ArticleProceedings of the National Academy of Sciences of the United States of America2008
CP1-dependent partitioning of pretransfer and posttransfer editing in leucyl-tRNA synthetase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 75 citations in OpenAlex.
- Partitioning of the initial catalytic steps of leucyl-tRNA synthetase is driven by an active site peptide-plane flip.Communications biology · 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
- Reciprocally-Coupled Gating: Strange Loops in Bioenergetics, Genetics, and Catalysis.Biomolecules · 2021Review
- Aminoacyl-tRNA synthetases.RNA (New York, N.Y.) · 2020Review
- Deciphering the interaction of benzoxaborole inhibitor AN2690 with connective polypeptide 1 (CP1) editing domain ofJournal of biosciences · 2020Article
- Translational Control using an Expanded Genetic Code.International journal of molecular sciences · 2019Review
- Stoichiometry of triple-sieve tRNA editing complex ensures fidelity of aminoacyl-tRNA formation.Nucleic acids research · 2019Article
- Conditional accumulation of toxic tRNAs to cause amino acid misincorporation.Nucleic acids research · 2018Article
- Translation system engineering in Escherichia coli enhances non-canonical amino acid incorporation into proteins.Biotechnology and bioengineering · 2017Article
- 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
- The physiological target for LeuRS translational quality control is norvaline.The EMBO journal · 2014Article
- Human tRNA synthetase catalytic nulls with diverse functions.Science (New York, N.Y.) · 2014Article
- Mechanism of oxidant-induced mistranslation by threonyl-tRNA synthetase.Nucleic acids research · 2014Article
- Upgrading protein synthesis for synthetic biology.Nature chemical biology · 2013Article
- Leucyl-tRNA synthetase editing domain functions as a molecular rheostat to control codon ambiguity in Mycoplasma pathogens.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Kinetic proofreading at single molecular level: aminoacylation of tRNA(Ile) and the role of water as an editor.PloS one · 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
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4 authors at 1 institution in 1 country.
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Abstract
Mistranslation is toxic to bacterial and mammalian cells and can lead to neurodegeneration in the mouse. Mistranslation is caused by the attachment of the wrong amino acid to a specific tRNA. Many aminoacyl-tRNA synthetases have an editing activity that deacylates the mischarged amino acid before capture by the elongation factor and transport to the ribosome. For class I tRNA synthetases, the editing activity is encoded by the CP1 domain, which is distinct from the active site for aminoacylation. What is not clear is whether the enzymes also have an editing activity that is separable from CP1. A point mutation in CP1 of class I leucyl-tRNA synthetase inactivates deacylase activity and produces misacylated tRNA. In contrast, although deletion of the entire CP1 domain also disabled the deacylase activity, the deletion-bearing enzyme produced no mischarged tRNA. Further investigation showed that a second tRNA-dependent activity prevented misacylation and is intrinsic to the active site for aminoacylation.
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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.