GAL4 is phosphorylated as a consequence of transcriptional activation.
GAL4 protein isolated from yeast in which it is active is phosphorylated predominantly on two different serine residues. One of these was identified as Ser-837; substitution of this residue for alanine has no detectable effect on transcriptional activation by GAL4. Phosphorylation at Ser-837 requires that both the DNA binding and transcriptional activation functions be intact. We propose that some phosphorylations of GAL4, including that at Ser-837, occur concomitantly with activation of transcription.
Sadowski
I
I
Department of Biochemistry, Faculty of Medicine, University of British Columbia, Vancouver, Canada.
Niedbala
D
D
Wood
K
K
Ptashne
M
M
D000595:Amino Acid Sequence; D001483:Base Sequence; D002872:Chromosome Deletion; D004268:DNA-Binding Proteins; D005656:Fungal Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D008715:Methionine / Q000378:metabolism; D008970:Molecular Weight; D010766:Phosphorylation; D010768:Phosphoserine / Q000378:metabolism; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins; D012694:Serine; D014157:Transcription Factors / Q000378:metabolism*; D014158:Transcription, Genetic
D004268:DNA-Binding Proteins; D005656:Fungal Proteins; C052130:GAL4 protein, S cerevisiae; D011994:Recombinant Proteins; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D010768:Phosphoserine; D012694:Serine; D008715:Methionine