ArticleRNA (New York, N.Y.)2010
Multi-site-specific 16S rRNA methyltransferase RsmF from Thermus thermophilus.
Article in RNA (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 23 citations in OpenAlex.
- Compendium of RNA modifications for bacterial stress adaptation.Microbiology and molecular biology reviews : MMBR · 2026Review
- Stress-induced modification ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- 16S rRNA Methyltransferases as Novel Drug Targets Against Tuberculosis.The protein journal · 2022Review
- Advances in mRNA 5-methylcytosine modifications: Detection, effectors, biological functions, and clinical relevance.Molecular therapy. Nucleic acids · 2021Review
- Review
- Methylation of Ribosomal RNA: A Mitochondrial Perspective.Frontiers in genetics · 2020Review
- The mammalian mitochondrial epitranscriptome.Biochimica et biophysica acta. Gene regulatory mechanisms · 2019Review
- Structural basis for substrate binding and catalytic mechanism of a human RNA:m5C methyltransferase NSun6.Nucleic acids research · 2017Article
- Identification of the methyltransferase targeting C2499 in Deinococcus radiodurans 23S ribosomal RNA.Extremophiles : life under extreme conditions · 2016Article
- Evolutionary and sequence-based relationships in bacterial AdoMet-dependent non-coding RNA methyltransferases.BMC research notes · 2014Article
- NSUN4 is a dual function mitochondrial protein required for both methylation of 12S rRNA and coordination of mitoribosomal assembly.PLoS genetics · 2014Article
- Molecular characterization of an rsmD-like rRNA methyltransferase from the Wolbachia endosymbiont of Brugia malayi and antifilarial activity of specific inhibitors of the enzyme.Antimicrobial agents and chemotherapy · 2013Article
- Structure of the human MTERF4-NSUN4 protein complex that regulates mitochondrial ribosome biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Identification and characterization of the Thermus thermophilus 5-methylcytidine (m5C) methyltransferase modifying 23 S ribosomal RNA (rRNA) base C1942.The Journal of biological chemistry · 2012Article
- Structural insights into the function of 23S rRNA methyltransferase RlmG (m²G1835) from Escherichia coli.RNA (New York, N.Y.) · 2012Article
- A single methyltransferase YefA (RlmCD) catalyses both m5U747 and m5U1939 modifications in Bacillus subtilis 23S rRNA.Nucleic acids research · 2011Article
- Intrinsic resistance to aminoglycosides in Enterococcus faecium is conferred by the 16S rRNA m5C1404-specific methyltransferase EfmM.RNA (New York, N.Y.) · 2011Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Cells devote a significant effort toward the production of multiple modified nucleotides in rRNAs, which fine tune the ribosome function. Here, we report that two methyltransferases, RsmB and RsmF, are responsible for all four 5-methylcytidine (m(5)C) modifications in 16S rRNA of Thermus thermophilus. Like Escherichia coli RsmB, T. thermophilus RsmB produces m(5)C967. In contrast to E. coli RsmF, which introduces a single m(5)C1407 modification, T. thermophilus RsmF modifies three positions, generating m(5)C1400 and m(5)C1404 in addition to m(5)C1407. These three residues are clustered near the decoding site of the ribosome, but are situated in distinct structural contexts, suggesting a requirement for flexibility in the RsmF active site that is absent from the E. coli enzyme. Two of these residues, C1400 and C1404, are sufficiently buried in the mature ribosome structure so as to require extensive unfolding of the rRNA to be accessible to RsmF. In vitro, T. thermophilus RsmF methylates C1400, C1404, and C1407 in a 30S subunit substrate, but only C1400 and C1404 when naked 16S rRNA is the substrate. The multispecificity of T. thermophilus RsmF is potentially explained by three crystal structures of the enzyme in a complex with cofactor S-adenosyl-methionine at up to 1.3 A resolution. In addition to confirming the overall structural similarity to E. coli RsmF, these structures also reveal that key segments in the active site are likely to be dynamic in solution, thereby expanding substrate recognition by T. thermophilus RsmF.
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