title: Cyclic AMP controls the plasma membrane H+-ATPase activity from Saccharomyces cerevisiae.
abstract: The thermosensitive G1-arrested cdc35-10 mutant from Saccharomyces cerevisiae, defective in adenylate cyclase activity, was shifted to restrictive temperature. After 1 h incubation at this temperature, the plasma membrane H+-ATPase activity of cdc35-10 was reduced to 50%, whereas that in mitochondria doubled. Similar data were obtained with cdc25, another thermosensitive G1-arrested mutant modified in the cAMP pathway. In contrast, the ATPase activities of the G1-arrested mutant cdc19, defective in pyruvate kinase, were not affected after 2 h incubation at restrictive temperature. In the double mutants cdc35-10 cas1 and cdc25 cas1, addition of extracellular cAMP prevented the modifications of ATPase activities observed in the single mutants cdc35-10 and cdc25. These data indicate that cAMP acts as a positive effector on the H+-ATPase activity of plasma membranes and as a negative effector on that of mitochondria.
authors.affiliation: Laboratoire d'Enzymologie, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.
authors.forename: S
authors.initials: S
authors.lastname: Ulaszewski
authors.forename: F
authors.initials: F
authors.lastname: Hilger
authors.forename: A
authors.initials: A
authors.lastname: Goffeau
mesh_terms: D000262:Adenylyl Cyclases / Q000235:genetics / Q000378:metabolism; D002462:Cell Membrane / Q000201:enzymology; D000242:Cyclic AMP / Q000494:pharmacology*; D006358:Hot Temperature; D007399:Interphase; D008928:Mitochondria / Q000201:enzymology; D009154:Mutation; D010641:Phenotype; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D011770:Pyruvate Kinase / Q000235:genetics / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics
chemical_list: D000242:Cyclic AMP; D011770:Pyruvate Kinase; D006180:Proton-Translocating ATPases; D000262:Adenylyl Cyclases