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J. Biol. Chem., Vol. 275, Issue 21, 15645-15651, May 26, 2000
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From the Estrogen receptor (ER)
p300 Mediates Functional Synergism between AF-1 and AF-2 of
Estrogen Receptor
and 
by Interacting Directly with the
N-terminal A/B Domains*
,,,,,¶, and¶
Institute of Molecular and Cellular
Biosciences, The University of Tokyo,
Bunkyo-ku, Tokyo 113-0032, Japan, § Institut de Genetique
et de Biologiè Moleculaire et Cellulaire/CNRS/INSERM/ULP College
de France, BP 163, 67404 Illkirch Cedex, C.U. de Strasbourg, France,
and ¶ CREST, Japan Science and Technology, Kawaguchi,
Saitama 332-0012, Japan
and 
mediate
estrogen actions in target cells through transcriptional control of
target gene expression. For 17-estradiol-induced transactivation,
the N-terminal A/B domain (AF-1) and the C-terminal E/F domain (AF-2)
of ERs are required. Ligand binding is considered to induce functional
synergism between AF-1 and AF-2, but the molecular mechanism remains
unknown. To clarify this synergism, we studied the role of reported
AF-2 coactivators, p300/CREB binding protein, steroid receptor
coactivator-1/transcriptional intermediary factor-2 (SRC-1/TIF2) family
proteins and thyroid hormone receptor-associated protein-220/(vitamin
D3 receptor-interacting protein- 205-(TRAP220/DRIP205) on the AF-1
activity in terms of synergism with the AF-2 function. We found that
neither any of the SRC-1/TIF2 family coactivators nor TRAP220/DRIP205
is potent, whereas p300 potentiates the AF-1 function of both human
ER and human ER. Direct interactions of p300 with the A/B domains
of ER and ER were observed in an in vitro glutathione
S-transferase pull-down assay in accordance with the
interactions in yeast and mammalian two-hybrid assays. Furthermore,
mutations in the p300 binding sites (56-72 amino acids in ER and
62-72 amino acids in ER) in the A/B domains caused a reduction in
ligand-induced transactivation functions of both ER and ER. Thus,
these findings indicate that ligand-induced functional synergism
between AF-1 and AF-2 is mediated through p300 by its direct binding to
the A/B regions of ER and ER.
*
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.
To whom correspondence should be addressed: Inst. of Molecular
and Cellular Biosciences, The University of Tokyo, Yayoi 1-1-1, Bunkyo-ku, Tokyo 113-0032, Japan. Tel.: 81-3-5841-8478; Fax:
81-3-5841-8477; E-mail: uskato@mail.ecc.u-tokyo.ac.jp.
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