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ErmE methyltransferase recognition elements in RNA substrates

B Vester1, A K Nielsen, L H Hansen

  • 1RNA Regulation Centre Department of Molecular Biology, University of Copenhagen, Denmark.

Journal of Molecular Biology
|September 15, 1998
PubMed
Summary
This summary is machine-generated.

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ErmE methyltransferase resistance to MLS antibiotics involves dimethylation of adenine 2058 in 23 S rRNA. Specific RNA motifs and magnesium ion concentrations influence this crucial methylation process.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Microbiology

Background:

  • Antibiotic resistance in bacteria is a growing concern.
  • Erm methyltransferases confer resistance to macrolide-lincosamide-streptogramin B (MLS) antibiotics.
  • This resistance is mediated by methylation of adenine 2058 (A2058) in bacterial 23 S ribosomal RNA (rRNA).

Purpose of the Study:

  • To investigate the minimal RNA motif required for ErmE methyltransferase recognition and activity.
  • To elucidate the role of magnesium ions in the methylation process.
  • To understand how RNA structure influences ErmE-mediated A2058 methylation.

Main Methods:

  • Site-directed mutagenesis and RNA truncation of domain V of 23 S rRNA.
  • In vitro methylation assays using ErmE methyltransferase from Saccharopolyspora erythraea.

Related Experiment Videos

  • Analysis of methylation efficiency under varying magnesium and monovalent cation concentrations.

    • Main Results:

    • Localized the ErmE recognition motif to a 27-nucleotide stem-loop structure (helix 73) containing A2058.
    • Optimal methylation of truncated RNAs occurred without magnesium, while 2-3 mM magnesium inhibited it.
    • Intact domain V RNA showed optimal methylation with 2 mM magnesium, indicating a conformational difference.
    • Monovalent cations influenced truncated RNA methylation, suggesting interactions with external RNA structures are supportive but not essential.

    Conclusions:

    • The minimal structural requirement for ErmE recognition is a specific stem-loop in domain V of 23 S rRNA.
    • Magnesium ions play a critical, concentration-dependent role in modulating ErmE activity by altering RNA conformation.
    • Understanding these structural and ionic requirements provides insights into antibiotic resistance mechanisms and potential therapeutic strategies.