ArticleRNA (New York, N.Y.)2012
The Escherichia coli RlmN methyltransferase is a dual-specificity enzyme that modifies both rRNA and tRNA and controls translational accuracy.
Article in RNA (New York, N.Y.), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.
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73 citing papers in PubMed, 101 citations in OpenAlex.
- Compendium of RNA modifications for bacterial stress adaptation.Microbiology and molecular biology reviews : MMBR · 2026Review
- Comprehensive post-transcriptional modification profiles in individual Staphylococcus aureus tRNA species.Nucleic acids research · 2026Article
- Mapping the rRNA methylome reveals contributions of methyltransferases to ribosome function and antibiotic sensitivity.bioRxiv : the preprint server for biology · 2026Article
- Growth-dependent tRNA Reprogramming and Codon Bias Link Translation to Metabolic State inbioRxiv : the preprint server for biology · 2026Article
- Direct RNA Sequencing Reveals Stress-Dependent and Pathway-Specific rRNA Modification Reprogramming during 50S Biogenesis.Biochemistry · 2026Article
- Structural Basis for CbioRxiv : the preprint server for biology · 2026Article
- Direct RNA Sequencing Reveals Stress-Dependent and Pathway-Specific rRNA Modification Reprogramming During 50S Biogenesis.bioRxiv : the preprint server for biology · 2026Article
- Epitranscriptomic modifications in plant RNAs.RNA biology · 2025Review
- tRNA modifications as regulators of bacterial virulence and stress responses.PLoS pathogens · 2025Review
- tRNA-modifying enzymes in bacterial stress adaptation.Open biology · 2025Review
- tRNA modification profiling reveals epitranscriptome regulatory networks in Pseudomonas aeruginosa.Nucleic acids research · 2025Article
- tRNA pseudouridine synthase D (TruD) fromRNA (New York, N.Y.) · 2025Article
- Article
- Stress-induced modification ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- BglaTNB6, a tailocin produced by a plant-associated nonpathogenic bacterium, prevents rice seed-borne bacterial diseases.PLoS pathogens · 2024Article
- Multi-Omics Integrative Analysis to Reveal the Impacts ofInternational journal of molecular sciences · 2024Article
- The modification landscape ofRNA (New York, N.Y.) · 2024Article
- Structural basis of Cfr-mediated antimicrobial resistance and mechanisms to evade it.Nature chemical biology · 2024Article
- Ribosomal RNA modification enzymes stimulate large ribosome subunit assembly in E. coli.Nucleic acids research · 2024Article
- The modification landscape ofbioRxiv : the preprint server for biology · 2024Article
13 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 2 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Modifying RNA enzymes are highly specific for substrate-rRNA or tRNA-and the target position. In Escherichia coli, there are very few multisite acting enzymes, and only one rRNA/tRNA dual-specificity enzyme, pseudouridine synthase RluA, has been identified to date. Among the tRNA-modifying enzymes, the methyltransferase responsible for the m(2)A synthesis at purine 37 in a tRNA set still remains unknown. m(2)A is also present at position 2503 in the peptidyl transferase center of 23S RNA, where it is introduced by RlmN, a radical S-adenosyl-L-methionine (SAM) enzyme. Here, we show that E. coli RlmN is a dual-specificity enzyme that catalyzes methylation of both rRNA and tRNA. The ΔrlmN mutant lacks m(2)A in both RNA types, whereas the expression of recombinant RlmN from a plasmid introduced into this mutant restores tRNA modification. Moreover, RlmN performs m(2)A(37) synthesis in vitro using a tRNA chimera as a substrate. This chimera has also proved useful to characterize some tRNA identity determinants for RlmN and other tRNA modification enzymes. Our data suggest that RlmN works in a late step during tRNA maturation by recognizing a precise 3D structure of tRNA. RlmN inactivation increases the misreading of a UAG stop codon. Since loss of m(2)A(37) from tRNA is expected to produce a hyperaccurate phenotype, we believe that the error-prone phenotype exhibited by the ΔrlmN mutant is due to loss of m(2)A from 23S rRNA and, accordingly, that the m(2)A2503 modification plays a crucial role in the proofreading step occurring at the peptidyl transferase center.
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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.