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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.
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.
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:
- 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.
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