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Redox regulation of fos and jun DNA-binding activity in vitro

C Abate1, L Patel, F J Rauscher

  • 1Department of Molecular Oncology and Virology, Roche Institute of Molecular Biology, Nutley, NJ 07110.

Science (New York, N.Y.)
|September 7, 1990
PubMed

Insights

Proto-oncogenes c-fos and c-jun form a Fos-Jun complex regulating gene transcription. This DNA binding is controlled by redox mechanisms and a novel nuclear protein, suggesting redox regulation of AP-1 transcription factors.

Area of Science:

  • Molecular Biology
  • Cell Signaling
  • Gene Regulation

Background:

  • Proto-oncogenes c-fos and c-jun are key inducible transcription factors in cellular signaling pathways.
  • Their protein products, Fos and Jun, form heterodimers that bind to the activator protein-1 (AP-1) DNA regulatory site.

Purpose of the Study:

  • To investigate the mechanism regulating DNA binding of the Fos-Jun heterodimer.
  • To explore the role of redox status and novel nuclear factors in modulating AP-1 transcriptional activity.

Main Methods:

  • Investigated protein-protein interactions and DNA binding of Fos and Jun proteins.
  • Analyzed the effect of reduction-oxidation (redox) on DNA binding.
  • Identified and characterized a nuclear protein influencing Fos-Jun DNA binding in vitro.

Main Results:

  • Fos-Jun heterodimerization and DNA binding are modulated by the redox state of a conserved cysteine residue.
  • A novel nuclear protein was identified that reduces Fos-Jun and enhances their DNA-binding activity.
  • These findings indicate a redox-sensitive mechanism controlling AP-1 transcriptional regulation.

Conclusions:

  • Transcriptional activity mediated by AP-1 factors is subject to redox regulation.
  • A newly identified nuclear protein plays a role in modulating AP-1 DNA binding through a redox-dependent mechanism.

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