The SNF1 kinase complex from Saccharomyces cerevisiae phosphorylates the transcriptional repressor protein Mig1p in vitro at four sites within or near regulatory domain 1.

Mig1p is a zinc finger protein required for repression of glucose-regulated genes in budding yeast. On removal of medium glucose, gene repression is relieved via a mechanism that requires the SNF1 protein kinase complex. We show that Mig1p expressed as a glutathione-S-transferase fusion in bacteria is readily phosphorylated by the ...
SNF1 kinase in vitro. Four phosphorylation sites were identified, i.e. Ser-222, Ser-278, Ser-311 and Ser-381. The latter three are exact matches to the recognition motif we previously defined for SNF1 and lie within regions shown to be required for SNF1-dependent derepression and nuclear-to-cytoplasmic translocation.
Mesh Terms:
Aspartic Acid, DNA-Binding Proteins, Enzyme Repression, Gene Expression Regulation, Fungal, Glucose, Glutamic Acid, Glutathione Transferase, Kluyveromyces, Mutagenesis, Site-Directed, Phosphorylation, Protein-Serine-Threonine Kinases, Recombinant Fusion Proteins, Regulatory Sequences, Nucleic Acid, Repressor Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Serine, Substrate Specificity
FEBS Lett.
Date: Jun. 18, 1999
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