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Related Experiment Videos

Substrate requirements for ErmC' methyltransferase activity

P Zhong1, S D Pratt, R P Edalji

  • 1Pharmaceutical Products Division, Abbott Laboratories, Abbott Park, Illinois 60064, USA.

Journal of Bacteriology
|August 1, 1995
PubMed
Summary
This summary is machine-generated.

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ErmC

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Microbiology

Background:

  • ErmC' methyltransferase confers antibiotic resistance by methylating 23S rRNA.
  • This methylation targets a specific adenine residue, hindering antibiotic binding.

Purpose of the Study:

  • To investigate the substrate requirements and kinetics of the ErmC' methyltransferase.
  • To characterize the interaction between ErmC' and its RNA substrate.

Main Methods:

  • Cloning and high-level expression of the ErmC' gene in E. coli.
  • Purification of ErmC' protein to virtual homogeneity.
  • Enzymatic assays using RNA fragments and full-length 23S rRNA to determine kinetic parameters.

Main Results:

Related Experiment Videos

  • A 262-nucleotide RNA fragment from domain V of B. subtilis 23S rRNA was efficiently methylated by ErmC' at A-2085.
  • The apparent Km for the RNA fragment was 26-fold higher, and Vmax increased sevenfold compared to full-size rRNA.
  • Kinetic data suggest a model of RNA-ErmC' interaction involving multiple binding sites.

    • Conclusions:

    • ErmC' can efficiently methylate a specific domain V rRNA fragment.
    • The kinetic data provide insights into the mechanism of RNA-ErmC' binding and methylation.
    • A model for RNA-ErmC' interaction is proposed based on the observed kinetics.