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| MOUSE RETINOID-X RECEPTOR CONTAINS A SEPARABLE LIGAND-BINDING AND TRANSACTIVATION DOMAIN IN ITS E-REGION |
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| Author(s): LENG XH, BLANCO J, TSAI SY, OZATO K, OMALLEY BW, TSAI MJ |
| Source: MOLECULAR AND CELLULAR BIOLOGY Volume: 15 Issue: 1 Pages: 255-263 Published: JAN 1995 |
| Times Cited: 91 References: 54 |
| Abstract: Steroid, thyroid, and retinoid hormones exert their biological functions by interacting with their cognate nuclear receptors. Upon binding receptors, hormones induce a protease-resistant structural change in the receptor ligand-binding domain and subsequently activate the receptors. Utilizing partial proteolysis, we have been able to delineate a region in the mouse retinoid X receptor beta (mRXR beta) required for ligand binding. A separable activation domain within the mRXR beta E region has been identified. The activation domain, which is 21 amino acids in length, is located at the extreme C terminus of mRXR beta. This domain is not required for ligand binding since removal of this sequence neither eliminates the ligand-induced, protease-resistant conformational change nor alters the ligand-enhanced DNA binding. Furthermore, deletion of this activation domain converts the receptor into a transcriptional silencer. Finally, a further truncation of 9 amino acids (for a total of 30 amino acids) from the C terminus results in a mutant which does not undergo the protease-resistant conformational change and cannot bind DNA as a homodimer. Nevertheless, this mutant is still able to form a heterodimer with the thyroid hormone receptor. Therefore, homodimerization and heterodimerization can be distinguished by this nine-amino-acid sequence. |
| Document Type: Article |
| Language: English |
Addresses:
1. BAYLOR COLL MED, DEPT CELL BIOL, HOUSTON, TX 77030 USA
2. NICHHD, MOLEC GROWTH REGULAT LAB, BETHESDA, MD 20892 USA |
| Publisher: AMER SOC MICROBIOLOGY, 1325 MASSACHUSETTS AVENUE, NW, WASHINGTON, DC 20005-4171 |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: PX953 |
| ISSN: 0270-7306 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |