The SNF1 kinase complex from Saccharomyces cerevisiae phosphorylates the transcriptional repressor protein Mig1p in vitro at four sites within or near regulatory domain 1
Fc. Smith et al., The SNF1 kinase complex from Saccharomyces cerevisiae phosphorylates the transcriptional repressor protein Mig1p in vitro at four sites within or near regulatory domain 1, FEBS LETTER, 453(1-2), 1999, pp. 219-223
Mig1p is a zinc finger protein required for repression of glucose-regulated
genes in Budding yeast. On removal of medium glucose, gene repression is r
elieved via a mechanism that requires the SNF1 protein kinase complex, We s
how 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 lat
ter three are exact matches to the recognition motif we previously defined
for SNF1 and lie within regions shown to be required for SNF1-dependent der
epression and nuclear-to-cytoplasmic translocation, (C) 1999 Federation of
European Biochemical Societies.