Inhibition of membrane Ca2(+)-ATPase of Saccharomyces cerevisiae by mating pheromone alpha-factor in vitro.
Plasma membrane Ca2(+)-ATPase of Saccharomyces cerevisiae was solubilized and partially purified by calmodulin-affinity chromatography. The activity of Ca2(+)-ATPase isolated from MATa cells was inhibited by physiological concentrations of the mating pheromone alpha-factor in a dose-dependent manner. The enzyme prepared from a receptor-deficient sterile mutant cells (delta ste-2) was similarly inhibited by alpha-factor, but the enzyme from MAT alpha cells was resistant to the mating pheromone. We suggest that the inhibition may be involved in the alpha-factor-induced increase of Ca2+ uptake reaction of MATa cells.
Hiraga
K
K
Department of Fermentation Technology, Faculty of Engineering, Hiroshima University, Japan.
Tahara
H
H
Taguchi
N
N
Tsuchiya
E
E
Fukui
S
S
Miyakawa
T
T
D001426:Bacterial Proteins / Q000494:pharmacology; D000252:Calcium-Transporting ATPases / Q000037:antagonists & inhibitors*; D002462:Cell Membrane / Q000187:drug effects / Q000201:enzymology; D002846:Chromatography, Affinity; D066298:In Vitro Techniques; D000072235:Mating Factor; D009154:Mutation; D010455:Peptides / Q000494:pharmacology*; D010675:Pheromones / Q000494:pharmacology*; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000201:enzymology* / Q000235:genetics; D012995:Solubility
D001426:Bacterial Proteins; D010455:Peptides; D010675:Pheromones; C032677:syringomycin; D000072235:Mating Factor; D000252:Calcium-Transporting ATPases