ArticleMethods (San Diego, Calif.)2008
In vitro assays for the determination of aminoacyl-tRNA synthetase editing activity.
Article in Methods (San Diego, Calif.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed.
- Strategies for detecting aminoacylation and aminoacyl-tRNA editingIsrael journal of chemistry · 2024Article
- The 3'tsRNAs are aminoacylated: Implications for their biogenesis.PLoS genetics · 2021Article
- Exploiting evolutionary trade-offs for posttreatment management of drug-resistant populations.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Deciphering the interaction of benzoxaborole inhibitor AN2690 with connective polypeptide 1 (CP1) editing domain ofJournal of biosciences · 2020Article
- Non-equilibrium dynamics of a nascent polypeptide during translation suppress its misfolding.Nature communications · 2019Article
- A continuous assay for monitoring the synthetic and proofreading activities of multiple aminoacyl-tRNA synthetases for high-throughput drug discovery.RNA biology · 2018Article
- Quality control by trans-editing factor prevents global mistranslation of non-protein amino acid α-aminobutyrate.RNA biology · 2018Article
- Double mimicry evades tRNA synthetase editing by toxic vegetable-sourced non-proteinogenic amino acid.Nature communications · 2017Article
- Aminoacyl-tRNA synthetases.Methods (San Diego, Calif.) · 2017Article
- A conserved proline triplet in Val-tRNA synthetase and the origin of elongation factor P.Cell reports · 2014Article
- Revisiting the biosynthesis of dehydrophos reveals a tRNA-dependent pathway.Proceedings of the National Academy of Sciences of the United States of America · 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
- Coordination of tRNA synthetase active sites for chemical fidelity.The Journal of biological chemistry · 2012Article
- Article
- Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.The Journal of biological chemistry · 2010Article
- Discovery and investigation of misincorporation of serine at asparagine positions in recombinant proteins expressed in Chinese hamster ovary cells.The Journal of biological chemistry · 2009Article
- Architectural underpinnings of the genetic code for glutamine.Biochemistry · 2009Article
- DNA polymerases and aminoacyl-tRNA synthetases: shared mechanisms for ensuring the fidelity of gene expression.Biochemistry · 2008Review
- tRNA synthetase: tRNA aminoacylation and beyond.Wiley interdisciplinary reviews. RNAReview
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Authors and funding
4 authors.
Funding
Abstract
Aminoacyl-tRNA synthetases are essential enzymes that help to ensure the fidelity of protein translation by accurately aminoacylating (or "charging") specific tRNA substrates with cognate amino acids. Many synthetases have an additional catalytic activity to confer amino acid editing or proofreading. This activity relieves ambiguities during translation of the genetic code that result from one synthetase activating multiple amino acid substrates. In this review, we describe methods that have been developed for assaying both pre- and post-transfer editing activities. Pre-transfer editing is defined as hydrolysis of a misactivated aminoacyl-adenylate prior to transfer to the tRNA. This reaction has been reported to occur either in the aminoacylation active site or in a separate editing domain. Post-transfer editing refers to the hydrolysis reaction that cleaves the aminoacyl-ester linkage formed between the carbonyl carbon of the amino acid and the 2' or 3' hydroxyl group of the ribose on the terminal adenosine. Post-transfer editing takes place in a hydrolytic active site that is distinct from the site of amino acid activation. Here, we focus on methods for determination of steady-state reaction rates using editing assays developed for both classes of synthetases.
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