ArticleNucleic acids research2020
The methyltransferase TrmA facilitates tRNA folding through interaction with its RNA-binding domain.
Article in Nucleic acids research, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 42 citations in OpenAlex.
- Guanosine 10 methylation by TRMT11-TRMT112 optimizes human mitochondrial tRNAs for efficient translation.Nucleic acids research · 2026Article
- Chronology of tRNA structural dynamics prior to and during interaction with a pseudouridine synthase.RNA (New York, N.Y.) · 2026Article
- Contribution of three tRNA modification enzymes toInfection and immunity · 2026Article
- The tRNA dihydrouridine synthase DusA has a distinct mechanism in optimizing tRNAs for translation.Nucleic acids research · 2026Article
- METTL1 interacts with XPO5 to modulate pre-miRNA export.Nucleic acids research · 2026Article
- Analysis of tRNA Aminoacylation by Northern Blotting and Multiplex Small RNA-Seq.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Beyond RNA modification: a novel role for tRNA modifying enzyme in oxidative stress response and metabolism.Nucleic acids research · 2025Article
- The tRNA epitranscriptomic landscape and RNA modification enzymes in Vibrio cholerae.PLoS genetics · 2025Article
- tRNA-modifying enzymes in bacterial stress adaptation.Open biology · 2025Review
- tRNA modifications as regulators of bacterial virulence and stress responses.PLoS pathogens · 2025Review
- RAPDOR: Using Jensen-Shannon Distance for the computational analysis of complex proteomics datasets.Nature communications · 2025Article
- 5-Methyluridine is Ubiquitous in Pseudomonas aeruginosa tRNA and Modulates Antimicrobial Resistance and Virulence.Journal of molecular biology · 2025Article
- Decoding the Minimal Translation System of the Plasmodium falciparum Apicoplast: Essential tRNA-modifying Enzymes and Their Roles in Organelle Maintenance.Journal of molecular biology · 2025Article
- Circuit logic: interdependent RNA modifications shape mRNA and noncoding RNA structure and function.RNA (New York, N.Y.) · 2025Review
- Conserved 5-methyluridine tRNA modification modulates ribosome translocation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- RNA modifying enzymes shape tRNA biogenesis and function.The Journal of biological chemistry · 2024Review
- Modifications in the T arm of tRNA globally determine tRNA maturation, function, and cellular fitness.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Review
- Human TRMT2A methylates tRNA and contributes to translation fidelity.Nucleic acids research · 2023Article
- Restoration of mitochondrial function through activation of hypomodified tRNAs with pathogenic mutations associated with mitochondrial diseases.Nucleic acids research · 2023Article
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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
tRNAs are the most highly modified RNAs in all cells, and formation of 5-methyluridine (m5U) at position 54 in the T arm is a common RNA modification found in all tRNAs. The m5U modification is generated by the methyltransferase TrmA. Here, we test and prove the hypothesis that Escherichia coli TrmA has dual functions, acting both as a methyltransferase and as a tRNA chaperone. We identify two conserved residues, F106 and H125, in the RNA-binding domain of TrmA, which interact with the tRNA elbow and are critical for tRNA binding. Co-culture competition assays reveal that the catalytic activity of TrmA is important for cellular fitness, and that substitutions of F106 or H125 impair cellular fitness. We directly show that TrmA enhances tRNA folding in vitro independent of its catalytic activity. In conclusion, our study suggests that F106 and H125 in the RNA-binding domain of TrmA act as a wedge disrupting tertiary interactions between tRNA's D arm and T arm; this tRNA unfolding is the mechanistic basis for TrmA's tRNA chaperone activity. TrmA is the second tRNA modifying enzyme next to the pseudouridine synthase TruB shown to act as a tRNA chaperone supporting a functional link between RNA modification and folding.
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