Regulation of phosphatidylinositol kinase activity in Saccharomyces cerevisiae.

AUTOR(ES)

Holland, K M

RESUMO

The effects of growth phase and carbon source on membrane-associated phosphatidylinositol kinase in cell extracts of Saccharomyces cerevisiae were examined. Phosphatidylinositol kinase activity increased 2- and 2.5-fold in glucose- and glycerol-grown cells, respectively, in the stationary phase as compared with the exponential phase of growth. The increase in phosphatidylinositol kinase activity in the stationary phase of growth correlated with an increase in the relative amounts of phosphatidylinositol 4-phosphate, the product of the reaction. The increase in phosphatidylinositol kinase activity was not due to the presence of water-soluble effector molecules in cell extracts as indicated by mixing experiments. Phosphatidylinositol kinase activity decreased in cell extracts of exponential-phase cells preincubated under phosphorylation conditions which favor cyclic AMP-dependent protein kinase activity. Phosphatidylinositol kinase activity was not affected in cell extracts of stationary-phase cells preincubated under phosphorylation conditions.

Documentos Relacionados

• Membrane-associated phosphatidylinositol kinase from Saccharomyces cerevisiae.
• Regulation of phosphatidylinositol:ceramide phosphoinositol transferase in Saccharomyces cerevisiae.
• Regulation of CDP-diacylglycerol synthase activity in Saccharomyces cerevisiae.
• Regulation of phosphatidate phosphatase activity by inositol in Saccharomyces cerevisiae.
• Developmental regulation of a sporulation-specific enzyme activity in Saccharomyces cerevisiae.