The objective of this study is to determine if DNA bending induced by binding of the human ER plays a role in transcription activation of E- responsive genes.
Aim l is to determine if the effectiveness of ER in DNA bending is influenced by E, salt activation, or phosphorylation.
Aim 2 is to determine if unoccupied ER, ER occupied by E, and ER occupied by antiE bend DNA in the same direction.
Aim 3 is to determine if the extent of DNA bending induced by the ER correlates with the magnitude of gene transcription activation by the ER.

Agency
National Institute of Health (NIH)
Institute
Eunice Kennedy Shriver National Institute of Child Health & Human Development (NICHD)
Type
First Independent Research Support & Transition (FIRST) Awards (R29)
Project #
5R29HD031299-02
Application #
2203738
Study Section
Biochemical Endocrinology Study Section (BCE)
Project Start
1994-01-01
Project End
1998-12-31
Budget Start
1995-01-01
Budget End
1995-12-31
Support Year
2
Fiscal Year
1995
Total Cost
Indirect Cost
Name
University of Illinois Urbana-Champaign
Department
Physiology
Type
Schools of Arts and Sciences
DUNS #
041544081
City
Champaign
State
IL
Country
United States
Zip Code
61820
Kim, J; Petz, L N; Ziegler, Y S et al. (2000) Regulation of the estrogen-responsive pS2 gene in MCF-7 human breast cancer cells. J Steroid Biochem Mol Biol 74:157-68
Petz, L N; Nardulli, A M (2000) Sp1 binding sites and an estrogen response element half-site are involved in regulation of the human progesterone receptor A promoter. Mol Endocrinol 14:972-85
Romine, L E; Wood, J R; Lamia, L A et al. (1998) The high mobility group protein 1 enhances binding of the estrogen receptor DNA binding domain to the estrogen response element. Mol Endocrinol 12:664-74
Wood, J R; Greene, G L; Nardulli, A M (1998) Estrogen response elements function as allosteric modulators of estrogen receptor conformation. Mol Cell Biol 18:1927-34
Petz, L N; Nardulli, A M; Kim, J et al. (1997) DNA bending is induced by binding of the glucocorticoid receptor DNA binding domain and progesterone receptors to their response element. J Steroid Biochem Mol Biol 60:31-41
Lazennec, G; Ediger, T R; Petz, L N et al. (1997) Mechanistic aspects of estrogen receptor activation probed with constitutively active estrogen receptors: correlations with DNA and coregulator interactions and receptor conformational changes. Mol Endocrinol 11:1375-86
Ozers, M S; Hill, J J; Ervin, K et al. (1997) Equilibrium binding of estrogen receptor with DNA using fluorescence anisotropy. J Biol Chem 272:30405-11
Kim, J; de Haan, G; Nardulli, A M et al. (1997) Prebending the estrogen response element destabilizes binding of the estrogen receptor DNA binding domain. Mol Cell Biol 17:3173-80
Potthoff, S J; Romine, L E; Nardulli, A M (1996) Effects of wild type and mutant estrogen receptors on DNA flexibility, DNA bending, and transcription activation. Mol Endocrinol 10:1095-106
Nardulli, A M; Romine, L E; Carpo, C et al. (1996) Estrogen receptor affinity and location of consensus and imperfect estrogen response elements influence transcription activation of simplified promoters. Mol Endocrinol 10:694-704

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