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Volume 272, Number 19, Issue of May 9, 1997 pp. 12771-12777
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

The DNA Binding Pattern of the Retinoid X Receptor Is Regulated by Ligand-dependent Modulation of Its Oligomeric State

(Received for publication, February 3, 1997, and in revised form, March 5, 1997)

Sander Kersten , Hinrich Gronemeyer Dagger and Noa Noy

From Cornell University, Division of Nutritional Sciences, Savage Hall, Ithaca, New York 14853-6301, and the Dagger  Institut de Génétique et de Biologie Moléculaire et Cellulaire, BP 163, F-67404 Illkirch Cedex, France

The retinoid X receptor (RXR) regulates target gene transcription via its association with cognate DNA response elements either as a homodimer or as a heterodimer with a number of other nuclear receptors. We previously demonstrated that, in solution, RXR forms tetramers with a high affinity and that ligand binding leads to dissociation of receptor tetramers to smaller species. Here it is shown that RXR tetramers form stable complexes with direct repeats (DR-1 or DR-5) or palindromic (TREpal) response elements. Binding of RXR tetramers to cognate DNA occurs with a significantly higher affinity as compared with dimers. Ligand binding by DNA-bound RXR tetramers results in their dissociation to DNA-bound dimers, a process that is completely reversed upon removal of the ligand. Formation of stable tetramer-DNA complexes requires binding of two oligonucleotides/tetramer. It is proposed that ligand-dependent modulation of the oligomeric state of RXR is a regulatory feature of this nuclear receptor.


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Copyright © 1997 by the American Society for Biochemistry and Molecular Biology.