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Effect of Ligand and DNA Binding on the Interaction between Human Transcription Intermediary Factor 1 and Estrogen Receptors

INSERM U148 Hormones and Cancer and University of Montpellier (S.T., S.B., A.B., V.C.) 34090 Montpellier, France
INSERM U414-Centre de Biochimie Structurale (E.M., C.A.R.) 34060 Montpellier, France
INSERM U439 (J.-L.B.) 34090 Montpellier, France

Hormonal regulation of gene activity is mediated by nuclear receptors acting as ligand-activated transcription factors. To achieve efficient regulation of gene expression, these receptors must interact with different type of molecules: 1) the steroid hormone, 2) the DNA response element, and 3) various proteins acting as transcriptional cofactors. In the present study, we have investigated how ligand and DNA binding influence the in vitro interaction between estrogen receptors (ERs) and the transcription intermediary factor hTIF1 (human transcriptional intermediary factor 1). We first optimized conditions for the coactivator-dependent receptor ligand assay to lower ED₅₀, and we then analyzed the ability of various natural and synthetic estrogens to allow the binding of the two types of proteins. Results were compared with the respective affinities of these ligands for the receptor. We then developed a protein-protein-DNA assay allowing the quantification of cofactor-ER-estrogen response element (ERE) complex formation in the presence of ligand and used measurements of fluorescence anisotropy to define the equilibrium binding parameters of the interaction. We demonstrated that the leucine-charged domain of hTIF1 is sufficient to interact with ERE-bound ER in a ligand-dependent manner and showed that binding of ER onto DNA does not significantly affect its hormone-dependent association with TIF1. Finally, we show that, mainly in the absence of hormone, hTIF1 interacts better with ERß than with ER independently of the presence of ERE.

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