ArticleThe Journal of biological chemistry2014
Reduced amino acid specificity of mammalian tyrosyl-tRNA synthetase is associated with elevated mistranslation of Tyr codons.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 27 citations in OpenAlex.
- Article
- Comparison of enriched charge variants from different anti-CD3 bispecific antibodies reveals differential susceptibility of each bispecific arm to post-translational modification.Protein science : a publication of the Protein Society · 2025Article
- Simultaneous determination of cytosolic aminoacyl-tRNA synthetase activities by LC-MS/MS.Nucleic acids research · 2024Article
- Mistranslation of the genetic code by a new family of bacterial transfer RNAs.The Journal of biological chemistry · 2023Article
- Eukaryotic tRNA sequences present conserved and amino acid-specific structural signatures.Nucleic acids research · 2022Article
- Article
- Chemical-Genetic Interactions with the Proline Analog L-Azetidine-2-Carboxylic Acid inG3 (Bethesda, Md.) · 2020Article
- Errors in translational decoding: tRNA wobbling or misincorporation?PLoS genetics · 2019Review
- Compound heterozygosity for loss-of-function FARSB variants in a patient with classic features of recessive aminoacyl-tRNA synthetase-related disease.Human mutation · 2018Article
- Visualizing tRNA-dependent mistranslation in human cells.RNA biology · 2018Article
- Function and origin of mistranslation in distinct cellular contexts.Critical reviews in biochemistry and molecular biology · 2017Review
- Multiple Quality Control Pathways Limit Non-protein Amino Acid Use by Yeast Cytoplasmic Phenylalanyl-tRNA Synthetase.The Journal of biological chemistry · 2016Article
- Article
- Mistranslation of the genetic code.FEBS letters · 2014Review
- Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Quality control operates at different steps in translation to limit errors to approximately one mistranslated codon per 10,000 codons during mRNA-directed protein synthesis. Recent studies have suggested that error rates may actually vary considerably during translation under different growth conditions. Here we examined the misincorporation of Phe at Tyr codons during synthesis of a recombinant antibody produced in tyrosine-limited Chinese hamster ovary (CHO) cells. Tyr to Phe replacements were previously found to occur throughout the antibody at a rate of up to 0.7% irrespective of the identity or context of the Tyr codon translated. Despite this comparatively high mistranslation rate, no significant change in cellular viability was observed. Monitoring of Phe and Tyr levels revealed that changes in error rates correlated with changes in amino acid pools, suggesting that mischarging of tRNA(Tyr) with noncognate Phe by tyrosyl-tRNA synthetase was responsible for mistranslation. Steady-state kinetic analyses of CHO cytoplasmic tyrosyl-tRNA synthetase revealed a 25-fold lower specificity for Tyr over Phe as compared with previously characterized bacterial enzymes, consistent with the observed increase in translation error rates during tyrosine limitation. Functional comparisons of mammalian and bacterial tyrosyl-tRNA synthetase revealed key differences at residues responsible for amino acid recognition, highlighting differences in evolutionary constraints for translation quality control.
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