleic acids research · 2015Article
- Homologous trans-editing factors with broad tRNA specificity prevent mistranslation caused by serine/threonine misactivation.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Bacterial transfer RNAs.FEMS microbiology reviews · 2015Review
- Ancestral AlaX editing enzymes for control of genetic code fidelity are not tRNA-specific.The Journal of biological chemistry · 2015Article
- Structure of the Pseudomonas aeruginosa transamidosome reveals unique aspects of bacterial tRNA-dependent asparagine biosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Mistranslation of the genetic code.FEBS letters · 2014Review
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Errors in protein synthesis due to mispairing of amino acids with tRNAs jeopardize cell viability. Several checkpoints to prevent formation of Ala- and Cys-tRNA(Pro) have been described, including the Ala-specific editing domain (INS) of most bacterial prolyl-tRNA synthetases (ProRSs) and an autonomous single-domain INS homolog, YbaK, which clears Cys-tRNA(Pro) in trans. In many species where ProRS lacks an INS domain, ProXp-ala, another single-domain INS-like protein, is responsible for editing Ala-tRNA(Pro). Although the amino acid specificity of these editing domains has been established, the role of tRNA sequence elements in substrate selection has not been investigated in detail. Critical recognition elements for aminoacylation by bacterial ProRS include acceptor stem elements G72/A73 and anticodon bases G35/G36. Here, we show that ProXp-ala and INS require these same acceptor stem and anticodon elements, respectively, whereas YbaK lacks inherent tRNA specificity. Thus, these three related domains use divergent approaches to recognize tRNAs and prevent mistranslation. Whereas some editing domains have borrowed aspects of tRNA recognition from the parent aminoacyl-tRNA synthetase, relaxed tRNA specificity leading to semi-promiscuous editing may offer advantages to cells.
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