ArticleNucleic acids research2016
Temperature dependent mistranslation in a hyperthermophile adapts proteins to lower temperatures.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 58 citations in OpenAlex.
- Article
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- Protein aggregation as a bistable switch in bacterial cell fate: from adaptive dormancy to cytotoxic death.Frontiers in microbiology · 2026Review
- Reduced Amino Acid Substitution Matrices Find Traces of Ancient Coding Alphabets in Modern Day Proteins.Molecular biology and evolution · 2025Article
- Article
- Genome-wide impact of codon usage bias on translation optimization in Drosophila melanogaster.Nature communications · 2024Article
- Oxidative Stress, Transfer RNA Metabolism, and Protein Synthesis.Antioxidants & redox signaling · 2024Review
- Article
- Methylated guanosine and uridine modifications inRSC chemical biology · 2023Article
- Alternative CUG Codon Usage in the Halotolerant YeastJournal of fungi (Basel, Switzerland) · 2022Article
- Increase in Ribosomal Fidelity BenefitsGenes · 2022Article
- Regulating Expression of Mistranslating tRNAs by Readthrough RNA Polymerase II Transcription.ACS synthetic biology · 2021Article
- Role of a cryptic tRNA gene operon in survival under translational stress.Nucleic acids research · 2021Article
- A molecular-level perspective on the frequency, distribution, and consequences of messenger RNA modifications.Wiley interdisciplinary reviews. RNA · 2020Review
- Premature termination codon readthrough in Drosophila varies in a developmental and tissue-specific manner.Scientific reports · 2020Article
- Duplication of leucyl-tRNA synthetase in an archaeal extremophile may play a role in adaptation to variable environmental conditions.The Journal of biological chemistry · 2020Article
- Pseudouridinylation of mRNA coding sequences alters translation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Increased mistranslation protects E. coli from protein misfolding stress due to activation of a RpoS-dependent heat shock response.FEBS letters · 2019Article
- Modulating Mistranslation Potential of tRNAGenetics · 2019Article
- Conditional accumulation of toxic tRNAs to cause amino acid misincorporation.Nucleic acids research · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
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Abstract
All organisms universally encode, synthesize and utilize proteins that function optimally within a subset of growth conditions. While healthy cells are thought to maintain high translational fidelity within their natural habitats, natural environments can easily fluctuate outside the optimal functional range of genetically encoded proteins. The hyperthermophilic archaeon Aeropyrum pernix (A. pernix) can grow throughout temperature variations ranging from 70 to 100°C, although the specific factors facilitating such adaptability are unknown. Here, we show that A. pernix undergoes constitutive leucine to methionine mistranslation at low growth temperatures. Low-temperature mistranslation is facilitated by the misacylation of tRNA(Leu) with methionine by the methionyl-tRNA synthetase (MetRS). At low growth temperatures, the A. pernix MetRS undergoes a temperature dependent shift in tRNA charging fidelity, allowing the enzyme to conditionally charge tRNA(Leu) with methionine. We demonstrate enhanced low-temperature activity for A. pernix citrate synthase that is synthesized during leucine to methionine mistranslation at low-temperature growth compared to its high-fidelity counterpart synthesized at high-temperature. Our results show that conditional leucine to methionine mistranslation can make protein adjustments capable of improving the low-temperature activity of hyperthermophilic proteins, likely by facilitating the increasing flexibility required for greater protein function at lower physiological temperatures.
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