ArticleThe Journal of biological chemistry2011
Structural and functional characterization of Rv2966c protein reveals an RsmD-like methyltransferase from Mycobacterium tuberculosis and the role of its N-terminal domain in target recognition.
Article in The Journal of biological chemistry, 2011. 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, 46 citations in OpenAlex.
- A Frameshift Mutation in the MethyltransferaseComputational and structural biotechnology journal · 2026Article
- Structural basis for phosphatidylcholine synthesis by bacterial phospholipid N-methyltransferases.The Journal of biological chemistry · 2025Article
- Complete list of canonical post-transcriptional modifications in the Bacillus subtilis ribosome and their link to RbgA driven large subunit assembly.Nucleic acids research · 2024Article
- The Restriction Activity Investigation of Rv2528c, an Mrr-like Modification-Dependent Restriction Endonuclease fromMicroorganisms · 2024Article
- Complete list of canonical post-transcriptional modifications in thebioRxiv : the preprint server for biology · 2024Article
- A prophage encoded ribosomal RNA methyltransferase regulates the virulence of Shiga-toxin-producing Escherichia coli (STEC).Nucleic acids research · 2024Article
- Computational analysis of RNA methyltransferase Rv3366 as a potential drug target for combating drug-resistantFrontiers in molecular biosciences · 2023Article
- 16S rRNA Methyltransferases as Novel Drug Targets Against Tuberculosis.The protein journal · 2022Review
- Complete genome sequence of high-yield strainSynthetic and systems biotechnology · 2020Article
- Cyclipostins and Cyclophostin analogs as promising compounds in the fight against tuberculosis.Scientific reports · 2017Article
- The interaction of mycobacterial protein Rv2966c with host chromatin is mediated through non-CpG methylation and histone H3/H4 binding.Nucleic acids research · 2015Article
- Unique subunit packing in mycobacterial nanoRNase leads to alternate substrate recognitions in DHH phosphodiesterases.Nucleic acids research · 2014Article
- The structure of Rv3717 reveals a novel amidase from Mycobacterium tuberculosis.Acta crystallographica. Section D, Biological crystallography · 2013Article
- 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
- Integration host factor of Mycobacterium tuberculosis, mIHF, compacts DNA by a bending mechanism.PloS one · 2013Article
- Structural insights into the function of 23S rRNA methyltransferase RlmG (m²G1835) from Escherichia coli.RNA (New York, N.Y.) · 2012Article
- Properties of small rRNA methyltransferase RsmD: mutational and kinetic study.RNA (New York, N.Y.) · 2012Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nine of ten methylated nucleotides of Escherichia coli 16 S rRNA are conserved in Mycobacterium tuberculosis. All the 10 different methyltransferases are known in E. coli, whereas only TlyA and GidB have been identified in mycobacteria. Here we have identified Rv2966c of M. tuberculosis as an ortholog of RsmD protein of E. coli. We have shown that rv2966c can complement rsmD-deleted E. coli cells. Recombinant Rv2966c can use 30 S ribosomes purified from rsmD-deleted E. coli as substrate and methylate G966 of 16 S rRNA in vitro. Structure determination of the protein shows the protein to be a two-domain structure with a short hairpin domain at the N terminus and a C-terminal domain with the S-adenosylmethionine-MT-fold. We show that the N-terminal hairpin is a minimalist functional domain that helps Rv2966c in target recognition. Deletion of the N-terminal domain prevents binding to nucleic acid substrates, and the truncated protein fails to carry out the m(2)G966 methylation on 16 S rRNA. The N-terminal domain also binds DNA efficiently, a property that may be utilized under specific conditions of cellular growth.
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