Interaction of Oct-1 and automodification domain of poly(ADP-ribose) synthetase

FEBS Lett. 1998 Mar 6;424(1-2):27-32. doi: 10.1016/s0014-5793(98)00131-8.


We isolated several clones from a matchmaker two-hybrid system human lymphocyte cDNA library using an automodification domain of poly(ADP-ribose) synthetase (PARS) as a probe. A DNA sequence (approximately 1 kbp) of the clone was identical to part of the Oct-1 DNA sequence. We then constructed either a His-tagged or GST fusion protein of the inserted cDNA from the clone and the fusion protein was shown to interact with PARS by far-Western blot analysis and co-precipitation with affinity resin. Furthermore, the His-tagged Oct-1/POU-homeo fusion protein interacted weakly with the octamer motif of the DRa promoter and the addition of PARS fusion protein greatly increased the DNA binding activity. These results suggest that PARS interacts with Oct-1 and stabilizes the binding of Oct-1 to the octamer motif.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Base Sequence
  • Cell Culture Techniques
  • DNA, Complementary / analysis*
  • DNA-Binding Proteins*
  • Homeodomain Proteins / genetics*
  • Homeodomain Proteins / metabolism
  • Host Cell Factor C1
  • Humans
  • Lymphocytes / chemistry
  • Lymphocytes / enzymology
  • Molecular Sequence Data
  • Octamer Transcription Factor-1
  • Poly(ADP-ribose) Polymerases / chemistry
  • Poly(ADP-ribose) Polymerases / genetics*
  • Poly(ADP-ribose) Polymerases / metabolism
  • Protein Conformation
  • Sequence Alignment
  • Transcription Factors / genetics*
  • Transcription Factors / metabolism


  • DNA, Complementary
  • DNA-Binding Proteins
  • HCFC1 protein, human
  • Homeodomain Proteins
  • Host Cell Factor C1
  • Octamer Transcription Factor-1
  • POU2F1 protein, human
  • Transcription Factors
  • Poly(ADP-ribose) Polymerases