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Related Experiment Videos

Integron-sequestered dihydrofolate reductase: a recently redeployed enzyme.

Hernán Alonso1, Jill E Gready

  • 1Division of Molecular Bioscience, John Curtin School of Medical Research, Australian National University, Canberra, ACT 0200, Australia.

Trends in Microbiology
|April 6, 2006
PubMed
Summary

The bacterial enzyme DfrB dihydrofolate reductase (DHFR), conferring trimethoprim resistance, is poorly adapted. Recent studies suggest its novel function arose due to selective pressure from antibacterial drug use.

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Area of Science:

  • Microbiology
  • Enzymology
  • Evolutionary Biology

Background:

  • The widespread use of antibacterial drugs has led to the emergence of resistant organisms.
  • DfrB dihydrofolate reductase (DHFR) is a bacterial enzyme conferring resistance to trimethoprim, often found on mobile gene cassettes within integrons.
  • This enzyme has been of interest for over 30 years due to its simple structure, low efficiency, and trimethoprim insensitivity.

Purpose of the Study:

  • To present a comprehensive discussion of genetic, evolutionary, structural, and functional studies of the DfrB DHFR enzyme.
  • To explore the origins and adaptations of DfrB DHFR in response to selective pressures.

Main Methods:

  • Review and synthesis of existing genetic studies.
  • Analysis of evolutionary data.

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  • Examination of structural and functional data.

    • Main Results:

    • DfrB DHFR is characterized as a poorly adapted catalyst.
    • Evidence suggests recent recruitment of DfrB DHFR for a novel enzymatic activity.
    • The enzyme's characteristics are linked to selective pressures, likely from antibacterial drug use.

    Conclusions:

    • DfrB DHFR's properties indicate it is not optimally evolved for its catalytic role.
    • The enzyme likely acquired its current function relatively recently under evolutionary pressure.
    • Understanding DfrB DHFR provides insights into bacterial resistance mechanisms and enzyme evolution.