Purification, cloning, and RXR identity of the HeLa cell factor with which RAR or TR heterodimerizes to bind target sequences efficiently

We have purified and cloned a HeLa cell nuclear protein that strongly stimulates binding of retinoic acid and thyroid hormone receptors (RARs and TRs) to response elements. The purified protein is a human retinoid X receptor β (hRXRβ). Three murine members of the RXR family (mRXRα, β, and γ) have al...

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Veröffentlicht in:	Cell 1992-01, Vol.68 (2), p.377-395
Hauptverfasser:	Leid, Mark, Kastner, Philippe, Lyons, Ruth, Nakshatri, Harikrishna, Saunders, Michael, Zacharewski, Tim, Chen, Jia-Yang, Staub, Adrien, Garnier, Jean-Marie, Mader, Sylvie, Chambon, Pierre
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Base Sequence Binding Sites Carrier Proteins - metabolism Cloning, Molecular DNA - metabolism HeLa Cells Humans Macromolecular Substances Molecular Sequence Data Nuclear Proteins - genetics Nuclear Proteins - isolation & purification Nuclear Proteins - metabolism Precipitin Tests Receptors, Cell Surface - genetics Receptors, Cell Surface - isolation & purification Receptors, Cell Surface - metabolism Receptors, Retinoic Acid Receptors, Thyroid Hormone - metabolism Regulatory Sequences, Nucleic Acid - genetics Regulatory Sequences, Nucleic Acid - physiology Repetitive Sequences, Nucleic Acid - genetics Repetitive Sequences, Nucleic Acid - physiology Retinoid X Receptors Signal Transduction Transcription Factors Tretinoin - metabolism
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