ArticleNucleic acids research2007
Functional specialization of domains tandemly duplicated within 16S rRNA methyltransferase RsmC.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 30 citations in OpenAlex.
- Compendium of RNA modifications for bacterial stress adaptation.Microbiology and molecular biology reviews : MMBR · 2026Review
- 16S rRNA Methyltransferases as Novel Drug Targets Against Tuberculosis.The protein journal · 2022Review
- Crystal structure of the Legionella pneumophila Lpg2936 in complex with the cofactor S-adenosyl-L-methionine reveals novel insights into the mechanism of RsmE family methyltransferases.Protein science : a publication of the Protein Society · 2017Article
- 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
- Base methylations in the double-stranded RNA by a fused methyltransferase bearing unwinding activity.Nucleic acids research · 2012Article
- The open reading frame TTC1157 of Thermus thermophilus HB27 encodes the methyltransferase forming N²-methylguanosine at position 6 in tRNA.RNA (New York, N.Y.) · 2012Article
- Crystallization and preliminary X-ray crystallographic analysis of putative tRNA-modification enzymes from Pyrococcus furiosus and Thermus thermophilus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Identification and modeling of a phosphatase-like domain in a tRNA 2'-O-ribosyl phosphate transferase Rit1p.Cell cycle (Georgetown, Tex.) · 2011Article
- 2'-O-ribose methylation of cap2 in human: function and evolution in a horizontally mobile family.Nucleic acids research · 2011Article
- Actin-binding protein ABP140 is a methyltransferase for 3-methylcytidine at position 32 of tRNAs in Saccharomyces cerevisiae.RNA (New York, N.Y.) · 2011Article
- Expression, purification and crystallization of adenosine 1408 aminoglycoside-resistance rRNA methyltransferases for structural studies.Protein expression and purification · 2011Article
- Determinants, discriminants, conserved residues--a heuristic approach to detection of functional divergence in protein families.PloS one · 2011Article
- 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
- Multiple Motif Scanning to identify methyltransferases from the yeast proteome.Molecular & cellular proteomics : MCP · 2009Article
- Predicting RNA-binding sites of proteins using support vector machines and evolutionary information.BMC bioinformatics · 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
- Critical residues for cofactor binding and catalytic activity in the aminoglycoside resistance methyltransferase Sgm.Journal of bacteriology · 2008Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNA methyltransferases (MTases) are important players in the biogenesis and regulation of the ribosome, the cellular machine for protein synthesis. RsmC is a MTase that catalyzes the transfer of a methyl group from S-adenosyl-l-methionine (SAM) to G1207 of 16S rRNA. Mutations of G1207 have dominant lethal phenotypes in Escherichia coli, underscoring the significance of this modified nucleotide for ribosome function. Here we report the crystal structure of E. coli RsmC refined to 2.1 A resolution, which reveals two homologous domains tandemly duplicated within a single polypeptide. We characterized the function of the individual domains and identified key residues involved in binding of rRNA and SAM, and in catalysis. We also discovered that one of the domains is important for the folding of the other. Domain duplication and subfunctionalization by complementary degeneration of redundant functions (in particular substrate binding versus catalysis) has been reported for many enzymes, including those involved in RNA metabolism. Thus, RsmC can be regarded as a model system for functional streamlining of domains accompanied by the development of dependencies concerning folding and stability.
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