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The SNF1 kinase complex from Saccharomyces cerevisiae phosphorylates the transcriptional repressor protein Mig1p in vitro at four sites within or near regulatory domain 1
Author(s) -
Smith Fiona C.,
Davies Stephen P.,
Wilson Wayne A.,
Carling David,
Hardie D.Grahame
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00725-5
Subject(s) - derepression , biochemistry , saccharomyces cerevisiae , cyclin dependent kinase 7 , repressor , biology , psychological repression , cyclin dependent kinase complex , phosphorylation , mitogen activated protein kinase kinase , autophagy related protein 13 , protein kinase a , fusion protein , zinc finger , microbiology and biotechnology , gene , transcription factor , recombinant dna , gene expression
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.