Binding of the ERα nuclear receptor to DNA is coupled to proton uptake

Biochemistry

Volumn 49, Issue 29, 2010, Pages 5978-5988

  Deegan, Brian J ^a   Seldeen, Kenneth L ^a   McDonald, Caleb B ^a   Bhat, Vikas ^a   Farooq, Amjad ^a  

^a UNIVERSITY OF MIAMI MILLER SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE SUBSTITUTION; AS-LIGANDS; CELLULAR FUNCTION; CRITICAL STEPS; DNA RESPONSE ELEMENT; INTRACELLULAR PH; ISOTHERMAL TITRATION CALORIMETRY; MECHANISM OF ACTION; NUCLEAR RECEPTORS; ORDER OF MAGNITUDE; PROTEIN-DNA INTERACTIONS; PROTEIN-DNA INTERFACE; PROTON UPTAKE;

DNA SEQUENCES; ENZYME ACTIVITY; GENES; LAWS AND LEGISLATION; PROTONS; TRANSCRIPTION FACTORS;

DNA;

ALANINE; ESTROGEN RECEPTOR ALPHA; DNA; PROTON;

AMINO ACID SUBSTITUTION; ARTICLE; CELL PH; CONTROLLED STUDY; DNA RESPONSIVE ELEMENT; ISOTHERMAL TITRATION CALORIMETRY; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTON TRANSPORT; RECEPTOR BINDING; REGULATORY MECHANISM; AMINO ACID SEQUENCE; CALORIMETRY; CELL NUCLEUS; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PH; PROTEIN TERTIARY STRUCTURE; STATIC ELECTRICITY; THERMODYNAMICS;

AMINO ACID SEQUENCE; CALORIMETRY; CELL NUCLEUS; CONSERVED SEQUENCE; DNA; ESTROGEN RECEPTOR ALPHA; HUMANS; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, TERTIARY; PROTONS; RESPONSE ELEMENTS; STATIC ELECTRICITY; THERMODYNAMICS;

EID: 77954830192     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1004359     Document Type: Article

References (52)

1. Evans, R. M. (1988) The steroid and thyroid hormone receptor superfamily Science 240, 889-895
2. Escriva, H., Bertrand, S., and Laudet, V. (2004) The evolution of the nuclear receptor superfamily Essays Biochem. 40, 11-26
3. Thornton, J. W. (2001) Evolution of vertebrate steroid receptors from an ancestral estrogen receptor by ligand exploitation and serial genome expansions Proc. Natl. Acad. Sci. U.S.A. 98, 5671-5676
4. McKenna, N. J., Cooney, A. J., DeMayo, F. J., Downes, M., Glass, C. K., Lanz, R. B., Lazar, M. A., Mangelsdorf, D. J., Moore, D. D., Qin, J., Steffen, D. L., Tsai, M. J., Tsai, S. Y., Yu, R., Margolis, R. N., Evans, R. M., and OMalley, B. W. (2009) Minireview: Evolution of NURSA, the Nuclear Receptor Signaling Atlas Mol. Endocrinol. 23, 740-746
5. McEwan, I. J. (2009) Nuclear receptors: One big family Methods Mol. Biol. 505, 3-18
6. Barnett, P., Tabak, H. F., and Hettema, E. H. (2000) Nuclear receptors arose from pre-existing protein modules during evolution Trends Biochem. Sci. 25, 227-228
7. Kumar, R. and Thompson, E. B. (1999) The structure of the nuclear hormone receptors Steroids 64, 310-319
8. Egea, P. F., Klaholz, B. P., and Moras, D. (2000) Ligand-protein interactions in nuclear receptors of hormones FEBS Lett. 476, 62-67
9. Claessens, F. and Gewirth, D. T. (2004) DNA recognition by nuclear receptors Essays Biochem. 40, 59-72
10. Green, S. and Chambon, P. (1988) Nuclear receptors enhance our understanding of transcription regulation Trends Genet. 4, 309-314
11. Darimont, B. D., Wagner, R. L., Apriletti, J. W., Stallcup, M. R., Kushner, P. J., Baxter, J. D., Fletterick, R. J., and Yamamoto, K. R. (1998) Structure and specificity of nuclear receptor-coactivator interactions Genes Dev. 12, 3343-3356
12. Ham, J. and Parker, M. G. (1989) Regulation of gene expression by nuclear hormone receptors Curr. Opin. Cell Biol. 1, 503-511
13. Kato, S., Endoh, H., Masuhiro, Y., Kitamoto, T., Uchiyama, S., Sasaki, H., Masushige, S., Gotoh, Y., Nishida, E., Kawashima, H., Metzger, D., and Chambon, P. (1995) Activation of the estrogen receptor through phosphorylation by mitogen-activated protein kinase Science 270, 1491-1494
14. Warnmark, A., Treuter, E., Wright, A. P., and Gustafsson, J. A. (2003) Activation functions 1 and 2 of nuclear receptors: Molecular strategies for transcriptional activation Mol. Endocrinol. 17, 1901-1909
15. Noy, N. (2007) Ligand specificity of nuclear hormone receptors: Sifting through promiscuity Biochemistry 46, 13461-13467
16. Gottlieb, B., Beitel, L. K., Wu, J., Elhaji, Y. A., and Trifiro, M. (2004) Nuclear receptors and disease: Androgen receptor Essays Biochem. 40, 121-136
17. Gurnell, M. and Chatterjee, V. K. (2004) Nuclear receptors in disease: Thyroid receptor β, peroxisome-proliferator-activated receptor γ and orphan receptors Essays Biochem. 40, 169-189
18. Brzozowski, A. M., Pike, A. C., Dauter, Z., Hubbard, R. E., Bonn, T., Engstrom, O., Ohman, L., Greene, G. L., Gustafsson, J. A., and Carlquist, M. (1997) Molecular basis of agonism and antagonism in the oestrogen receptor Nature 389, 753-758
19. Sonoda, J., Pei, L., and Evans, R. M. (2008) Nuclear receptors: Decoding metabolic disease FEBS Lett. 582, 2-9
20. Jensen, E. V. and Jacobson, H. (1962) Basic guides to the mechanism of estrogen action Recent Prog. Horm. Res. 18, 318-414
21. Jensen, E. V. (1962) On the mechanism of estrogen action Perspect. Biol. Med. 6, 47-59
22. Toft, D. and Gorski, J. (1966) A receptor molecule for estrogens: Isolation from the rat uterus and preliminary characterization Proc. Natl. Acad. Sci. U.S.A. 55, 1574-1581
23. Toft, D., Shyamala, G., and Gorski, J. (1967) A receptor molecule for estrogens: Studies using a cell-free system Proc. Natl. Acad. Sci. U.S.A. 57, 1740-1743
24. Jensen, E. V. and Jordan, V. C. (2003) The estrogen receptor: A model for molecular medicine Clin. Cancer Res. 9, 1980-1989
25. Heldring, N., Pike, A., Andersson, S., Matthews, J., Cheng, G., Hartman, J., Tujague, M., Strom, A., Treuter, E., Warner, M., and Gustafsson, J. A. (2007) Estrogen receptors: How do they signal and what are their targets Physiol. Rev. 87, 905-931
26. Kumar, V., Green, S., Stack, G., Berry, M., Jin, J. R., and Chambon, P. (1987) Functional domains of the human estrogen receptor Cell 51, 941-951
27. Klinge, C. M. (2001) Estrogen receptor interaction with estrogen response elements Nucleic Acids Res. 29, 2905-2919
28. Schwabe, J. W., Chapman, L., Finch, J. T., and Rhodes, D. (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
29. Schwabe, J. W., Neuhaus, D., and Rhodes, D. (1990) Solution structure of the DNA-binding domain of the oestrogen receptor Nature 348, 458-461
30. Gasteiger, E., Hoogland, C., Gattiker, A., Duvaud, S., Wilkins, M. R., Appel, R. D., and Bairoch, A. (2005) in The Proteomics Protocols Handbook (Walker, J. M., Ed.) pp 571 - 607, Humana Press, Totowa, NJ.
31. Cantor, C. R., Warshaw, M. M., and Shapiro, H. (1970) Oligonucleotide interactions. 3. Circular dichroism studies of the conformation of deoxyoligonucleotides Biopolymers 9, 1059-1077
32. Wiseman, T., Williston, S., Brandts, J. F., and Lin, L. N. (1989) Rapid measurement of binding constants and heats of binding using a new titration calorimeter Anal. Biochem. 179, 131-137
33. Fukada, H. and Takahashi, K. (1998) Enthalpy and heat capacity changes for the proton dissociation of various buffer components in 0.1 M potassium chloride Proteins 33, 159-166
34. Kozlov, A. G. and Lohman, T. M. (2000) Large contributions of coupled protonation equilibria to the observed enthalpy and heat capacity changes for ssDNA binding to Escherichia coli SSB protein Proteins 4 (Suppl.) 8-22
35. Ortiz-Salmeron, E., Yassin, Z., Clemente-Jimenez, M. J., Las Heras-Vazquez, F. J., Rodriguez-Vico, F., Baron, C., and Garcia-Fuentes, L. (2001) Thermodynamic analysis of the binding of glutathione to glutathione S-transferase over a range of temperatures Eur. J. Biochem. 268, 4307-4314
36. Marti-Renom, M. A., Stuart, A. C., Fiser, A., Sanchez, R., Melo, F., and Sali, A. (2000) Comparative Protein Structure Modeling of Genes and Genomes Annu. Rev. Biophys. Biomol. Struct. 29, 291-325 (Pubitemid 30599596)
37. Carson, M. (1991) Ribbons 2.0 J. Appl. Crystallogr. 24, 958-961
38. Koradi, R., Billeter, M., and Wuthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures J. Mol. Graphics 14, 51-55
39. Lumry, R. and Rajender, S. (1970) Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: A ubiquitous property of water Biopolymers 9, 1125-1227
40. Eftink, M. R., Anusiem, A. C., and Biltonen, R. L. (1983) Enthalpy-entropy compensation and heat capacity changes for protein-ligand interactions: General thermodynamic models and data for the binding of nucleotides to ribonuclease A Biochemistry 22, 3884-3896
41. Cooper, A., Johnson, C. M., Lakey, J. H., and Nollmann, M. (2001) Heat does not come in different colours: Entropy-enthalpy compensation, free energy windows, quantum confinement, pressure perturbation calorimetry, solvation and the multiple causes of heat capacity effects in biomolecular interactions Biophys. Chem. 93, 215-230
42. Sharp, K. (2001) Entropy-enthalpy compensation: Fact or artifact? Protein Sci. 10, 661-667
43. Starikov, E. B. and Norden, B. (2007) Enthalpy-entropy compensation: A phantom or something useful? J. Phys. Chem. B 111, 14431-14435
44. Chen, Y. X., Du, J. T., Zhou, L. X., Liu, X. H., Zhao, Y. F., Nakanishi, H., and Li, Y. M. (2006) Alternative O-GlcNAcylation/O-phosphorylation of Ser16 induce different conformational disturbances to the N terminus of murine estrogen receptor β Chem. Biol. 13, 937-944
45. Faus, H. and Haendler, B. (2006) Post-translational modifications of steroid receptors Biomed. Pharmacother. 60, 520-528
46. Popov, V. M., Wang, C., Shirley, L. A., Rosenberg, A., Li, S., Nevalainen, M., Fu, M., and Pestell, R. G. (2007) The functional significance of nuclear receptor acetylation Steroids 72, 221-230
47. Weigel, N. L. and Moore, N. L. (2007) Steroid receptor phosphorylation: A key modulator of multiple receptor functions Mol. Endocrinol. 21, 2311-2319
48. Boron, W. F. (2004) Regulation of intracellular pH Adv. Physiol. Educ. 28, 160-179
49. Khaled, A. R., Moor, A. N., Li, A., Kim, K., Ferris, D. K., Muegge, K., Fisher, R. J., Fliegel, L., and Durum, S. K. (2001) Trophic factor withdrawal: p38 mitogen-activated protein kinase activates NHE1, which induces intracellular alkalinization Mol. Cell. Biol. 21, 7545-7557
50. 1-ATPase J. Biol. Chem. 276, 6453-6462
51. Puceat, M., Roche, S., and Vassort, G. (1998) Src family tyrosine kinase regulates intracellular pH in cardiomyocytes J. Cell Biol. 141, 1637-1646
52. Harris, T. K. and Turner, G. J. (2002) Structural basis of perturbed pKa values of catalytic groups in enzyme active sites IUBMB Life 53, 85-98