ArticleProceedings of the National Academy of Sciences of the United States of America2016
Translation quality control is critical for bacterial responses to amino acid stress.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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42 citing papers in PubMed, 61 citations in OpenAlex.
- Systems-level analysis of 1,6-hexanediol stress response and tolerance engineering inSynthetic and systems biotechnology · 2027Article
- MiaA-mediated tRNA modifications couple tryptophan attenuation and changes in tRNA abundance to complex phenotypes in Pseudomonas aeruginosa.Nucleic acids research · 2026Article
- Bacterial extracellular vesicles as recyclable nutrient reservoirs.Nature communications · 2026Article
- Cost of Altered Translation Accuracy Shapes Adaptation to Antibiotics in E. coli.Molecular biology and evolution · 2025Article
- Bacterial ribosome heterogeneity facilitates rapid response to stress.Journal of bacteriology · 2025Review
- Analysis of stress response in multiple bacterial pathogens using a network biology approach.Scientific reports · 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
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- Translational T-box riboswitches bind tRNA by modulating conformational flexibility.Nature communications · 2024Article
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- Methionyl-tRNA synthetase synthetic and proofreading activities are determinants of antibiotic persistence.Frontiers in microbiology · 2024Article
- Global profiling of ribosomal protein acetylation reveals essentiality of acetylation homeostasis in maintaining ribosome assembly and function.Nucleic acids research · 2023Article
- System-wide optimization of an orthogonal translation system with enhanced biological tolerance.Molecular systems biology · 2023Article
- The tRNA identity landscape for aminoacylation and beyond.Nucleic acids research · 2023Review
- Transcriptome and metabolome profiling to elucidate the mechanism underlying the poor growth ofFrontiers in veterinary science · 2023Article
- Transcriptomic profiling of Escherichia coli K-12 in response to a compendium of stressors.Scientific reports · 2022Article
- Article
- A molecular link between cell wall biosynthesis, translation fidelity, and stringent response inProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Designing next generation recombinant protein expression platforms by modulating the cellular stress response in Escherichia coli.Microbial cell factories · 2020Article
- Charging State Analysis of Transfer RNA from an α-proteobacterium.Bio-protocol · 2020Article
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Gene expression relies on quality control for accurate transmission of genetic information. One mechanism that prevents amino acid misincorporation errors during translation is editing of misacylated tRNAs by aminoacyl-tRNA synthetases. In the absence of editing, growth is limited upon exposure to excess noncognate amino acid substrates and other stresses, but whether these physiological effects result solely from mistranslation remains unclear. To explore if translation quality control influences cellular processes other than protein synthesis, an Escherichia coli strain defective in Tyr-tRNA(Phe) editing was used. In the absence of editing, cellular levels of aminoacylated tRNA(Phe) were elevated during amino acid stress, whereas in the wild-type strain these levels declined under the same growth conditions. In the editing-defective strain, increased levels of aminoacylated tRNA(Phe) led to continued synthesis of the PheL leader peptide and attenuation of pheA transcription under amino acid stress. Consequently, in the absence of editing, activation of the phenylalanine biosynthetic operon becomes less responsive to phenylalanine limitation. In addition to raising aminoacylated tRNA levels, the absence of editing lowered the amount of deacylated tRNA(Phe) in the cell. This reduction in deacylated tRNA was accompanied by decreased synthesis of the second messenger guanosine tetraphosphate and limited induction of stringent response-dependent gene expression in editing-defective cells during amino acid stress. These data show that a single quality-control mechanism, the editing of misacylated aminoacyl-tRNAs, provides a critical checkpoint both for maintaining the accuracy of translation and for determining the sensitivity of transcriptional responses to amino acid stress.
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