The flavoprotein Mcap0476 (RlmFO) catalyzes m 5U1939 modification in Mycoplasma capricolum 23Ś rRNA

Carole Lartigue, Anne Lebaudy, Alain Blanchard, Basma El Yacoubi, Simon Rose, Henri Grosjean, Stephen Roger Douthwaite

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Efficient protein synthesis in all organisms requires the post-transcriptional methylation of specific ribosomal ribonucleic acid (rRNA) and transfer RNA (tRNA) nucleotides. The methylation reactions are almost invariably catalyzed by enzymes that use S-adenosylmethionine (AdoMet) as the methyl group donor. One noteworthy exception is seen in some bacteria, where the conserved tRNA methylation at m5U54 is added by the enzyme TrmFO using flavin adenine dinucleotide together with N5,N10-methylenetetrahydrofolate as the one-carbon donor. The minimalist bacterium Mycoplasma capricolum possesses two homologs of trmFO, but surprisingly lacks the m5U54 tRNA modification. We created single and dual deletions of the trmFO homologs using a novel synthetic biology approach. Subsequent analysis of the M. capricolum RNAs by mass spectrometry shows that the TrmFO homolog encoded by Mcap0476 specifically modifies m5U1939 in 23S rRNA, a conserved methylation catalyzed by AdoMet-dependent enzymes in all other characterized bacteria. The Mcap0476 methyltransferase (renamed RlmFO) represents the first folate-dependent flavoprotein seen to modify ribosomal RNA.

Original languageEnglish
JournalNucleic Acids Research
Volume42
Issue number12
Pages (from-to)8073-8082
Number of pages10
ISSN0305-1048
DOIs
Publication statusPublished - 8. Jul 2014

Keywords

  • Bacterial Proteins
  • Biocatalysis
  • Flavoproteins
  • Methylation
  • Methyltransferases
  • Mycoplasma capricolum
  • RNA, Ribosomal, 23S
  • RNA, Transfer
  • Uridine

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