Open AccessInteractions between the gene products of pma1 encoding plasma membrane H(+)-ATPase, and pdr1 controlling multiple drug resistance in Saccharomyces cerevisiae.
Author(s) -
Stanisław Ułaszewski
Publication year - 1993
Publication title -
acta biochimica polonica
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.452
H-Index - 78
eISSN - 1734-154X
pISSN - 0001-527X
DOI - 10.18388/abp.1993_4789
Subject(s) - saccharomyces cerevisiae , vanadate , mutant , cycloheximide , gene , atpase , gene product , microbiology and biotechnology , mutation , yeast , biology , genetics , chemistry , biochemistry , gene expression , enzyme , protein biosynthesis
In Saccharomyces cerevisiae, the pma1 mutations controlling the vanadate resistance of the H(+)-ATPase activity from the plasma membrane, map on chromosome VII in the vicinity of pdr1 mutations controlling multiple drug resistance. However, the pma1-1 mutants exhibit a genotype and a multidrug resistant phenotype quite different from those obtained for pdr1 mutants. Quantitative modifications of cycloheximide and N,N'-(p-xylylidene)-bis-aminoguanidine-2HCl resistance are observed in diploids containing the pma1 and pdr1 genes in trans configuration. Each of the pdr1 mutations interacts with pma1 as shown by a decrease in the ATPase activity in pdr1/pma1 diploids. The in vitro resistance of ATPase activity to vanadate is totally or partially suppressed in pdr1 mutants in haploid double mutants. These results suggest that the expression of PMA1 might be controlled by the PDR1 gene product.