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1 Functionally Binds as a Monomer to Extended Half-Site Sequences Including Ones Contained within Estrogen-Response Elements
McArdle Laboratory for Cancer Research University of Wisconsin Medical School Madison, Wisconsin 53706-1599
The human estrogen-related receptor 
1
(hERR1) is an orphan member of the steroid/thyroid hormone receptor
superfamily. A cDNA encoding this protein was originally isolated on
the basis of sequence similarity in its DNA-binding domain with
estrogen receptor (ER). Previously, we reported the purification
of hERR1 from HeLa cell nuclear extracts on the basis of its ability
to bind two sites in the late promoter of simian virus 40 (SV40). We
have now determined the primary structure and the DNA and protein
binding specificities of hERR1 and developed in vivo and
in vitro assays for its functional activities. hERR1 was
found to bind as a monomer, with a high-affinity binding site
containing the extended half-site sequence 5'-TCAAGGTCA-3'. Binding
sites for hERR1 were identified in many cellular promoters,
including some that were previously shown to function as
estrogen-response elements (EREs). hERR1 was shown to function as a
sequence-specific repressor of the SV40 late promoter in both cell
culture and cell-free transcription sytems. It was also shown to
interact with both ER and the transcription factor TFIIB by direct
protein-protein contacts. Thus, hERR1 may play a role in the
response of some genes to estrogen via heterodimerization with ERs or
competition with ERs for binding to EREs.
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S.-K. Lee, H.-S. Choi, M.-R. Song, M.-O. Lee, and J. W. Lee Estrogen Receptor, a Common Interaction Partner for a Subset of Nuclear Receptors Mol. Endocrinol., August 1, 1998; 12(8): 1184 - 1192. [Abstract] [Full Text]
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C. M. Klinge, B. F. Silver, M. D. Driscoll, G. Sathya, R. A. Bambara, and R. Hilf Chicken Ovalbumin Upstream Promoter-Transcription Factor Interacts with Estrogen Receptor, Binds to Estrogen Response Elements and Half-Sites, and Inhibits Estrogen-induced Gene Expression J. Biol. Chem., December 12, 1997; 272(50): 31465 - 31474. [Abstract] [Full Text] [PDF]
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