ArticleProceedings of the National Academy of Sciences of the United States of America2019
Oxidation of phenylalanyl-tRNA synthetase positively regulates translational quality control.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 34 citations in OpenAlex.
- Human aminoacyl-tRNA synthetases as integrators of translation and cell signalling networks.Nature reviews. Molecular cell biology · 2026Review
- Comparative gut microbial enzyme functions in human amoebiasis: Implications for host-microbe interactions and veterinary parasitic models.Open veterinary journal · 2026Article
- Population structure and gene flux ofMicrobial genomics · 2025Article
- Broad-spectrum tolerance to disinfectant-mediated bacterial killing due to mutation of the PheS aminoacyl tRNA synthetase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- From dusty shelves toward the spotlight: growing evidence for Ap4A as an alarmone in maintaining RNA stability and proteostasis.Current opinion in microbiology · 2024Review
- Adaptation of a eukaryote-like ProRS to a prokaryote-like tRNAPro.Nucleic acids research · 2024Article
- Interplay between mistranslation and oxidative stress inArhiv za higijenu rada i toksikologiju · 2024Article
- Methionyl-tRNA synthetase synthetic and proofreading activities are determinants of antibiotic persistence.Frontiers in microbiology · 2024Article
- Genome-wide screening reveals metabolic regulation of stop-codon readthrough by cyclic AMP.Nucleic acids research · 2023Article
- The central role of translation elongation in response to stress.Biochemical Society transactions · 2023Article
- Translational Fidelity during Bacterial Stresses and Host Interactions.Pathogens (Basel, Switzerland) · 2023Review
- Protein family neighborhood analyzer-ProFaNA.PeerJ · 2023Article
- Mutations identified in engineeredFrontiers in microbiology · 2023Article
- Oxidative stress strongly restricts the effect of codon choice on the efficiency of protein synthesis inFrontiers in microbiology · 2022Article
- Oxidation alters the architecture of the phenylalanyl-tRNA synthetase editing domain to confer hyperaccuracy.Nucleic acids research · 2021Article
- Integrated Redox Proteomic Analysis Highlights New Mechanisms of Sensitivity to Silver Nanoparticles.Molecular & cellular proteomics : MCP · 2021Article
- Oxidative Stress in Bacteria and the Central Dogma of Molecular Biology.Frontiers in molecular biosciences · 2021Review
- Fine-Tuning of Alanyl-tRNA Synthetase Quality Control Alleviates Global Dysregulation of the Proteome.Genes · 2020Article
- Nitrosative stress inhibits aminoacylation and editing activities of mitochondrial threonyl-tRNA synthetase by S-nitrosation.Nucleic acids research · 2020Article
- Cross-editing by a tRNA synthetase allows vertebrates to abundantly express mischargeable tRNA without causing mistranslation.Nucleic acids research · 2020Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Accurate translation of the genetic code is maintained in part by aminoacyl-tRNA synthetases (aaRS) proofreading mechanisms that ensure correct attachment of a cognate amino acid to a transfer RNA (tRNA). During environmental stress, such as oxidative stress, demands on aaRS proofreading are altered by changes in the availability of cytoplasmic amino acids. For example, oxidative stress increases levels of cytotoxic tyrosine isomers, noncognate amino acids normally excluded from translation by the proofreading activity of phenylalanyl-tRNA synthetase (PheRS). Here we show that oxidation of PheRS induces a conformational change, generating a partially unstructured protein. This conformational change does not affect Phe or Tyr activation or the aminoacylation activity of PheRS. However, in vitro and ex vivo analyses reveal that proofreading activity to hydrolyze Tyr-tRNA
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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.