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Volumn 455, Issue A, 2009, Pages 41-70

Chapter 2 Using Thermodynamics to Understand Progesterone Receptor function. Method and Theory

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBONUCLEASE; DNA; DNA FRAGMENT; LIGAND; NUCLEAR RECEPTOR COACTIVATOR 2; PROGESTERONE RECEPTOR; TRANSCRIPTION FACTOR;

EID: 61849143816     PISSN: 00766879     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0076-6879(08)04202-X     Document Type: Review
Times cited : (4)

References (37)
  • 1
    • 0014730026 scopus 로고
    • Analytical gel chromatography of proteins
    • Academic Press, New York, NY
    • Ackers G.K. Analytical gel chromatography of proteins. Advances in protein chemistry Vol. 24 (1970), Academic Press, New York, NY 343-446
    • (1970) Advances in protein chemistry , vol.24 , pp. 343-446
    • Ackers, G.K.1
  • 2
    • 0001422329 scopus 로고
    • Quantitative model for gene regulation by lambda phage repressor
    • Ackers G.K., Johnson A.D., and Shea M.A. Quantitative model for gene regulation by lambda phage repressor. Proc. Natl. Acad. Sci. USA 79 (1982) 1129-1133
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 1129-1133
    • Ackers, G.K.1    Johnson, A.D.2    Shea, M.A.3
  • 3
    • 0026044065 scopus 로고
    • In two genes, synergism of steroid hormone action is not mediated by cooperative binding of receptors to adjacent sites
    • Bailly A., Rauch C., Cato A.C.B., and Milgrom E. In two genes, synergism of steroid hormone action is not mediated by cooperative binding of receptors to adjacent sites. Mol. Cell. Endocrin. 82 (1991) 313-323
    • (1991) Mol. Cell. Endocrin. , vol.82 , pp. 313-323
    • Bailly, A.1    Rauch, C.2    Cato, A.C.B.3    Milgrom, E.4
  • 4
    • 0034629344 scopus 로고    scopus 로고
    • The N-terminal region of the human progesterone A-receptor: Structural analysis and the influence of the DNA binding domain
    • Bain D.L., Franden M.A., McManaman J.L., Takimoto G.S., and Horwitz K.B. The N-terminal region of the human progesterone A-receptor: Structural analysis and the influence of the DNA binding domain. J. Biol. Chem. 275 (2000) 7313-7320
    • (2000) J. Biol. Chem. , vol.275 , pp. 7313-7320
    • Bain, D.L.1    Franden, M.A.2    McManaman, J.L.3    Takimoto, G.S.4    Horwitz, K.B.5
  • 5
    • 0035968162 scopus 로고    scopus 로고
    • The N-terminal region of human progesterone B-receptors: Biophysical and biochemical comparison to A-receptors
    • Bain D.L., Franden M.A., McManaman J.L., Takimoto G.S., and Horwitz K.B. The N-terminal region of human progesterone B-receptors: Biophysical and biochemical comparison to A-receptors. J. Biol. Chem. 276 (2001) 23825-23831
    • (2001) J. Biol. Chem. , vol.276 , pp. 23825-23831
    • Bain, D.L.1    Franden, M.A.2    McManaman, J.L.3    Takimoto, G.S.4    Horwitz, K.B.5
  • 7
    • 21344441515 scopus 로고    scopus 로고
    • Intra-domain communication between N-terminal and DNA-binding domains of the androgen receptor: Modulation of androgen response element DNA binding
    • Brodie J., and McEwan I.J. Intra-domain communication between N-terminal and DNA-binding domains of the androgen receptor: Modulation of androgen response element DNA binding. J. Mol. Endocrinol. 34 (2005) 603-615
    • (2005) J. Mol. Endocrinol. , vol.34 , pp. 603-615
    • Brodie, J.1    McEwan, I.J.2
  • 8
    • 0023938276 scopus 로고
    • Differential gene activation by glucocorticoids and progestins through the hormone regulatory element of mouse mammary tumor virus
    • Chalepakis G., Arnemann J., Slater E., Bruller H.-J., Gross B., and Beato M. Differential gene activation by glucocorticoids and progestins through the hormone regulatory element of mouse mammary tumor virus. Cell 53 (1988) 371-382
    • (1988) Cell , vol.53 , pp. 371-382
    • Chalepakis, G.1    Arnemann, J.2    Slater, E.3    Bruller, H.-J.4    Gross, B.5    Beato, M.6
  • 10
    • 33750715148 scopus 로고    scopus 로고
    • Hydrodynamic analysis of the human progesterone receptor A-isoform reveals that self-association occurs in the micromolar range
    • Connaghan-Jones K.D., Heneghan A.F., Miura M.T., and Bain D.L. Hydrodynamic analysis of the human progesterone receptor A-isoform reveals that self-association occurs in the micromolar range. Biochemistry 45 (2006) 12090-12099
    • (2006) Biochemistry , vol.45 , pp. 12090-12099
    • Connaghan-Jones, K.D.1    Heneghan, A.F.2    Miura, M.T.3    Bain, D.L.4
  • 11
    • 33847792712 scopus 로고    scopus 로고
    • Thermodynamic analysis of progesterone receptor-promoter interactions reveals a molecular model for isoform-specific function
    • Connaghan-Jones K.D., Heneghan A.F., Miura M.T., and Bain D.L. Thermodynamic analysis of progesterone receptor-promoter interactions reveals a molecular model for isoform-specific function. Proc. Natl. Acad. Sci. USA 104 (2007) 2187-2192
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 2187-2192
    • Connaghan-Jones, K.D.1    Heneghan, A.F.2    Miura, M.T.3    Bain, D.L.4
  • 12
    • 40849140749 scopus 로고    scopus 로고
    • Thermodynamic dissection of progesterone receptor interactions at the mouse mammary tumor virus promoter: Monomer binding and strong cooperativity dominate the assembly reaction
    • Connaghan-Jones K.D., Heneghan A.F., Miura M.T., and Bain D.L. Thermodynamic dissection of progesterone receptor interactions at the mouse mammary tumor virus promoter: Monomer binding and strong cooperativity dominate the assembly reaction. J. Mol. Biol. 377 (2008) 1144-1160
    • (2008) J. Mol. Biol. , vol.377 , pp. 1144-1160
    • Connaghan-Jones, K.D.1    Heneghan, A.F.2    Miura, M.T.3    Bain, D.L.4
  • 13
    • 43149123786 scopus 로고    scopus 로고
    • Quantitative DNase footprint titration: A tool for analyzing the energetics of protein-DNA interactions
    • Connaghan-Jones K.D., Moody A.D., and Bain D.L. Quantitative DNase footprint titration: A tool for analyzing the energetics of protein-DNA interactions. Nat. Protocols 3 (2008) 900-914
    • (2008) Nat. Protocols , vol.3 , pp. 900-914
    • Connaghan-Jones, K.D.1    Moody, A.D.2    Bain, D.L.3
  • 14
    • 21844477014 scopus 로고    scopus 로고
    • Self-association energetics of an intact, full-length nuclear receptor: The B-isoform of human progesterone receptor dimerizes in the micromolar range
    • Heneghan A.F., Berton N., Miura M.T., and Bain D.L. Self-association energetics of an intact, full-length nuclear receptor: The B-isoform of human progesterone receptor dimerizes in the micromolar range. Biochemistry 44 (2005) 9528-9537
    • (2005) Biochemistry , vol.44 , pp. 9528-9537
    • Heneghan, A.F.1    Berton, N.2    Miura, M.T.3    Bain, D.L.4
  • 15
    • 33644855967 scopus 로고    scopus 로고
    • Cooperative DNA binding by the B-isoform of human progesterone receptor: Thermodynamic analysis reveals strongly favorable and unfavorable contributions to assembly
    • Heneghan A.F., Connaghan-Jones K.D., Miura M.T., and Bain D.L. Cooperative DNA binding by the B-isoform of human progesterone receptor: Thermodynamic analysis reveals strongly favorable and unfavorable contributions to assembly. Biochemistry 45 (2006) 3285-3296
    • (2006) Biochemistry , vol.45 , pp. 3285-3296
    • Heneghan, A.F.1    Connaghan-Jones, K.D.2    Miura, M.T.3    Bain, D.L.4
  • 16
    • 34848844722 scopus 로고    scopus 로고
    • Coactivator assembly at the promoter: Efficient recruitment of SRC2 is coupled to cooperative DNA binding by the progesterone receptor
    • Heneghan A.F., Connaghan-Jones K.D., Miura M.T., and Bain D.L. Coactivator assembly at the promoter: Efficient recruitment of SRC2 is coupled to cooperative DNA binding by the progesterone receptor. Biochemistry 46 (2007) 11023-11032
    • (2007) Biochemistry , vol.46 , pp. 11023-11032
    • Heneghan, A.F.1    Connaghan-Jones, K.D.2    Miura, M.T.3    Bain, D.L.4
  • 18
    • 0023895160 scopus 로고
    • Characterization of R5020 and RU486 binding to progesterone receptor from calf uterus
    • Hurd C., and Moudgil V.K. Characterization of R5020 and RU486 binding to progesterone receptor from calf uterus. Biochemistry 27 (1988) 3618-3623
    • (1988) Biochemistry , vol.27 , pp. 3618-3623
    • Hurd, C.1    Moudgil, V.K.2
  • 19
    • 0026486367 scopus 로고
    • Why, when, and how biochemists should use least squares
    • Johnson M.L. Why, when, and how biochemists should use least squares. Anal. Biochem. 206 (1992) 215-225
    • (1992) Anal. Biochem. , vol.206 , pp. 215-225
    • Johnson, M.L.1
  • 20
    • 0037245786 scopus 로고    scopus 로고
    • Transactivation functions of the N-terminal domains of nuclear hormone receptors: Protein folding and coactivator interactions
    • Kumar R., and Thompson E.B. Transactivation functions of the N-terminal domains of nuclear hormone receptors: Protein folding and coactivator interactions. Mol. Endocrin. 17 (2003) 1-10
    • (2003) Mol. Endocrin. , vol.17 , pp. 1-10
    • Kumar, R.1    Thompson, E.B.2
  • 21
    • 0032580207 scopus 로고    scopus 로고
    • Allosteric effects of DNA on transcriptional regulators
    • Lefstin J.A., and Yamamoto K.R. Allosteric effects of DNA on transcriptional regulators. Nature 392 (1998) 885-888
    • (1998) Nature , vol.392 , pp. 885-888
    • Lefstin, J.A.1    Yamamoto, K.R.2
  • 22
    • 0035940497 scopus 로고    scopus 로고
    • Sequential recruitment of steroid receptor coactivator-1 (SRC-1) and p300 enhances progesterone receptor-dependent initiation and reinitiation of transcription from chromatin
    • Liu Z., Wong J., Tsai S.Y., Tsai M.-J., and O'Malley B.W. Sequential recruitment of steroid receptor coactivator-1 (SRC-1) and p300 enhances progesterone receptor-dependent initiation and reinitiation of transcription from chromatin. Proc. Natl. Acad. Sci. USA 98 (2001) 12426-12431
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12426-12431
    • Liu, Z.1    Wong, J.2    Tsai, S.Y.3    Tsai, M.-J.4    O'Malley, B.W.5
  • 23
    • 2642544592 scopus 로고    scopus 로고
    • Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter
    • Metivier R., Penot G., Hubner M.R., Reid G., Brand H., Kos M., and Gannon F. Estrogen receptor-alpha directs ordered, cyclical, and combinatorial recruitment of cofactors on a natural target promoter. Cell 115 (2003) 751-763
    • (2003) Cell , vol.115 , pp. 751-763
    • Metivier, R.1    Penot, G.2    Hubner, M.R.3    Reid, G.4    Brand, H.5    Kos, M.6    Gannon, F.7
  • 24
    • 0026768322 scopus 로고
    • A limiting factor mediates the differential activation of promoters by the human progesterone receptor isoforms
    • Meyer M.E., Quirin-Stricker C., Lerouge T., Bocquel M.T., and Gronemeyer H. A limiting factor mediates the differential activation of promoters by the human progesterone receptor isoforms. J. Biol. Chem. 267 (1992) 10882-10887
    • (1992) J. Biol. Chem. , vol.267 , pp. 10882-10887
    • Meyer, M.E.1    Quirin-Stricker, C.2    Lerouge, T.3    Bocquel, M.T.4    Gronemeyer, H.5
  • 25
    • 1942502820 scopus 로고    scopus 로고
    • Rapid periodic binding and displacement of the glucocorticoid receptor during chromatin remodeling
    • Nagaich A.K., Walker D.A., Wolford R., and Hager G.L. Rapid periodic binding and displacement of the glucocorticoid receptor during chromatin remodeling. Mol. Cell 14 (2004) 163-174
    • (2004) Mol. Cell , vol.14 , pp. 163-174
    • Nagaich, A.K.1    Walker, D.A.2    Wolford, R.3    Hager, G.L.4
  • 27
    • 0025007114 scopus 로고
    • Quantitative analysis of the glucocorticoid receptor-DNA interaction at the mouse mammary tumor virus glucocorticoid response element
    • Perlmann T., Eriksson P., and Wrange O. Quantitative analysis of the glucocorticoid receptor-DNA interaction at the mouse mammary tumor virus glucocorticoid response element. J. Biol. Chem. 265 (1990) 17222-17229
    • (1990) J. Biol. Chem. , vol.265 , pp. 17222-17229
    • Perlmann, T.1    Eriksson, P.2    Wrange, O.3
  • 28
    • 0037085303 scopus 로고    scopus 로고
    • Differential gene regulation by the two progesterone receptor isoforms in human breast cancer cells
    • Richer J.K., Jacobsen B.M., Manning N.G., Abel M.G., Wolf D.M., and Horwitz K.B. Differential gene regulation by the two progesterone receptor isoforms in human breast cancer cells. J. Biol. Chem. 277 (2002) 5209-5218
    • (2002) J. Biol. Chem. , vol.277 , pp. 5209-5218
    • Richer, J.K.1    Jacobsen, B.M.2    Manning, N.G.3    Abel, M.G.4    Wolf, D.M.5    Horwitz, K.B.6
  • 29
    • 0028073682 scopus 로고
    • A third transactivation function (AF3) of human progesterone receptors located in the unique N-terminal segment of the B-isoform
    • Sartorius C.A., Melville M.Y., Hovland A.R., Tung L., Takimoto G.S., and Horwitz K.B. A third transactivation function (AF3) of human progesterone receptors located in the unique N-terminal segment of the B-isoform. Mol. Endocrin. 8 (1994) 1347-1360
    • (1994) Mol. Endocrin. , vol.8 , pp. 1347-1360
    • Sartorius, C.A.1    Melville, M.Y.2    Hovland, A.R.3    Tung, L.4    Takimoto, G.S.5    Horwitz, K.B.6
  • 30
    • 0016451915 scopus 로고
    • Methods for extraction and quantification of receptors
    • Schrader W.T. Methods for extraction and quantification of receptors. Methods Enzymol. 36 (1975) 187-211
    • (1975) Methods Enzymol. , vol.36 , pp. 187-211
    • Schrader, W.T.1
  • 31
    • 0027308214 scopus 로고
    • Effects of anomalous migration and DNA to protein ratios on resolution of equilibrium constants from gel mobility-shift assays
    • Senear D.F., Dalma-Weiszhausz D.D., and Brenowitz M. Effects of anomalous migration and DNA to protein ratios on resolution of equilibrium constants from gel mobility-shift assays. Electrophoresis 14 (1993) 704-712
    • (1993) Electrophoresis , vol.14 , pp. 704-712
    • Senear, D.F.1    Dalma-Weiszhausz, D.D.2    Brenowitz, M.3
  • 32
    • 0025868144 scopus 로고
    • Differential DNA binding by calf uterine estrogen and progesterone receptors results from differences in oligomeric states
    • Skafar D.F. Differential DNA binding by calf uterine estrogen and progesterone receptors results from differences in oligomeric states. Biochemistry 30 (1991) 6148-6154
    • (1991) Biochemistry , vol.30 , pp. 6148-6154
    • Skafar, D.F.1
  • 33
    • 0021273674 scopus 로고
    • Characterization of the calf uterine progesterone receptor and its stabilization by nucleic acids
    • Theofan G., and Notides A.C. Characterization of the calf uterine progesterone receptor and its stabilization by nucleic acids. Endocrinology 114 (1984) 1173-1179
    • (1984) Endocrinology , vol.114 , pp. 1173-1179
    • Theofan, G.1    Notides, A.C.2
  • 34
    • 0028283503 scopus 로고
    • Molecular mechanisms of action of steroid/thyroid receptor superfamily members
    • Tsai M.J., and O'Malley B.W. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu. Rev. Biochem. 63 (1994) 451-486
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 451-486
    • Tsai, M.J.1    O'Malley, B.W.2
  • 35
    • 0024559926 scopus 로고
    • Cooperative binding of steroid hormone receptors contributes to transcriptional synergism at target enhancer elements
    • Tsai S.Y., Tsai M.-J., and O'Malley B.W. Cooperative binding of steroid hormone receptors contributes to transcriptional synergism at target enhancer elements. Cell 57 (1989) 443-448
    • (1989) Cell , vol.57 , pp. 443-448
    • Tsai, S.Y.1    Tsai, M.-J.2    O'Malley, B.W.3
  • 36
    • 0345650665 scopus 로고    scopus 로고
    • Activation functions 1 and 2 of nuclear receptors: Molecular strategies for transcriptional activation
    • Warnmark A., Treuter E., Wright A.P.H., and Gustafsson J.-A. Activation functions 1 and 2 of nuclear receptors: Molecular strategies for transcriptional activation. Mol. Endocrin. 17 (2003) 1901-1909
    • (2003) Mol. Endocrin. , vol.17 , pp. 1901-1909
    • Warnmark, A.1    Treuter, E.2    Wright, A.P.H.3    Gustafsson, J.-A.4


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