Identification and characterization of RsmE, the founding member of a new RNA base methyltransferase family

Georgeta N. Basturea, Kenneth E. Rudd, Murray P. Deutscher

Research output: Contribution to journalArticlepeer-review

61 Scopus citations


A variety of RNA methyltransferases act during ribosomal RNA maturation to modify nucleotides in a site-specificmanner. However, of the 10 base-methylated nucleotides present in the small ribosomal subunit of Escherichia coli, only three enzymes responsible for modification of four bases are known. Here, we show that the protein encoded by yggJ, a member of the uncharacterized DUF558 protein family of predicted alpha/beta (trefoil) knot methyltransferases is responsible for methylation at U1498 in 16S rRNA. The gene is well-conserved across bacteria and plants, and likely performs the same function in other organisms. A yggJ deletion strain lacks the methyl group at U1498 as well as the specific methyltransferase activity. Moreover, purified recombinant YggJ specifically methylates m3U1498 in vitro. The deletion strain was unaffected in exponential growth in rich or minimal media at multiple temperatures, but it was defective when grown in competition with isogenic wild-type cells. Based on these data, we conclude that yggJ is the founding member of a family of RNA base methyltransferases, and propose that it be renamed rsmE. Published by Cold Spring Harbor Laboratory Press.

Original languageEnglish (US)
Pages (from-to)426-434
Number of pages9
Issue number3
StatePublished - Mar 2006
Externally publishedYes


  • E. coli
  • Methyltransferase
  • Protein family
  • RNA modification

ASJC Scopus subject areas

  • Genetics
  • Molecular Biology


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