Analysis of second-site mutations that suppress the multiple drug resistance phenotype of the yeast PDR1-7 allele

Thomas M. McGuire, Elvira Carvajal, David Katzmann, Marisa Wagner, W. Scott Moye-Rowley, André Goffeau, John Golin

Research output: Contribution to journalArticlepeer-review

7 Scopus citations

Abstract

The yeast PDR1 locus encodes a member of the C6 zinc cluster family of transcriptional regulatory proteins. Among the targets of PDR1 is the yeast PDR5 locus. The product of this gene is a member of the ATP-binding cassette (ABC) transmembrane protein family and plays a major role in inhibitor efflux. Mutations in PDR1 affect the relative level of PDR5 transcript and can therefore result in increased or decreased drug resistance. We isolated three second-site suppressors of PDR1-7 semidominant hyper-resistant mutation. These mutants were drug hypersensitive, as compared with isogenic controls. Two of the three mutations contained alterations in a putative DNA-binding domain. Significantly, the mutant proteins exhibited reduced DNA-binding capacity.

Original languageEnglish (US)
Pages (from-to)151-155
Number of pages5
JournalGene
Volume167
Issue number1-2
DOIs
StatePublished - Dec 29 1995

Keywords

  • ABC
  • ATP-binding cassette
  • PDR genes
  • Saccharomyces cerevisiae
  • transcription factor
  • transmembrane

ASJC Scopus subject areas

  • Genetics

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