Phosphorylation and DNA Binding of the Octamer Binding Transcription Factor OCT-3

E. Rosfjord, B. Scholtz, R. Lewis, A. Rizzino

Research output: Contribution to journalArticle

4 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)847-853
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume212
Issue number3
DOIs
Publication statusPublished - Jul 26 1995

Fingerprint

Octamer Transcription Factors
Transcription Factor 3
Phosphorylation
Transcription Factors
Octamer Transcription Factor-3
DNA
POU Domain Factors
Trans-Activators
COS Cells
Serine
Alkaline Phosphatase

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology
  • Biophysics
  • Biochemistry

Cite this

Phosphorylation and DNA Binding of the Octamer Binding Transcription Factor OCT-3. / Rosfjord, E.; Scholtz, B.; Lewis, R.; Rizzino, A.

In: Biochemical and Biophysical Research Communications, Vol. 212, No. 3, 26.07.1995, p. 847-853.

Research output: Contribution to journalArticle

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