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Inhibition of membrane Ca2+-ATPase invitro by mating pheromone in Rhodosporidiumtoruloides, a heterobasidiomycetous yeast
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Description
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.
Journal
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- Biochemical and Biophysical Research Communications
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Biochemical and Biophysical Research Communications 143 893-900, 1987-03-01
Elsevier BV
