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Loss of function mutation in the yeast multiple drug resistance gene PDR5 causes a reduction in chloramphenicol

P J Leonard1, P K Rathod, J Golin

  • 1Department of Biology, Catholic University of America, Washington, D.C. 20064.

Antimicrobial Agents and Chemotherapy
|October 1, 1994
PubMed

Insights

The yeast PDR5 gene product, a transporter similar to human multidrug resistance proteins, is crucial for chloramphenicol efflux. Loss of PDR5 function causes hypersensitivity and impaired drug transport.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • The PDR5 gene in Saccharomyces cerevisiae encodes a protein belonging to the ATP-binding cassette (ABC) transporter superfamily.
  • This transporter shares homology with human multidrug resistance proteins like MDR1 p-glycoprotein.
  • Understanding PDR5 function is key to comprehending drug resistance mechanisms in yeast.

Purpose of the Study:

  • To investigate the role of the yeast PDR5 gene product in chloramphenicol transport.
  • To characterize the impact of PDR5 loss-of-function mutations on chloramphenicol sensitivity and efflux.

Main Methods:

  • Utilizing a pdr5::Tn5 loss-of-function mutant in Saccharomyces cerevisiae.
  • Comparing chloramphenicol efflux in the mutant strain versus an isogenic wild-type PDR5 strain.
  • Phenotypic analysis of chloramphenicol hypersensitivity.

Main Results:

  • Loss-of-function mutations in PDR5 lead to hypersensitivity to chloramphenicol.
  • The pdr5 mutant exhibited significantly impaired efflux of chloramphenicol compared to wild-type cells.
  • The PDR5 gene product is essential for efficient chloramphenicol export.

Conclusions:

  • The Saccharomyces cerevisiae PDR5 gene product is a critical efflux transporter for chloramphenicol.
  • Disruption of PDR5 function compromises the yeast's ability to export chloramphenicol, leading to cellular hypersensitivity.
  • PDR5 represents a potential target for modulating drug sensitivity in yeast systems.

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