Comparative studies between the glucose-induced phosphorylation signal and the heat shock response in mutants of Saccharomyces cerevisiae.
Addition of glucose to derepressed yeast cells, as well as a heat shock treatment, trigger the phosphorylation of trehalase and of trehalose-6-phosphate synthase. In the present paper, evidence is provided for the requirement of the RAS protein in the transduction of the glucose signal. On the other hand, a heat shock at 52 degrees C for 2 min was able to produce a significant phosphorylating effect even in mutant strains deficient in the GTP binding protein. Moreover, it was shown that this treatment does not affect exclusively the cAMP-dependent protein kinase. The use of a series of mutant strains confirmed that low levels of cAMP favor thermotolerance; the role of trehalose in yeast viability is also discussed.
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Departamento de Bioquimica, Universidade Federal do Rio de Janeiro, Brazil.
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Panek
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D000242:Cyclic AMP / Q000378:metabolism; D011905:Genes, ras; D005947:Glucose / Q000494:pharmacology*; D006358:Hot Temperature; D009154:Mutation; D010766:Phosphorylation; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D014198:Trehalase / Q000378:metabolism; D014199:Trehalose / Q000378:metabolism
D014199:Trehalose; D000242:Cyclic AMP; D014198:Trehalase; D005947:Glucose