ArticleJournal of molecular biology2011
The human mitochondrial tRNAMet: structure/function relationship of a unique modification in the decoding of unconventional codons.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 61 citations in OpenAlex.
- Review
- Role of RNA 5‑methylcytosine modification in cancer: Insights from coding and non‑coding RNAs (Review).Molecular medicine reports · 2026Review
- Emerging mechanisms of human mitochondrial translation regulation.Trends in biochemical sciences · 2025Review
- Dynamic Regulation of 5-Formylcytidine on tRNA.ACS chemical biology · 2025Article
- Selection of initiator tRNA and start codon by mammalian mitochondrial initiation factor 3 in leaderless mRNA translation.Nucleic acids research · 2025Article
- Mitochondrial RNA in Inflammation.International journal of biological sciences · 2025Review
- RNA modification in cardiovascular disease: implications for therapeutic interventions.Signal transduction and targeted therapy · 2023Review
- NSUN3-mediated mitochondrial tRNA 5-formylcytidine modification is essential for embryonic development and respiratory complexes in mice.Communications biology · 2023Article
- Reactivity-dependent profiling of RNA 5-methylcytidine dioxygenases.Nature communications · 2022Article
- Article
- Modifications of the human tRNA anticodon loop and their associations with genetic diseases.Cellular and molecular life sciences : CMLS · 2021Review
- Mechanisms and regulation of protein synthesis in mitochondria.Nature reviews. Molecular cell biology · 2021Review
- Article
- The mammalian mitochondrial epitranscriptome.Biochimica et biophysica acta. Gene regulatory mechanisms · 2019Review
- Review
- RNA cytosine methyltransferase Nsun3 regulates embryonic stem cell differentiation by promoting mitochondrial activity.Cellular and molecular life sciences : CMLS · 2018Article
- The mitochondrial epitranscriptome: the roles of RNA modifications in mitochondrial translation and human disease.Cellular and molecular life sciences : CMLS · 2018Review
- Regulation of Mammalian Mitochondrial Gene Expression: Recent Advances.Trends in biochemical sciences · 2017Review
- Dealing with an Unconventional Genetic Code in Mitochondria: The Biogenesis and Pathogenic Defects of the 5-Formylcytosine Modification in Mitochondrial tRNABiomolecules · 2017Review
- How RNA modification allows non-conventional decoding in mitochondria.Cell cycle (Georgetown, Tex.) · 2017Article
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10 authors at 3 institutions in 1 country.
Funding
Abstract
Human mitochondrial mRNAs utilize the universal AUG and the unconventional isoleucine AUA codons for methionine. In contrast to translation in the cytoplasm, human mitochondria use one tRNA, hmtRNA(Met)(CAU), to read AUG and AUA codons at both the peptidyl- (P-), and aminoacyl- (A-) sites of the ribosome. The hmtRNA(Met)(CAU) has a unique post-transcriptional modification, 5-formylcytidine, at the wobble position 34 (f(5)C(34)), and a cytidine substituting for the invariant uridine at position 33 of the canonical U-turn in tRNAs. The structure of the tRNA anticodon stem and loop domain (hmtASL(Met)(CAU)), determined by NMR restrained molecular modeling, revealed how the f(5)C(34) modification facilitates the decoding of AUA at the P- and the A-sites. The f(5)C(34) defined a reduced conformational space for the nucleoside, in what appears to have restricted the conformational dynamics of the anticodon bases of the modified hmtASL(Met)(CAU). The hmtASL(Met)(CAU) exhibited a C-turn conformation that has some characteristics of the U-turn motif. Codon binding studies with both Escherichia coli and bovine mitochondrial ribosomes revealed that the f(5)C(34) facilitates AUA binding in the A-site and suggested that the modification favorably alters the ASL binding kinetics. Mitochondrial translation by many organisms, including humans, sometimes initiates with the universal isoleucine codons AUU and AUC. The f(5)C(34) enabled P-site codon binding to these normally isoleucine codons. Thus, the physicochemical properties of this one modification, f(5)C(34), expand codon recognition from the traditional AUG to the non-traditional, synonymous codons AUU and AUC as well as AUA, in the reassignment of universal codons in the mitochondria.
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