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Related Experiment Videos

Retinoid X receptor alpha forms tetramers in solution

S Kersten1, D Kelleher, P Chambon

  • 1Cornell University, Division of Nutritional Sciences, Ithaca, NY 14853-6301, USA.

Proceedings of the National Academy of Sciences of the United States of America
|September 12, 1995
PubMed
Summary

Retinoid X receptor alpha (RXR) forms stable homodimers and homotetramers in solution. Tetramer formation is high-affinity, becoming the dominant species above 70 nM, suggesting a role in gene transcription regulation.

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Area of Science:

  • Molecular biology
  • Biochemistry
  • Genetics

Background:

  • Protein-protein interactions are crucial for retinoid X receptor (RXR) function in gene transcription.
  • RXR acts as a homo- or heterodimer to mediate hormonal effects on gene expression.

Purpose of the Study:

  • To systematically investigate the oligomeric state of RXR alpha in solution without a DNA template.
  • To elucidate the formation and affinity of RXR alpha dimers and tetramers.

Main Methods:

  • Electrophoresis under nondenaturing conditions.
  • Chemical crosslinking to analyze protein complexes.
  • Fluorescence anisotropy studies to determine dissociation constants.

Main Results:

Related Experiment Videos

  • RXR alpha exists as both homodimers and homotetramers in solution.
  • High-affinity tetramer formation was observed.
  • Tetramers become the predominant RXR species at concentrations above approximately 70 nM.

    • Conclusions:

    • RXR alpha forms stable homodimers and homotetramers.
    • Tetramer formation represents a significant oligomeric state for RXR.
    • Tetramerization may offer an additional regulatory mechanism for RXR-mediated gene transcription.