Novel alleles of yeast hexokinase PII with distinct effects on catalytic activity and catabolite repression of SUC2

Article Abstract:

Suppressor mutations of the growth defect of a tps1Deltahxk1Delta double mutant on fructose were isolated from the yeast Saccharomyces cerevisiae and identified as unique HXK2 alleles. All six alleles have single amino acid substitutions. Data indicated that the long- and short-term phases of catabolite repression can be dissected utilizing various hexokinase mutations. The absence of correlation between in vitro catalytic hexokinase activity, in vivo sugar phosphate accumulation and the establishment of catabolite repression indicate that the production of sugar phosphate is not the only function of hexokinase in repression.

Sugar, Yeast, Yeast (Food product)

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Constitutive glucose-induced activation of the Ras-cAMP pathway and aberrant stationary-phase entry on a glucose-containing medium in the Saccharomyces cerevisiae glucose-repression mutant hex2

Article Abstract:

The inhibitive character of the glucose-dependent pathway for the synthesis of cAMP in Saccharomyces cerevisiae is necessary for preventing the over production of cAMP so that the cell can enter the stationary phase of growth. Mutant hex2 cells grown on a medium containing glucose lose their viability due to the activation of cAMP synthesis by glucose. A spontaneous mutant shx (suppressor of hex2) is able to grow in conditions of nitrogen starvation in the glucose-containing medium.

Cyclic adenylic acid, Cyclic adenosine monophosphate, Microbial mutation

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The Sch9 protein kinase in the yeast Saccharomyces cerevisiae controls cAPK activity and is required for nitrogen activation of the fermentable-growth-medium-induced (FGM) pathway

Article Abstract:

Research shows that Sch9 protein kinase is needed in yeast Saccharomyces cerevisiae nitrogen-induced activation of the fermentable-growth-medium-induced pathway but is not needed for the glucose-inducted activation of protein kinase A. Its absence enhances cyclic adenosine monophosphate-dependent protein kinase physiological activity.

Protein kinases

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