Nucleic Acids Research, Vol 25, Issue 10 1903-1912, Copyright © 1997 by Oxford University Press
CM Klinge, DL Bodenner, D Desai, RM Niles and AM Traish
The mechanism by which retinoids, thyroid hormone (T3) and estrogens
modulate the growth of breast cancer cells is unclear. Since nuclear type
II nuclear receptors, including retinoic acid receptor (RAR), retinoid X
receptor (RXR) and thyroid hormone receptor (TR), bind direct repeats (DR)
of the estrogen response elements (ERE) half-site (5'-AGGTCA-3'), we
examined the ability of estrogen receptor (ER) versus type II nuclear
receptors, i.e. RARalpha, beta and gamma, RXRbeta, TRalpha and TRbeta, to
bind various EREs in vitro . ER bound a consensus ERE, containing a
perfectly palindromic 17 bp inverted repeat (IR), as a homodimer. In
contrast, ER did not bind to a single ERE half- site. Likewise, ER did not
bind two tandem (38 bp apart) half-sites, but low ER binding was detected
to three tandem copies of the same half- site. RARalpha,beta or gamma bound
both ERE and half-site constructs as a homodimer. RXRbeta did not bind full
or half-site EREs, nor did RXRbeta enhance RARalpha binding to a full ERE.
However, RARalpha and RXRbeta bound a half-site ERE cooperatively forming a
dimeric complex. The RARalpha-RXRbeta heterodimer bound the Xenopus
vitellogenin B1 estrogen responsive unit, with two non-consensus EREs, with
higher affinity than one or two copies of the full or half-site ERE. Both
TRalpha and TRbeta bound the full and the half-site ERE as monomers and
homodimers and cooperatively as heterodimers with RXRbeta. We suggest that
the cellular concentrations of nuclear receptors and their ligands, and the
nature of the ERE or half-site sequence and those of its flanking sequences
determine the occupation of EREs in estrogen- regulated genes in vivo .
ARTICLES
Binding of type II nuclear receptors and estrogen receptor to full and half-site estrogen response elements in vitro
Department of Biochemistry, the University of Louisville School of Medicine, Louisville, KY 40292, USA. cmklin01@ulkyvym.louisville.edu
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