DEFAR - Departamento de Farmácia
URI permanente desta comunidadehttp://www.hml.repositorio.ufop.br/handle/123456789/530
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Item Molecular cloning of a gene involved in glucose sensing in the yeast Saccharomyces cerevisiae.(1993) Aelst, Linda Van; Hohmann, Stefan; Bulaya, Botchaka; Koning, Wim de; Sierkstra, Laurens; Neves, Maria José; Luyten, Kattie; Alijo, Rafael; Ramos, José; Coccetti, Paola; Martegani, Enzo; Rocha, Neuza Maria de Magalhaes; Brandão, Rogélio Lopes; Dijck, Patrick Van; Vanhalewyn, Mieke; Durnez, Peter; Jans, Arnold W. H; Thevelein, Johan MariaCells of the yeast Saccharomyces cerevisiae display a wide range of glucose-induced regulatory phenomena, including glucose-induced activation of the RAS-adenylate cyclase pathway and phosphatidylinosrtot turnover, rapid post-translatronal effects on the activity of different enzymes as well as long-term effects at the transcriptional level. A gene called GGS1 (for general Glucose Sensor) that is apparently required for the glucose-induced regulatory effects and several ggsi aHeles (fic/pf, bypi and cifi) has been cloned and characterized. A GGS1 homologue is present in Methanobacterium thermoautotrophicum. Yeast ggsi mutants are unable to grow on glucose or Received 25 November, 1992; revised and accepted 15 February, 1993. •For correspondence. Tel. (16) 220931; Fax (16) 204415. tThese two authors contributed equally to this paper. related readily fermentable sugars, apparently owing to unrestricted influx of sugar Into glycolysis, resulting in its rapid deregulation. Levels of intracellular free glucose and metabolites measured over a period of a few minutes after addition of glucose to cells of a ggsi^ strain are consistent with our previous suggestion of a functional interaction between a sugar transporter, a sugar kinase and the GGS1 gene product. Such a glucose-sensing system might both restrict the influx of glucose and activate several signal transduction pathways, leading to the wide range of glucose-induced regulatory phenomena. Deregulation of these pathways in ggsi mutants might explain phenotypic defects observed in the absence of glucose, e.g. the inability of ggsi diploids to sporulate.Item Possible involvement of a phosphatidylinositol-type signaling pathway in glucose-induced activation of plasma membrane ATPase and cellular proton in the yeast Sacchamyces cerevisiae.(1994) Brandão, Rogélio Lopes; Rocha, Neuza Maria de Magalhaes; Alijo, Rafael; Ramos, José; Thevelein, Johan MariaAddition of glucose to cells of the yeast Saccharomyces cerevisiae causes rapid activation of plasma membrane H+-ATPase and a stimulation of cellular H ÷ extrusion. We show that addition of diacylglycerol and other activators of protein kinase C to intact cells also activates the H+-ATPase and causes at the same time a stimulation of H ÷ extrusion from the cells. Both effects are reversed by addition of staurosporine, a protein kinase C inhibitor. Addition of staurosporine or calmidazolium, an inhibitor of Ca2+/calmodulin-dependent protein kinases, separately, causes a partial inhibition of glucose-induced H+-ATPase activation and stimulation of cellular H + extrusion; together they cause a more potent inhibition. Addition of neomycin, which complexes with phosphatidylinositol 4,5-bisphosphate, or addition of compound 48/80, a phospholipase C inhibitor, also causes near complete inhibition. Diacylglycerol and other protein kinase C activators had no effect on the activity of the K+-uptake system and the activity of trehalase and glucose-induced activation of the K+-uptake system and trehalase was not inhibited by neomycin, supporting the specificity of the effects observed on the H+-ATPase. The results support a model in which glucose-induced activation of H+-ATPase is mediated by a phosphatidylinositol-type signaling pathway triggering phosphorylation of the enzyme both by protein kinase C and one or more Ca2+/calmodulin-dependent protein kinases.