The CCR1 (SNF1) and SCH9 protein kinases act independently of cAMP-dependent protein kinase and the transcriptional activator ADR1 in controlling yeast ADH2 expression

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Abstract
CAMP-dependent protein kinase (cAPK) is implicated in the inactivation of the yeast transcriptional activator ADR1, which regulates glucose-repressible ADH2 gene expression. The interdependence of cAPK, SCH9 (a protein kinase that when overexpressed can functionally substitute for cAPK), and the CCR1 (SNF1) protein kinase that is required for ADII2 expression was studied. SCH9 was found to be required for ADH2 expression in contrast to the inhibitory role played by cAPK. CCR1 and SCH9 were observed to affect ADH2 expression independently of both ADR1 and cAPK. In contrast, cAPK was shown to exert its effects on ADH2 solely through ADR1. These results indicate that the SCH9 and CCR1 protein kinases are components of regulatory pathways separate from that utilized by cAPK to control ADR1 activity and ADH2 expression.