ArticleNucleic acids research2019
Structural characterization of B. subtilis m1A22 tRNA methyltransferase TrmK: insights into tRNA recognition.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 13 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
- Review
- Rational design of oligonucleotides for enhanced in vitro transcription of small RNA.RNA (New York, N.Y.) · 2024Article
- Advances in the Structural and Functional Understanding of mAccounts of chemical research · 2024Article
- Prognostic signature and immune efficacy of mJournal of Cancer · 2024Article
- Application of mutational profiling: New functional analyses reveal the tRNA recognition mechanism of tRNA mThe Journal of biological chemistry · 2023Article
- Structure, dynamics, and molecular inhibition of the Staphylococcus aureus mThe Journal of biological chemistry · 2022Article
- tRNA elbow modifications affect the tRNA pseudouridine synthase TruB and the methyltransferase TrmA.RNA (New York, N.Y.) · 2020Article
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
1-Methyladenosine (m1A) is a modified nucleoside found at positions 9, 14, 22 and 58 of tRNAs, which arises from the transfer of a methyl group onto the N1-atom of adenosine. The yqfN gene of Bacillus subtilis encodes the methyltransferase TrmK (BsTrmK) responsible for the formation of m1A22 in tRNA. Here, we show that BsTrmK displays a broad substrate specificity, and methylates seven out of eight tRNA isoacceptor families of B. subtilis bearing an A22. In addition to a non-Watson-Crick base-pair between the target A22 and a purine at position 13, the formation of m1A22 by BsTrmK requires a full-length tRNA with intact tRNA elbow and anticodon stem. We solved the crystal structure of BsTrmK showing an N-terminal catalytic domain harbouring the typical Rossmann-like fold of Class-I methyltransferases and a C-terminal coiled-coil domain. We used NMR chemical shift mapping to drive the docking of BstRNASer to BsTrmK in complex with its methyl-donor cofactor S-adenosyl-L-methionine (SAM). In this model, validated by methyltransferase activity assays on BsTrmK mutants, both domains of BsTrmK participate in tRNA binding. BsTrmK recognises tRNA with very few structural changes in both partner, the non-Watson-Crick R13-A22 base-pair positioning the A22 N1-atom close to the SAM methyl group.
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