Phosphorylation and DNA binding of the octamer binding transcription factor Oct-3

Biochem Biophys Res Commun. 1995 Jul 26;212(3):847-53. doi: 10.1006/bbrc.1995.2046.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alkaline Phosphatase / metabolism
  • Animals
  • Binding Sites
  • Cattle
  • Cell Line
  • DNA / metabolism*
  • DNA-Binding Proteins / chemistry
  • DNA-Binding Proteins / genetics
  • DNA-Binding Proteins / metabolism*
  • Octamer Transcription Factor-3
  • Phosphorylation
  • Protein Processing, Post-Translational
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Transcription Factors / chemistry
  • Transcription Factors / genetics
  • Transcription Factors / metabolism*

Substances

  • DNA-Binding Proteins
  • Octamer Transcription Factor-3
  • Recombinant Proteins
  • Transcription Factors
  • DNA
  • Alkaline Phosphatase