Redox Regulation of Fos and Jun DNA-Binding Activity in Vitro

DOI Web Site 被引用文献15件
  • Cory Abate
    Department of Molecular Oncology and Virology, Roche Institute of Molecular Biology, Nutley, NJ 07110.
  • Lekha Patel
    Department of Molecular Oncology and Virology, Roche Institute of Molecular Biology, Nutley, NJ 07110.
  • Frank J. Rauscher
    Department of Molecular Oncology and Virology, Roche Institute of Molecular Biology, Nutley, NJ 07110.
  • Tom Curran
    Department of Molecular Oncology and Virology, Roche Institute of Molecular Biology, Nutley, NJ 07110.

抄録

<jats:p> The proto-oncogenes c- <jats:italic>fos</jats:italic> and c- <jats:italic>jun</jats:italic> function cooperatively as inducible transcription factors in signal transduction processes. Their protein products, Fos and Jun, form a heterodimeric complex that interacts with the DNA regulatory element known as the activator protein-1 (AP-1) binding site. Dimerization occurs via interaction between leucine zipper domains and serves to bring into proper juxtaposition a region in each protein that is rich in basic amino acids and that forms a DNA-binding domain. DNA binding of the Fos-Jun heterodimer was modulated by reduction-oxidation (redox) of a single conserved cysteine residue in the DNA-binding domains of the two proteins. Furthermore, a nuclear protein was identified that reduced Fos and Jun and stimulated DNA-binding activity in vitro. These results suggest that transcriptional activity mediated by AP-1 binding factors may be regulated by a redox mechanism. </jats:p>

収録刊行物

  • Science

    Science 249 (4973), 1157-1161, 1990-09-07

    American Association for the Advancement of Science (AAAS)

被引用文献 (15)*注記

もっと見る

詳細情報 詳細情報について

問題の指摘

ページトップへ