ArticlePloS one2016
Determinants of tRNA Recognition by the Radical SAM Enzyme RlmN.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 10 citations in OpenAlex.
- Comprehensive post-transcriptional modification profiles in individual Staphylococcus aureus tRNA species.Nucleic acids research · 2026Article
- Structural Basis for CbioRxiv : the preprint server for biology · 2026Article
- Structural Analysis of 23S rRNA Methylating Enzyme Cfr Reveals RNA-Binding Determinants for Methylation Regiospecificity and Antibiotic Resistance.ACS infectious diseases · 2026Article
- Structural analysis of 23S rRNA methylating enzyme Cfr reveals RNA binding determinants for methylation regiospecificity and antibiotic resistance.bioRxiv : the preprint server for biology · 2025Article
- The modification landscape ofRNA (New York, N.Y.) · 2024Article
- The modification landscape ofbioRxiv : the preprint server for biology · 2024Article
- New substrates and determinants for tRNA recognition of RNA methyltransferase DNMT2/TRDMT1.RNA biology · 2021Article
- miCLIP-MaPseq Identifies Substrates of Radical SAM RNA-Methylating Enzyme Using Mechanistic Cross-Linking and Mismatch Profiling.Methods in molecular biology (Clifton, N.J.) · 2021Article
- The y-ome defines the 35% of Escherichia coli genes that lack experimental evidence of function.Nucleic acids research · 2019Article
- miCLIP-MaPseq, a Substrate Identification Approach for Radical SAM RNA Methylating Enzymes.Journal of the American Chemical Society · 2018Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
RlmN, a bacterial radical SAM methylating enzyme, has the unusual ability to modify two distinct types of RNA: 23S rRNA and tRNA. In rRNA, RlmN installs a methyl group at the C2 position of A2503 of 23S rRNA, while in tRNA the modification occurs at nucleotide A37, immediately adjacent to the anticodon triplet. Intriguingly, only a subset of tRNAs that contain an adenosine at position 37 are substrates for RlmN, suggesting that the enzyme carefully probes the highly conserved tRNA fold and sequence features to identify its targets. Over the past several years, multiple studies have addressed rRNA modification by RlmN, while relatively few investigations have focused on the ability of this enzyme to modify tRNAs. In this study, we utilized in vitro transcribed tRNAs as model substrates to interrogate RNA recognition by RlmN. Using chimeras and point mutations, we probed how the structure and sequence of RNA influences methylation, identifying position 38 of tRNAs as a critical determinant of substrate recognition. We further demonstrate that, analogous to previous mechanistic studies with fragments of 23S rRNA, tRNA methylation requirements are consistent with radical SAM reactivity. Together, our findings provide detailed insight into tRNA recognition by a radical SAM methylating enzyme.
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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.