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Ref-1 controls pax-8 DNA-binding activity

G Tell1, L Pellizzari, D Cimarosti

  • 1Dipartimento di Scienze e Tecnologie Biomediche, Università degli Studi di Udine, via Gervasutta 48, Udine, 33100, Italy. immunoud@dstb.uniud.it

Biochemical and Biophysical Research Communications
|November 14, 1998
PubMed
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Redox factor-1 (Ref-1) enhances the DNA-binding activity of the Pax-8 paired domain in vitro. This redox regulation of Pax-8 DNA binding may control gene function in vivo and is conserved across species.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Redox potential influences transcription factor DNA-binding activity.
  • Nuclear factor Ref-1 mediates redox regulation of DNA binding for some transcription factors.

Purpose of the Study:

  • To investigate the effect of Ref-1 on the DNA-binding activity of the Pax-8 paired domain.
  • To explore the potential in vivo relevance of redox regulation for Pax-8 function.

Main Methods:

  • In vitro assays to assess Ref-1's effect on Pax-8 DNA binding.
  • Co-transfection experiments to evaluate Pax-8's transcriptional activity.
  • Immunoreactivity analysis of nuclear extracts from thyroid cells.

Main Results:

Related Experiment Videos

  • Ref-1 was shown to induce the DNA-binding activity of the Pax-8 paired domain in vitro.
  • Ref-1 enhanced the Pax-8 activating effect on the thyroglobulin promoter in co-transfection assays.
  • Thyroid cell nuclear extracts showed a correlation between Ref-1 levels and reduced Pax-8.

Conclusions:

  • Redox regulation of Pax-8 DNA-binding activity by Ref-1 is demonstrated in vitro and may control Pax protein function in vivo.
  • Conserved cysteine residues in paired domains suggest widespread phylogenetic conservation of redox regulation for DNA binding.