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. 1991 Dec 1;88(23):10510–10514. doi: 10.1073/pnas.88.23.10510

GAL4 is phosphorylated as a consequence of transcriptional activation.

I Sadowski 1, D Niedbala 1, K Wood 1, M Ptashne 1
PMCID: PMC52958  PMID: 1961715

Abstract

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.

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