ArticleBMC bioinformatics2002
RNA:(guanine-N2) methyltransferases RsmC/RsmD and their homologs revisited--bioinformatic analysis and prediction of the active site based on the uncharacterized Mj0882 protein structure.
Article in BMC bioinformatics, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 35 citations in OpenAlex.
- 16S rRNA Methyltransferases as Novel Drug Targets Against Tuberculosis.The protein journal · 2022Review
- AtRsmD Is Required for Chloroplast Development and Chloroplast Function inFrontiers in plant science · 2022Article
- Structural insights into the function of 23S rRNA methyltransferase RlmG (m²G1835) from Escherichia coli.RNA (New York, N.Y.) · 2012Article
- Trm13p, the tRNA:Xm4 modification enzyme from Saccharomyces cerevisiae is a member of the Rossmann-fold MTase superfamily: prediction of structure and active site.Journal of molecular modeling · 2010Article
- The divergent eukaryote Trichomonas vaginalis has an m7G cap methyltransferase capable of a single N2 methylation.Nucleic acids research · 2008Article
- Crystal structure of the Thermus thermophilus 16 S rRNA methyltransferase RsmC in complex with cofactor and substrate guanosine.The Journal of biological chemistry · 2008Article
- Methyltransferase that modifies guanine 966 of the 16 S rRNA: functional identification and tertiary structure.The Journal of biological chemistry · 2007Article
- Functional specialization of domains tandemly duplicated within 16S rRNA methyltransferase RsmC.Nucleic acids research · 2007Article
- Ribosomal RNA guanine-(N2)-methyltransferases and their targets.Nucleic acids research · 2007Review
- Identification and characterization of RsmE, the founding member of a new RNA base methyltransferase family.RNA (New York, N.Y.) · 2006Article
- Natural history of S-adenosylmethionine-binding proteins.BMC structural biology · 2005Article
- Sequence-structure-function relationships of Tgs1, the yeast snRNA/snoRNA cap hypermethylase.Nucleic acids research · 2003Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundEscherichia coli guanine-N2 (m2G) methyltransferases (MTases) RsmC and RsmD modify nucleosides G1207 and G966 of 16S rRNA. They possess a common MTase domain in the C-terminus and a variable region in the N-terminus. Their C-terminal domain is related to the YbiN family of hypothetical MTases, but nothing is known about the structure or function of the N-terminal domain.
resultsUsing a combination of sequence database searches and fold recognition methods it has been demonstrated that the N-termini of RsmC and RsmD are related to each other and that they represent a "degenerated" version of the C-terminal MTase domain. Novel members of the YbiN family from Archaea and Eukaryota were also indentified. It is inferred that YbiN and both domains of RsmC and RsmD are closely related to a family of putative MTases from Gram-positive bacteria and Archaea, typified by the Mj0882 protein from M. jannaschii (1dus in PDB). Based on the results of sequence analysis and structure prediction, the residues involved in cofactor binding, target recognition and catalysis were identified, and the mechanism of the guanine-N2 methyltransfer reaction was proposed.
conclusionsUsing the known Mj0882 structure, a comprehensive analysis of sequence-structure-function relationships in the family of genuine and putative m2G MTases was performed. The results provide novel insight into the mechanism of m2G methylation and will serve as a platform for experimental analysis of numerous uncharacterized N-MTases.
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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.