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Originally published In Press as doi:10.1074/jbc.M108491200 on December 31, 2001

J. Biol. Chem., Vol. 277, Issue 10, 8702-8707, March 8, 2002
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Differential Modulation of DNA Conformation by Estrogen Receptors alpha  and beta *

Jennifer R. SchultzDagger §, Margaret A. LovenDagger , Vida M. Senkus Melvin, Dean P. Edwards||, and Ann M. NardulliDagger **

From the Dagger  Department of Molecular and Integrative Physiology, University of Illinois, Urbana, Illinois 61801, and the  Molecular Biology Program and the || Department of Pathology, University of Colorado, Denver, Colorado 80262

The human estrogen receptor (ER) induces transcription of estrogen-responsive genes upon binding to estrogen and the estrogen response element (ERE). To determine whether receptor-induced changes in DNA structure are related to transactivation, we compared the abilities of ERalpha and ERbeta to activate transcription and induce distortion and bending in DNA. ERalpha induced higher levels of transcription than ERbeta in the presence of 17beta -estradiol. In circular permutation experiments ERalpha induced greater distortion in DNA fragments containing the consensus ERE sequence than ERbeta . Phasing analysis indicated that ERalpha induced a bend directed toward the major groove of the DNA helix but that ERbeta failed to induce a directed DNA bend. Likewise, the ERalpha DNA binding domain (DBD) and hinge region induced a bend directed toward the major groove of the DNA helix, but the ERbeta DBD and hinge region failed to bend ERE-containing DNA fragments. Using receptor chimeras we demonstrated that the ERalpha DBD C-terminal extension is required for directed DNA bending. Transient transfection assays revealed that appropriately oriented DNA bending enhances receptor-mediated transactivation. The different abilities of ERalpha and ERbeta to induce change in DNA structure could foster or inhibit the interaction of regulatory proteins with the receptor and other transcription factors and help to explain how estrogen-responsive genes are differentially regulated by these two receptors.

* This work was supported by National Institutes of Health Grant DK 53884 (to A. M. N.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by National Institutes of Health Cell and Molecular Biology Training Grant (T32 GM07283).

** To whom correspondence should be addressed: Dept. of Molecular and Integrative Physiology, Univ. of Illinois at Urbana-Champaign, 524 Burrill Hall, 407 S. Goodwin Ave., Urbana, IL 61801. Tel.: 217-244-5679; Fax: 217-333-1133; E-mail: anardull@life.uiuc.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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