Estrogen Response Elements Function as Allosteric Modulators of Estrogen Receptor Conformation

REFERENCES

• Alber, T. 1993. How GCN4 binds DNA. Curr. Biol. 3: 182–184.
   PubMedGoogle Scholar
• Beekman, J. M., G. F. Allan, S. Y. Tsai, M.-J. Tsai, and B. O’Malley 1993. Transcriptional activation by the estrogen receptor requires a conformational change in the ligand binding domain. Mol. Endocrinol. 7: 1266–1274.
   PubMedGoogle Scholar
• Berry, M., D. Metzger, and P. Chambon 1990. Role of the two activating domains of the oestrogen receptor in the cell-type and promoter-context dependent agonistic activity of the anti-oestrogen 4-hydroxytamoxifen. EMBO J. 9: 2811–2818.
   PubMed Web of Science ®Google Scholar
• Blaustein, J. 1993. Estrogen receptor immunoreactivity in rat brain: rapid effects of estradiol injection. Endocrinology 132: 1218–1224.
   PubMedGoogle Scholar
• Bourguet, W., M. Ruff, P. Chambon, H. Gronemeyer, and D. Moras 1995. Crystal structural of the ligand-binding domain of the human nuclear receptor RXR-alpha. Nature 375: 377–382.
   PubMed Web of Science ®Google Scholar
• Chang, T.-C., A. M. Nardulli, D. Lew, and D. J. Shapiro 1992. The role of estrogen response elements in expression of the Xenopus laevis vitellogenin B1 gene. Mol. Endocrinol. 6: 346–354.
   PubMedGoogle Scholar
• Fawell, S., R. White, S. Hoare, M. Sydenham, M. Page, and M. Parker 1990. Inhibition of estrogen receptor-DNA binding by the “pure” antiestrogen ICI 164,384 appears to be mediated by impaired receptor dimerization. Proc. Natl. Acad. Sci. USA 17: 6883–6887.
   Google Scholar
• Fawell, S. E., J. A. Lees, R. White, and M. G. Parker 1990. Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor. Cell 60: 953–962.
   PubMed Web of Science ®Google Scholar
• Frankel, A. D., and P. S. Kim 1991. Modular structure of transcription factors: implications for gene regulation. Cell 65: 717–719.
   PubMed Web of Science ®Google Scholar
• Fujita, T., G. P. Nolan, S. Ghosh, and D. Baltimore 1992. Independent modes of transcriptional activation by the p50 and p65 subunits of NF-KB. Genes Dev. 6: 775–787.
   PubMed Web of Science ®Google Scholar
• Furlow, J. D., F. E. Murdoch, and J. Gorski 1993. High affinity binding of the estrogen receptor to a DNA response element does not require homodimer formation or estrogen. J. Biol. Chem. 268: 12519–12525.
   PubMedGoogle Scholar
• Green, S., and P. Chambon 1987. Oestradiol induction of a glucocorticoid-responsive gene by a chimaeric receptor. Nature 325: 75–78.
   PubMed Web of Science ®Google Scholar
• Greene, G., N. Sobel, W. King, and E. Jensen 1984. Immunochemical studies of estrogen receptors. J. Steroid Biochem. 20: 51–56.
   PubMedGoogle Scholar
• Hansen, J. C., and J. Gorski 1986. Conformational transitions of the estrogen receptor monomer. J. Biol. Chem. 261: 13990–13996.
   PubMedGoogle Scholar
• Hard, T., E. Kellenbach, R. Boelens, B. A. Naler, K. Dahlman, L. P. Freedman, J. Carlstedt-Duke, K. R. Yamamoto, J.-A. Gustafsson, and R. Kaptein 1990. Solution structure of the glucocorticoid receptor DNA-binding domain. Science 249: 157–160.
   PubMed Web of Science ®Google Scholar
• Klein-Hitpass, L., G. U. Ryffel, E. Heitlinger, and A. C. B. Cato 1988. A 13 bp palindrome is a functional estrogen responsive element and interacts specifically with estrogen receptor. Nucleic Acids Res. 16: 647–663.
   PubMed Web of Science ®Google Scholar
• Klein-Hitpass, L., S. Y. Tsai, G. L. Greene, J. H. Clark, M.-J. Tsai, and B. W. O’Malley 1989. Specific binding of estrogen receptor to the estrogen response element. Mol. Cell. Biol. 9: 43–49.
   PubMed Web of Science ®Google Scholar
• Kuiper, G. G. J. M., E. Enmark, M. Pelto-Huikko, S. Nilsson, and J.-A. Gustafsson 1996. Cloning of a novel estrogen receptor expressed in rat prostate and ovary. Proc. Natl. Acad. Sci. USA 93: 5925–5930.
   PubMed Web of Science ®Google Scholar
• Lefstin, J. A., J. R. Thomas, and K. R. Yamamoto 1994. Influence of a steroid receptor DNA-binding domain on transcriptional regulatory functions. Genes Dev. 8: 2842–2856.
   PubMed Web of Science ®Google Scholar
• Littlewood, T. D., D. C. Hancock, P. S. Danielian, M. G. Parker, and G. I. Evan 1995. A modified oestrogen receptor ligand binding domain as an improved switch for the regulation of heterologous proteins. Nucleic Acids Res. 23: 1686–1690.
   PubMed Web of Science ®Google Scholar
• Luisi, B. F., W. X. Xu, Z. Otwinowski, L. P. Freedman, K. R. Yamamoto, and P. B. Sigler 1991. Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature 352: 497–505.
   PubMed Web of Science ®Google Scholar
• Martinez, E., and W. Wahli 1989. Cooperative binding of estrogen receptor to imperfect estrogen-responsive DNA elements correlates with their synergistic hormone-dependent enhancer activity. EMBO J. 8: 3781–3791.
   PubMed Web of Science ®Google Scholar
• Metzger, D., S. Ali, J.-M. Bornert, and P. Chambon 1995. Characterization of the amino-terminal transcriptional activation function of the human estrogen receptor in animal and yeast cells. J. Biol. Chem. 270: 9535–9542.
   PubMedGoogle Scholar
• Montano, M. M., K. Ekena, K. D. Krueger, A. L. Keller, and B. S. Katzenellenbogen 1996. Human estrogen receptor ligand activity inversion mutants: receptors that interpret antiestrogens as estrogens and estrogens as antiestrogens and discriminate among different antiestrogens. Mol. Endocrinol. 10: 230–242.
   PubMedGoogle Scholar
• Nardulli, A. M., G. L. Greene, and D. J. Shapiro 1993. Human estrogen receptor bound to an estrogen response element bends DNA. Mol. Endocrinol. 7: 331–340.
   PubMedGoogle Scholar
• Nardulli, A. M., C. Grobner, and D. Cotter 1995. Estrogen receptor-induced DNA bending: orientation of the bend and replacement of an estrogen response element with an intrinsic DNA bending sequence. Mol. Endocrinol. 9: 1064–1076.
   PubMedGoogle Scholar
• Nardulli, A. M., D. Lew, L. Erijman, and D. J. Shapiro 1991. Purified estrogen receptor DNA binding domain expressed in Escherichia coli activates transcription of an estrogen-responsive promoter in cultured cells. J. Biol. Chem. 266: 24070–24076.
   PubMedGoogle Scholar
• Nardulli, A. M., L. E. Romine, C. Carpo, G. L. Greene, and B. Rainish 1996. Estrogen receptor affinity and location of consensus and imperfect estrogen response elements influence transcription activation of simplified promoters. Mol. Endocrinol. 10: 694–704.
   PubMedGoogle Scholar
• Nardulli, A. M., and D. J. Shapiro 1992. Binding of the estrogen receptor DNA-binding domain to the estrogen response element induces DNA bending. Mol. Cell. Biol. 12: 2037–2042.
   PubMedGoogle Scholar
• Nunez, A.-M., M. Berry, J.-L. Imler, and P. Chambon 1989. The 5′ flanking region of the pS2 gene contains a complex enhancer region responsive to oestrogens, epidermal growth factor, a tumour promoter (TPA), the c-Ha-ras oncoprotein and the c-jun protein. EMBO J. 8: 823–829.
   PubMed Web of Science ®Google Scholar
• Pabo, C. O., and R. T. Sauer 1992. Transcription factors: structural families and principles of DNA recognition. Annu. Rev. Biochem. 61: 1053–1095.
   PubMed Web of Science ®Google Scholar
• Ponglikitmongkol, M., S. Green, and P. Chambon 1988. Genomic organization of the human oestrogen receptor gene. EMBO J. 7: 3385–3388.
   PubMed Web of Science ®Google Scholar
• Potthoff, S. J., L. E. Romine, and A. M. Nardulli 1996. Effects of wild type and mutant estrogen receptors on DNA flexibility, DNA bending, and transcription activation. Mol. Endocrinol. 10: 1095–1106.
   PubMedGoogle Scholar
• Renaud, J.-P., N. Rochel, M. Ruff, V. Vivat, P. Chambon, H. Gronemeyer, and D. Moras 1995. Crystal structure of the RAR- gamma ligand-binding domain bound to all-trans retinoic acid. Nature 378: 681–689.
   PubMed Web of Science ®Google Scholar
• Schreiber, E., P. Matthias, M. Müller, and W. Schaffner 1988. Identification of a novel lymphoid specific octamer binding protein (OTF-2B) by proteolytic clipping bandshift assay (PCBA). EMBO J. 7: 4221–4229.
   PubMed Web of Science ®Google Scholar
• Schwabe, J. W. R., L. Chapman, J. T. Finch, and D. Rhodes 1993. The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements. Cell 75: 567–578.
   PubMed Web of Science ®Google Scholar
• Schwabe, J. W. R., L. Chapman, J. T. Finch, D. Rhodes, and D. Neuhaus 1993. DNA recognition by the oestrogen receptor: From solution to the crystal. Structure 1: 187–204.
   PubMedGoogle Scholar
• Schwabe, J. W. R., L. Chapman, and D. Rhodes 1995. The oestrogen receptor recognizes an imperfectly palindromic response element through an alternative side-chain conformation. Structure 3: 201–213.
   PubMedGoogle Scholar
• Spolar, R. S., and M. T. Record 1994. Coupling of local folding to site-specific binding of proteins to DNA. Science 263: 777–784.
   PubMed Web of Science ®Google Scholar
• Staal, A., A. J. van Wijnen, J. C. Birkenhäger, H. A. P. Pols, J. Prahl, H. DeLuca, M.-P. Gaub, J. B. Lian, G. S. Stein, J. P. T. M. van Leeuwen, and J. L. Stein 1996. Distinct conformations of vitamin D receptor/retinoid X receptor-α heterodimers are specified by dinucleotide differences in the vitamin D-responsive elements of the osteocalcin and osteopontin genes. Mol. Endocrinol. 10: 1444–1456.
   PubMedGoogle Scholar
• Starr, D. B., W. Matsui, J. R. Thomas, and K. R. Yamamoto 1996. Intracellular receptors use a common mechanism to interpret signaling information at response elements. Genes Dev. 10: 1271–1283.
   PubMed Web of Science ®Google Scholar
• Steitz, T. A. 1990. Structural studies of protein-nucleic acid interaction: the sources of sequence-specific binding. Q. Rev. Biophys. 23: 205–280.
   PubMed Web of Science ®Google Scholar
• Talanian, R. V., C. J. McKnight, and P. S. Kim 1990. Sequence-specific DNA binding by a short peptide dimer. Science 249: 769–771.
   PubMed Web of Science ®Google Scholar
• Tan, S., and T. J. Richmond 1990. DNA binding-induced conformational change of the yeast transcriptional activator PRTF. Cell 62: 367–377.
   PubMedGoogle Scholar
• Tasset, D., L. Tora, C. Fromental, E. Scheer, and P. Chambon 1990. Distinct classes of transcriptional activating domains function by different mechanisms. Cell 62: 1177–1187.
   PubMed Web of Science ®Google Scholar
• Tora, L., J. White, C. Brou, D. Tasset, N. Webster, E. Scheer, and P. Chambon 1989. The human estrogen receptor has two independent nonacidic transcriptional activation functions. Cell 59: 477–487.
   PubMed Web of Science ®Google Scholar
• Tzukerman, M. T., A. Esty, D. Santiso-Mere, P. Danielian, M. G. Parker, R. B. Stein, J. W. Pike, and D. P. McDonnell 1994. Human estrogen receptor transactivational capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions. Mol. Endocrinol. 8: 21–30.
   PubMed Web of Science ®Google Scholar
• von Hippel, P. H. 1994. Protein-DNA recognition: new perspectives and underlying themes. Science 263: 769–770.
   PubMed Web of Science ®Google Scholar
• Wagner, R., J. Apriletti, M. McGrath, B. West, J. Baxter, and R. Fletterick 1995. A structural role for hormone in the thyroid hormone receptor. Nature 378: 690–697.
   PubMed Web of Science ®Google Scholar
• Walker, P., J.-E. Germond, M. Brown-Luedi, F. Givel, and W. Wahli 1984. Sequence homologies in the region preceding the transcription initiation site of the liver estrogen-responsive vitellogenin and apo-VLDLII genes. Nucleic Acids Res. 12: 8611–8626.
   PubMed Web of Science ®Google Scholar
• Webster, N. J. G., S. Green, J. R. Jin, and P. Chambon 1988. The hormone-binding domains of the estrogen and glucocorticoid receptors contain an inducible transcription activation function. Cell 54: 199–207.
   PubMed Web of Science ®Google Scholar