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

      Science (New York, N.Y.)
      Amino Acid Sequence, Animals, Cell-Free System, Cysteine, physiology, DNA Mutational Analysis, DNA-Binding Proteins, drug effects, Diamide, pharmacology, Humans, In Vitro Techniques, Molecular Sequence Data, Oxidation-Reduction, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-fos, Proto-Oncogene Proteins c-jun, Rats, Recombinant Proteins, Signal Transduction, Structure-Activity Relationship, Sulfhydryl Reagents, Transcription Factors

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          Abstract

          The proto-oncogenes c-fos and c-jun 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.

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