| Literature DB >> 1961715 |
I Sadowski1, D Niedbala, K Wood, M Ptashne.
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.Entities:
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Year: 1991 PMID: 1961715 PMCID: PMC52958 DOI: 10.1073/pnas.88.23.10510
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN: 0027-8424 Impact factor: 11.205