The yeast PDR1 locus encodes a member of the C6 zinc cluster family of transciptional 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 a 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.
McGuire, T., Carvajal, E., Katzmann, D., Wagner, M., Moyerowley, WS., Goffeau, A., & Golin, J. (1995). Analysis of second-site mutations that suppress the multiple drug resistance phenotype of the yeast PDR1-7 allele. Gene, 167(1-2), 151-155. https://doi.org/10.1016/0378-1119(95)00663-X (Original work published 1995)