Inhibition of membrane Ca2+-ATPase in vitro by mating pheromone in Rhodosporidium toruloides, a heterobasidiomycetous yeast.
Direct addition of physiological concentrations of rhodotorucine A, a lipopeptide mating pheromone of Rhodosporidium toruloides, to the particulate fraction of the target cell strongly inhibited Ca2+-ATPase activity. The pheromone effect was mating-type specific. Membrane Ca2+-ATPase solubilized by a nonionic detergent and further purified by calmodulin-affinity chromatography was also inhibited by the pheromone. Rhodotorucine A S-oxide, a biologically inactive analogue, had no effect on Ca2+-ATPase. The results suggested that the inhibition of membrane Ca2+-ATPase is a critical event in the signaling of mating pheromone and the inhibition of membrane Ca2+-pump could be responsible for the pheromone-induced rapid raise of intracellular Ca2+ concentration reported.
D001487:Basidiomycota / Q000166:cytology / Q000187:drug effects* / Q000201:enzymology; D000252:Calcium-Transporting ATPases / Q000037:antagonists & inhibitors*; D009842:Oligopeptides / Q000494:pharmacology*; D010675:Pheromones / Q000494:pharmacology; D013347:Subcellular Fractions / Q000201:enzymology
D009842:Oligopeptides; D010675:Pheromones; C017944:rhodotorucine A; D000252:Calcium-Transporting ATPases