The plasticity of estrogen receptor-DNA complexes: Binding affinity and specificity of estrogen receptors to estrogen response element half-sites separated by variant spacers

Journal of Steroid Biochemistry and Molecular Biology

Volumn 110, Issue 1-2, 2008, Pages 186-195

  El Marzouk, S ^a   Gahattamaneni, R ^a   Joshi, S R ^a   Scovell, W M ^a  

^a BOWLING GREEN STATE UNIVERSITY   (United States)

Author keywords

Estrogen receptors; Estrogen response element half sites; F domain; HMGB1

Indexed keywords

ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; HIGH MOBILITY GROUP B1 PROTEIN;

ANTIGEN BINDING; ARTICLE; BINDING AFFINITY; BINDING SITE; PLASTICITY; RECEPTOR BINDING; SEQUENCE ANALYSIS;

ANIMALS; BINDING SITES; BINDING, COMPETITIVE; DNA; ELECTROPHORETIC MOBILITY SHIFT ASSAY; HMGB1 PROTEIN; HUMANS; OLIGONUCLEOTIDES; PEPTIDE HYDROLASES; PROTEIN BINDING; RECEPTORS, ESTROGEN; RESPONSE ELEMENTS;

EID: 44649144538     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsbmb.2008.03.034     Document Type: Article

References (53)

1. Klinge C.M. Estrogen receptor interactions with estrogen response elements. Nucleic Acids Res. 16 (2001) 647-663
2. Bourdeau V., Deschenes J., Metivier R., Nagai Y., Nguyen D., Bretschneider N., Gannon F., White J.H., and Mader S. Genome-wide identification of high affinity estrogen response elements in human and mouse. Mol. Endocrinol. 18 (2004) 1411-1427
3. O'Lone R., Frith M.C., Karlsson E.K., and Hansen U. Genomic targets of nuclear estrogen receptors. Mol. Endocrinol. 18 (2004) 1859-2175
4. Sanchez R., Nyguyen D., Rocha W., White J.H., and Mader S. Diversity in the mechanisms of gene regulation by estrogen receptors. BioEssays 24 (2002) 244-254
5. Geserick C., Meyer A.-H., and Haendler B. The role of DNA response elements as allosteric modulators of steroid receptor function. Mol. Cell. Endocrinol. 236 (2005) 1-7
6. Das D., Peterson R.C., and Scovell W.M. High mobility group B proteins facilitate strong estrogen receptor binding to classical and half-site estrogen response elements and relax binding selectivity. Mol. Endocrinol. 18 (2004) 2616-2632
7. + exchanger regulatory factor/ezrin-radixin-moesin binding protein 50(NHE-RF/EBP50) gene involving multiple half-estrogen response elements. Mol. Endocrinol. 16 (2002) 1828-1839
8. Bustin M., and Reeves R. High-mobility-group chromosomal proteins: architectural components that facilitate chromatin function. Prog. Nucleic Acid Res. Mol. Biol. 54 (1996) 35-100
9. Romine L.E., Wood J.R., Lamia L.A., Prendergast P., Edwards D.P., and Nardulli A.M. The high mobility group protein 1 enhances binding of the estrogen receptor DNA-binding domain to the estrogen response element. Mol. Endocrinol. 12 (1998) 664-674
10. Melvin V.S., and Edwards D.P. Coregulatory proteins in steroid hormone receptor action: the role of chromatin high mobility group proteins HMG-1 and -2. Steroids 64 (1999) 576-586
11. Melvin V.S., Harrell C., Adelman J.S., Kraus W.L., Churchill M., and Edwards D.P. The role of the C-terminal extension (CTE) of the estrogen receptor and DNA binding domain in DNA binding and interaction with HMGB. J. Biol. Chem. 279 (2004) 14763-14771
12. Anderson I., and Gorski J. Estrogen receptor interaction with response element half-sites from the rat prolactin gene. Biochemistry 39 (2000) 3842-3847
13. Richard S., and Zingg H.H. The human oxytocin gene promoter is regulated by estrogens. J. Biol. Chem. 265 (1990) 6098-6103
14. Tora L., Gaub M.P., Mader S., Dierich A., Bellard M., and Chambon P. Cell-specific activity of a GGTCA half-palindromic oestrogen-responsive element in the chicken ovalbumin gene promoter. EMBO J. 7 (1988) 3771-3778
15. Borrmann L., Kim I., Schultheiss D., Ragalla P., and Bullerdiek J. Regulation of the expression of HMGB1, a coactivator of the estrogen receptor. Anticancer Res. 21 (2001) 301-306
16. Dana S.L., Hoener P.A., Wheeler D.A., Lawence C.B., and McDonnell D.P. Novel estrogen response elements identified by genetic selection in yeast are differentially responsive to estrogens and antiestrogens in mammalian cell. Mol. Endocrinol. 8 (1994) 1193-1207
17. Gearhart M.D., Hombeck S.M.A., Evans R.M., Dyson H.J., and Wright P.E. Monomeric complex of human orphan estrogen related receptor-2 with DNA: a pseudo-dimer interface mediates extended half-site recognition. J. Mol. Biol. 327 (2003) 819-832
18. Zhao Q., Khorasanizadeh S., Miyoshi S., Lazar M.A., and Rastinejad F. Structural elements of an orphan nuclear receptor-DNA complex. Mol. Cell 1 (1998) 849-861
19. Aumais J.P., Lee H.S., DeGannes C., Horsford J., and White J.H. Function of directly repeated half-sites as response elements for steroid hormone receptors. J. Biol. Chem. 271 (1996) 12568-12577
20. Schwabe J.W.R., Chapman L., Finch J.T., Rhodes D., and Neuhaus D. DNA recognition by the estrogen receptor: from solution to the crystal. Structure 1 (1993) 187-204
21. Schwabe J.W.R., Chapman L., Finch J.T., and Rhodes D. The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: how receptors discriminate between their response elements. Cell 7 (1993) 567-578
22. Schwabe J.W.R., Chapman L., and Rhodes D. The oestrogen receptor recognizes an inperfectly palindromic response element through an alternative side-chain conformation. Structure 3 (1995) 201-213
23. Luisi B.F., Xu W.X., Otwinowski Z., Freedman L.P., Yamamoto k.R., and Sigler P.B. Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA. Nature 352 (1991) 497-505
24. Gewirth D.T., and Sigler P.B. The basis for half-site specificity explored through a non-cognate steroid receptor-DNA complex. Nat. Struct. Biol. 2 (1995) 386-394
25. Shaffer P.L., Jivan A., Dollins D.E., Claessens F., and Gewirth D.T. Structural basis of androgen receptor binding to selective androgen response elements. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 4758-4763
26. Tyulmenkov V.V., and Klinge C.M. A mathematical approach to predict the affinity of estrogen receptors α and β Binding to DNA. Mol. Cell. Endocrinol. 182 (2001) 109-119
27. Schultz J.R., Lovent M.A., Melvin V.M.S., Edwards D.P., and Nardulli A.M. Differential modulation of DNA conformation by estrogen receptors α and β. J. Biol. Chem. 277 (2002) 8702-8707
28. Vanacker J.-M., Pettersson K., Gustafsson J.-A., and Laudet V. Transcriptional targets shared by estrogen receptor-related receptors (ERRs) and estrogen receptor, ERα, but not ER. EMBO J. 18 (1999) 4270-4279
29. Warnmark A., Almlof T.A., Leers J., Gustafsson J.-A., and Treuter E. Differential recruitment of the mammalian mediator subunit TRAP220 by estrogen receptor ERα and ERβ. J. Biol. Chem. 276 (2001) 23397-23404
30. Das D., and Scovell W.M. The binding interaction of HMG-1 with the TATA-binding protein/TATA complex. J. Biol. Chem. 276 (2001) 32597-32605
31. Truss M., and Beato M.M. Steroid hormone receptors: interaction with deoxyribonucleic acid and transcription factors. Endocrine Rev. 14 (1993) 459-479
32. Wood J.R., Greene G.L., and Nardulli A.M. Estrogen response elements function as allosteric modulators of estrogen receptor conformation. Mol. Cell. Biol. 18 (1998) 1927-1934
33. Loven M.A., Wood J.R., and Nardulli A.M. Interaction of estrogen receptors α and β with estrogen response elements. Mol. Cell. Endocrinol. 181 (2001) 151-163
34. Love J.J., Li X., Case D.A., Geise K., Grosshedl R., and Wright P.E. Structural basis for DNA binding by the architectural transcription factor LEF-1. Nature 276 (1995) 791-795
35. Murphy II F.V., Sweet R.M., and Churchill M.E.A. The structure of a chromosomal high mobility group protein-DNA complex reveals sequence-neutral mechanisms important for non-sequence-specific DNA recognition. EMBO J. 18 (1999) 6610-6618
36. Lundback T., and Hard T. Sequence-specific DNA-binding dominated by dehydration. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 4754-4759
37. Drew H.R., and Dickerson R.E. Structure of a B-DNA dodecamer: a quantitative study. J. Mol. Biol. 151 (1981) 535-556
38. Chiu T.K., Kaczor-Grzeskowiak M., and Dickerson R.E. Absence of minor groove monovalent cations in the crosslinked dodecamer C-G-C-G-A-A-T-T-C-G-C-G. J. Mol. Biol. 292 (1999) 589-608
39. Brzozowski A.M., Pike A.C.W., Dauter Z., Hubbard R.E., Bonn T., Engstrom O., Ohman L., Greene G.L., Gustafsson J.-A., and Carlquis M.T. Molecular basis of agonism and antagonism in the oestrogen receptor. Nature 389 (1997) 753-758
40. Peters G.A., and Khan S.A. Estrogen receptor domains E and F: role in dimerization and interaction with coactivator RIP-40. Mol. Endocrinol. 13 (1999) 286-296
41. Montana M.M., Muller V., Trobaugh A., and Katzenellenbogan B.S. The carboxyl-terminal F Domain of the human estrogen receptor: role in the transcriptional activity of the receptor and the effectiveness of antiestrogens as estrogen antagonists. Mol. Endocrinol. 9 (1995) 814-825
42. Nichols M., Rientjes J.M.J., and Steward A.F. Different positioning of the ligand-binding domain helix 12 and the F domain of the estrogen receptor accounts for functional differences between agonist and antagonists. EMBO J. 17 (1998) 765-773
43. Kumar V., and Chambon P. The estrogen receptor binds tightly to its responsive element as a ligand-induced homodimer. Cell 55 (1998) 145-156
44. Perlmann T., Umesono K., Rangarajan P.N., Forman B.M., and Evans R.M. Two distinct dimerization interfaces differentially modulate target gene specificity of nuclear hormone receptors. Mol. Endocrinol. 10 (1996) 959-966
45. Dahlman-Wright K., Sitala-Roos H., Carlstedt-Duke J., and Gustafsson J.A. Protein-protein interactions facilitate DNA binding by the glucocorticoid receptor DNA-binding domain. J. Biol. Chem. 265 (1990) 14030-14035
46. Ascenzi P., Bocedi A., and Marino M. Structure-function relationships of estrogen receptor α and β: impact on human health. Mol. Aspects Med. 27 (2006) 299-402
47. Glass C.K., Holloway J.M., Devary O.V., and Rosenfeld M.G. The thyroid hormone receptor binds with opposite transcriptional effects to a common motif in thyroid hormone and estrogen response elements. Cell 54 (1998) 313-323
48. Umesono K., Giguere V., Glass C.K., Rosenfeld M.G., and Evans R.M. Retinoic acid and thyroid hormone induce gene expression through a common responsive element. Nature 336 (1988) 262-265
49. Zhu Y.S., Yen P.M., Chin D.W., and Pfaff D.W. Estrogen and thyroid hormone interaction on regulation of gene expression. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 12587-12592
50. Vasudevan N., Zhu Y.-S., Daniel S., Koibuchi N., Chin W.W., and Pfaff D. Crosstalk between oestrogen receptors and thyroid hormone receptor isoforms results in differential regulation of the preproenkephalin gene. J. Neuroendocrinol. 1 (2001) 779-790
51. Vasudevan N., Koibuchi N., Chin W.W., and Pfaff D.W. Differential crosstalk between estrogen receptor ERα and ERβ and the thyroid hormone receptor isoforms results in flexible regulation of the consensus ERE. Mol. Brain Res. 95 (2001) 9-17
52. Carroll J.S., Liu X.S., Broadsky A.S., Li W., Meyer C.A., Szary A.J., Eeckhoute J., Shao W., Hestermann E.V., Geistlinger T.R., Fox E.A., Silver P.A., and Brown M. Chromosome-wide mapping of estrogen receptor binding reveals long-range regulation requiring the forkhead protein FoxA1. Cell 122 (2005) 33-44
53. Mayo A.E., Setty Y., Shavit S., Zaslaver A., and Alon U. Plasticity of the cis-regulatory input function of a gene. PLoS Biol. 4 (2006) 555-561