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Cyclic AMP-dependent protein kinase phosphorylates and inactivates the yeast transcriptional activator ADR1

J R Cherry1, T R Johnson, C Dollard

  • 1Department of Biochemistry, University of New Hampshire, Durham 03824.

Cell
|February 10, 1989
PubMed

Insights

The yeast transcriptional activator ADR1 is phosphorylated by a specific kinase, suggesting this process regulates gene transcription. Mutations affecting ADR1

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Yeast Genetics

Background:

  • Gene transcription regulation in eukaryotes often involves the phosphorylation of transcription factors.
  • The specific mechanisms of glucose repression in yeast, particularly concerning the ADH2 gene, require further elucidation.

Purpose of the Study:

  • To investigate the role of phosphorylation in the regulation of the yeast transcriptional activator ADR1.
  • To determine the relationship between ADR1 phosphorylation, ADH2 gene expression, and glucose repression.

Main Methods:

  • In vitro phosphorylation assays using purified yeast transcriptional activator ADR1 and cyclic AMP-dependent protein kinase.
  • Analysis of ADR1 phosphorylation levels in yeast strains with specific ADR1 mutations.
  • In vivo studies assessing the impact of altered kinase activity on ADH2 expression.

Main Results:

  • The yeast transcriptional activator ADR1 is phosphorylated in vitro by cyclic AMP-dependent protein kinase.
  • Mutations enhancing ADR1's ability to activate ADH2 expression are correlated with decreased ADR1 phosphorylation.
  • Increased in vivo kinase activity inhibits ADH2 expression in an ADR1 allele-specific manner.

Conclusions:

  • Suggests that glucose repression of ADH2 gene expression is, in part, mediated by cAMP-dependent phosphorylation of the ADR1 protein.
  • Phosphorylation appears to inactivate the ADR1 regulatory protein, thereby downregulating ADH2 expression under specific conditions.

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