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Related Experiment Video

Updated: Jun 5, 2026

Enhanced Reduced Representation Bisulfite Sequencing for Assessment of DNA Methylation at Base Pair Resolution
13:47

Enhanced Reduced Representation Bisulfite Sequencing for Assessment of DNA Methylation at Base Pair Resolution

Published on: February 24, 2015

Minimal substrate features for Erm methyltransferases defined by using a combinatorial oligonucleotide library.

Lykke H Hansen1, Sune Lobedanz, Stephen Douthwaite

  • 1Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, 5230 Odense M, Denmark.

Chembiochem : a European Journal of Chemical Biology
|January 26, 2011
PubMed
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Erm methyltransferases confer antibiotic resistance by modifying 23S ribosomal RNA. Researchers identified key RNA structural motifs essential for Erm enzyme activity, aiding in the design of novel resistance-blocking molecules.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Erm methyltransferases are crucial for bacterial resistance to macrolide, lincosamide, and streptogramin B antibiotics.
  • These enzymes function by methylating the 23S ribosomal RNA at the A2058 nucleotide.

Purpose of the Study:

  • To identify specific structural motifs within the rRNA substrate recognized by Erm methyltransferases.
  • To understand the role of different RNA strands and modifications in the methylation process.
  • To lay the groundwork for designing molecules that inhibit Erm activity.

Main Methods:

  • Combinatorial synthesis of short RNA sequences to create substrate molecules.
  • Incorporation of Locked Nucleic Acid (LNA) monomers to stabilize RNA structures.

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Last Updated: Jun 5, 2026

Enhanced Reduced Representation Bisulfite Sequencing for Assessment of DNA Methylation at Base Pair Resolution
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Enhanced Reduced Representation Bisulfite Sequencing for Assessment of DNA Methylation at Base Pair Resolution

Published on: February 24, 2015

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
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Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues

Published on: November 22, 2014

DNAzyme-dependent Analysis of rRNA 2&#8217;-O-Methylation
09:12

DNAzyme-dependent Analysis of rRNA 2’-O-Methylation

Published on: September 16, 2019

  • Functional assays to assess methylation efficiency with modified substrates.

    • Main Results:

    • Erm recognizes specific structural features: an unpaired A2058 target following an irregular helix on the top strand.
    • Stabilizing the top strand with LNA at G2056 enhanced methylation.
    • The bottom strand is essential for methylation, primarily by maintaining the top strand's conformation, and can be substituted with DNA.
    • Excessive LNA modification on the top strand hindered methylation, indicating a need for substrate flexibility.

    Conclusions:

    • The study elucidates the precise structural requirements of rRNA substrates for Erm-mediated methylation.
    • Findings provide insights into the mechanism of antibiotic resistance conferred by Erm enzymes.
    • This research facilitates the development of strategies to overcome Erm-mediated resistance by designing inhibitors.