Phosphorylation and DNA binding of the octamer binding transcription factor Oct-3.
Phosphorylation influences DNA binding and transactivator capabilities of multiple transcription factors. In this study, we demonstrate that the POU-domain transcription factor, Oct-3, can be phosphorylated in vivo. In addition, we show that in COS-1 cells Oct-3 is phosphorylated exclusively on serine residues. Lastly, we provide evidence that phosphorylation is not required for Oct-3 binding to DNA and treatment of Oct-3 with calf intestinal alkaline phosphatase does not influence its ability to bind DNA.
Rosfjord
E
E
Eppley Institute for Research in Cancer and Allied Diseases, University of Nebraska Medical Center, Omaha 68198-6805, USA.
Scholtz
B
B
Lewis
R
R
Rizzino
A
A
D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002460:Cell Line; D004247:DNA / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D050814:Octamer Transcription Factor-3; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014157:Transcription Factors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D004268:DNA-Binding Proteins; D050814:Octamer Transcription Factor-3; D011994:Recombinant Proteins; D014157:Transcription Factors; D004247:DNA; D000469:Alkaline Phosphatase