Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity.

We demonstrated that the DNA-binding activity of Fos and Jun is regulated in vitro by a novel redox mechanism

S. Xanthoudakis; T. Curran

2018

Scholarcy highlights

  • Fos and Jun form a heterodimeric complex that regulates gene transcription by binding to the activator protein-1 DNA sequence motif
  • We demonstrated that the DNA-binding activity of Fos and Jun is regulated in vitro by a novel redox mechanism
  • Ref-1 does not bind to the AP-1 site in association with Fos and Jun, it partially copurifies with a subset of AP-1 proteins
  • Purified Ref-1 protein stimulates activator protein-1 DNA-binding activity through the conserved Cys residues in Fos and Jun, but it does not alter the DNA-binding specificity of Fos and Jun. Ref-1 may represent a novel redox component of the signal transduction processes that regulate eukaryotic gene expression

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