The 70-kilodalton adenylyl cyclase-associated protein is not essential for interaction of Saccharomyces cerevisiae adenylyl cyclase with RAS proteins.

摘要: In the yeast Saccharomyces cerevisiae, adenylyl cyclase is regulated by RAS proteins. We show here that forms at least two high-molecular-weight complexes, one with protein-dependent activity and other Mn(2+)-dependent activity, which are separable their size difference. The 70-kDa cyclase-associated protein (CAP) existed in former complex but not latter. Missense mutations conserved motifs of leucine-rich repeats catalytic subunit abolished RAS-dependent was accompanied formation a very high molecular weight having activity. Contrary to previous results, disruption gene encoding CAP did alter extent activation cyclase, while concomitant decrease RAS-responsive observed. These results indicate essential for interaction proteins even though it an inherent component complex.