mnmC

Summary

Gene Symbol: mnmC
Description: fused 5-methylaminomethyl-2-thiouridine-forming enzyme methyltransferase and FAD-dependent demodification enzyme
Alias: ECK2318, JW5380, trmC, yfcK
Species: Escherichia coli str. K-12 substr. MG1655

Top Publications

  1. Roovers M, Oudjama Y, Kaminska K, Purta E, Caillet J, Droogmans L, et al. Sequence-structure-function analysis of the bifunctional enzyme MnmC that catalyses the last two steps in the biosynthesis of hypermodified nucleoside mnm5s2U in tRNA. Proteins. 2008;71:2076-85 pubmed publisher
    ..Previously, we reported that this bifunctional enzyme is encoded by the yfcK open reading frame in the Escherichia coli K12 genome...
  2. Hagervall T, Edmonds C, McCloskey J, Björk G. Transfer RNA(5-methylaminomethyl-2-thiouridine)-methyltransferase from Escherichia coli K-12 has two enzymatic activities. J Biol Chem. 1987;262:8488-95 pubmed
    ..The molecular activity of the methyltransferase activity (nm5s2U34----mnm5s2U34) is 74 min-1, and the steady state concentration of the enzyme is only 78 molecules/genome equivalent in cells growing at a specific growth rate of 1.0/h. ..
  3. Hagervall T, Björk G. Undermodification in the first position of the anticodon of supG-tRNA reduces translational efficiency. Mol Gen Genet. 1984;196:194-200 pubmed
    ..It was found that two different undermodified derivatives of mnm5s2U were present in the two trmC mutants, which suggests that the two mutations affect two different enzymatic activities...
  4. Hagervall T, Björk G. Genetic mapping and cloning of the gene (trmC) responsible for the synthesis of tRNA (mnm5s2U)methyltransferase in Escherichia coli K12. Mol Gen Genet. 1984;196:201-7 pubmed
    The trmC gene, responsible for the formation of 5-methylaminomethyl-2-thiouridine (mnm5s2U) from 2-thiouridine, present in the first position in the anticodon of some tRNAs, has been located at 50...
  5. Bujnicki J, Oudjama Y, Roovers M, Owczarek S, Caillet J, Droogmans L. Identification of a bifunctional enzyme MnmC involved in the biosynthesis of a hypermodified uridine in the wobble position of tRNA. RNA. 2004;10:1236-42 pubmed
    The gene encoding the bifunctional enzyme MnmC that catalyzes the two last steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm5s2U) in tRNA has been previously mapped at about 50 min on the Escherichia coli K12 chromosome, ..
  6. Pearson D, Carell T. Assay of both activities of the bifunctional tRNA-modifying enzyme MnmC reveals a kinetic basis for selective full modification of cmnm5s2U to mnm5s2U. Nucleic Acids Res. 2011;39:4818-26 pubmed publisher
    ..of the mnm(5)s(2)U nucleoside in Escherichia coli tRNA(Glu), which are both catalysed by the bifunctional MnmC enzyme...
  7. Björk G, Kjellin Stråby K. General screening procedure for RNA modificationless mutants: isolation of Escherichia coli strains with specific defects in RNA methylation. J Bacteriol. 1978;133:499-507 pubmed
    ..In 23S rRNA from the other mutant, the only product formed in vitro was 5-methylcytidine. The tRNA mutants are characterized in the accompanying paper. ..
  8. Björk G, Kjellin Stråby K. Escherichia coli mutants with defects in the biosynthesis of 5-methylaminomethyl-2-thio-uridine or 1-methylguanosine in their tRNA. J Bacteriol. 1978;133:508-17 pubmed
  9. Kim J, Almo S. Structural basis for hypermodification of the wobble uridine in tRNA by bifunctional enzyme MnmC. BMC Struct Biol. 2013;13:5 pubmed publisher
    ..In the biosynthetic pathway responsible for this post-transcriptional modification, the bifunctional enzyme MnmC catalyzes the conversion of its hypermodified substrate carboxymethylaminomethyl uridine (cmnm5U34) to mnm5U34...

More Information

Publications10

  1. Moukadiri I, Garzón M, Bjork G, Armengod M. The output of the tRNA modification pathways controlled by the Escherichia coli MnmEG and MnmC enzymes depends on the growth conditions and the tRNA species. Nucleic Acids Res. 2014;42:2602-23 pubmed publisher
    ..the MnmEG products are converted into 5-methylaminomethyl (mnm(5)) through the two-domain, bi-functional enzyme MnmC. MnmC(o) transforms cmnm(5) into nm(5), whereas MnmC(m) converts nm(5) into mnm(5), thus producing an atypical ..