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Volumn 57, Issue 1-2, 1996, Pages 43-50

Putative steroid binding domain of the human mineralocorticoid receptor, expressed in E. coli in the presence of heat shock proteins shows typical native receptor characteristics

Author keywords

[No Author keywords available]

Indexed keywords

ALDOSTERONE; CORTICOSTERONE; GLUTATHIONE TRANSFERASE; HEAT SHOCK PROTEIN; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; MINERALOCORTICOID RECEPTOR; PROGESTERONE; SPIRONOLACTONE;

EID: 0029935336     PISSN: 09600760     EISSN: None     Source Type: Journal    
DOI: 10.1016/0960-0760(95)00250-2     Document Type: Article
Times cited : (14)

References (29)
  • 1
    • 0022327612 scopus 로고
    • Steroid receptor regulated transcription of specific genes and gene networks
    • Yamamoto K. R.: Steroid receptor regulated transcription of specific genes and gene networks. A. Rev. Genet. 19 (1985) 209-252.
    • (1985) A. Rev. Genet. , vol.19 , pp. 209-252
    • Yamamoto, K.R.1
  • 3
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor super-family
    • Evans R. M.: The steroid and thyroid hormone receptor super-family. Science 240 (1988) 889-895.
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 4
    • 0023221667 scopus 로고
    • Cloning of human mineralocorticoid receptor complementary DNA: Structural and functional kinship with the glucocorticoid receptor
    • Arriza J. L., Weinberger C., Cerelli G., Glaser T. M., Handelin B. L., Housman D. E. and Evans R. M.: Cloning of human mineralocorticoid receptor complementary DNA: structural and functional kinship with the glucocorticoid receptor. Science 237 (1987) 268-275.
    • (1987) Science , vol.237 , pp. 268-275
    • Arriza, J.L.1    Weinberger, C.2    Cerelli, G.3    Glaser, T.M.4    Handelin, B.L.5    Housman, D.E.6    Evans, R.M.7
  • 5
    • 0023649571 scopus 로고
    • Co-localization of DNA-binding and transcriptional activation function in the human glucocorticoid receptor
    • Hollenberg S. M., Giguere V., Segui P. and Evans R. M.: Co-localization of DNA-binding and transcriptional activation function in the human glucocorticoid receptor. Cell 49 (1987) 39-46.
    • (1987) Cell , vol.49 , pp. 39-46
    • Hollenberg, S.M.1    Giguere, V.2    Segui, P.3    Evans, R.M.4
  • 6
    • 0026079736 scopus 로고
    • Overexpression and characterization of the human mineralocoritcoid receptor
    • Alnemri E. S., Maksymowych A. B., Robertson N. M. and Litwack G. : Overexpression and characterization of the human mineralocoritcoid receptor. J. Biol. Chem. 266 (1991) 18,072-18,081.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18072-18081
    • Alnemri, E.S.1    Maksymowych, A.B.2    Robertson, N.M.3    Litwack, G.4
  • 7
    • 0025787868 scopus 로고
    • Characterization of human mineralocorticosteroid receptor expressed in the baculovirus system
    • Binart N., Lombes M., Rafestin-Oblin M. E. and Beaulieu E. E.: Characterization of human mineralocorticosteroid receptor expressed in the baculovirus system. Proc. Natn. Acad. Sci. U.S.A. 88 (1991) 10,681-10,685.
    • (1991) Proc. Natn. Acad. Sci. U.S.A. , vol.88 , pp. 10681-10685
    • Binart, N.1    Lombes, M.2    Rafestin-Oblin, M.E.3    Beaulieu, E.E.4
  • 8
    • 0026640216 scopus 로고
    • Association of the 90-kDa heat shock protein does not affect the ligand-binding ability of androgen receptor
    • Nemoto T., Ohara-Nemoto Y. and Ota M.: Association of the 90-kDa heat shock protein does not affect the ligand-binding ability of androgen receptor. J. Steroid Biochem. Molec. Biol. 42 (1992) 803-812.
    • (1992) J. Steroid Biochem. Molec. Biol. , vol.42 , pp. 803-812
    • Nemoto, T.1    Ohara-Nemoto, Y.2    Ota, M.3
  • 9
    • 0021261383 scopus 로고
    • Common non-hormone binding component in non transformed chick oviduct receptors of four steroid hormones
    • Joab I., Radanyi C., Renoir M., Buchou T., Catelli M. G., Binart N., Mester J. and Baulieu E. E.: Common non-hormone binding component in non transformed chick oviduct receptors of four steroid hormones. Nature 308 (1984) 850-853.
    • (1984) Nature , vol.308 , pp. 850-853
    • Joab, I.1    Radanyi, C.2    Renoir, M.3    Buchou, T.4    Catelli, M.G.5    Binart, N.6    Mester, J.7    Baulieu, E.E.8
  • 10
    • 0026343608 scopus 로고
    • Structure of the glucocorticoid receptor in the absence of hormone
    • Rexin M., Busch W. and Gehring U.: Structure of the glucocorticoid receptor in the absence of hormone. J. Biol. Chem. 266 (1991) 24,601-24,605.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24601-24605
    • Rexin, M.1    Busch, W.2    Gehring, U.3
  • 11
    • 0027451956 scopus 로고
    • The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptors
    • Pratt W. B.: The role of heat shock proteins in regulating the function, folding, and trafficking of the glucocorticoid receptors. J. Biol. Chem. 268 (1993) 21,455-21,458.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21455-21458
    • Pratt, W.B.1
  • 12
    • 0027305758 scopus 로고
    • A bacterially expressed mineralocorticoid receptor is associated in vitro with the 90-kilodalton heat shock protein and shows typical hormone- and DNA-binding characteristics
    • Caamaño C. A., Morano M. I., Patel P. D., Watson S. J. and Akil U.: A bacterially expressed mineralocorticoid receptor is associated in vitro with the 90-kilodalton heat shock protein and shows typical hormone- and DNA-binding characteristics. Biochemistry 32 (1993) 8589-8595.
    • (1993) Biochemistry , vol.32 , pp. 8589-8595
    • Caamaño, C.A.1    Morano, M.I.2    Patel, P.D.3    Watson, S.J.4    Akil, U.5
  • 13
    • 0024567048 scopus 로고
    • Evidence that the 90 kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor
    • Bresnick E. H., Dalman F. C., Sanchez E. R. and Pratt W. B.: Evidence that the 90 kDa heat shock protein is necessary for the steroid binding conformation of the L cell glucocorticoid receptor. J. Biol. Chem. 264 (1989) 4992-4997.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4992-4997
    • Bresnick, E.H.1    Dalman, F.C.2    Sanchez, E.R.3    Pratt, W.B.4
  • 14
    • 0024332067 scopus 로고
    • Direct evidence that the glucocorticoid receptor binds to hsp90 at or near the termination of receptor translation in vitro
    • Dalman F. C., Bresnick E. H., Patel P. D., Pardew G. H., Watson S. J. and Pratt W. B.: Direct evidence that the glucocorticoid receptor binds to hsp90 at or near the termination of receptor translation in vitro. J. Biol. Chem. 264 (1989) 19,815-19,819.
    • (1989) J. Biol. Chem. , vol.264 , pp. 19815-19819
    • Dalman, F.C.1    Bresnick, E.H.2    Patel, P.D.3    Pardew, G.H.4    Watson, S.J.5    Pratt, W.B.6
  • 15
    • 0026543821 scopus 로고
    • Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events
    • Smith D. F., Stensgard B. A., Welch W. J. and Toft D. O.: Assembly of progesterone receptor with heat shock proteins and receptor activation are ATP mediated events. J. Biol. Chem. 267 (1992) 1350-1356.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1350-1356
    • Smith, D.F.1    Stensgard, B.A.2    Welch, W.J.3    Toft, D.O.4
  • 16
    • 0027239861 scopus 로고
    • Mutational analysis of hsp90 binding to the progesterone receptor
    • Sullivan W. P. and Toft D. O.: Mutational analysis of hsp90 binding to the progesterone receptor. J. Biol. Chem. 268 (1993) 20,373-20,379.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20373-20379
    • Sullivan, W.P.1    Toft, D.O.2
  • 17
    • 0024461893 scopus 로고
    • Expression of active hormone and DNA-binding domains of the chicken progresterone receptor in E. coli
    • Eul J., Meyer M. E., Tora L., Bocquel M. T., Quirin-Stricker C., Chambon P. and Gronemeyer H.: Expression of active hormone and DNA-binding domains of the chicken progresterone receptor in E. coli. EMBO J. 8 (1989) 83-90.
    • (1989) EMBO J. , vol.8 , pp. 83-90
    • Eul, J.1    Meyer, M.E.2    Tora, L.3    Bocquel, M.T.4    Quirin-Stricker, C.5    Chambon, P.6    Gronemeyer, H.7
  • 19
    • 0028278467 scopus 로고
    • Development of specific bioluminescent in vitro assays for selecting potential antimineralocorticoids
    • Jausons-Loffreda N., Balaguer P., Auzou G. and Pons M.: Development of specific bioluminescent in vitro assays for selecting potential antimineralocorticoids. J. Steroid. Biochem. Molec. Biol. 49 (1994) 31-38.
    • (1994) J. Steroid. Biochem. Molec. Biol. , vol.49 , pp. 31-38
    • Jausons-Loffreda, N.1    Balaguer, P.2    Auzou, G.3    Pons, M.4
  • 20
    • 0028200018 scopus 로고
    • The hormone binding domain of the mineralocorticoid receptor can regulate heterologous activities in cis
    • Fankhauser C. P., Briand P. A. and Picard D.: The hormone binding domain of the mineralocorticoid receptor can regulate heterologous activities in cis. Biochem. Biophys. Res. Commun. 200 (1994) 195-201.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 195-201
    • Fankhauser, C.P.1    Briand, P.A.2    Picard, D.3
  • 25
    • 0026548053 scopus 로고
    • Aldosterone antagonists destabilize the mineralocorticosteroid receptor
    • Couette B., Lombes M., Baulieu E. E. and Rafestin-Oblin M. E.: Aldosterone antagonists destabilize the mineralocorticosteroid receptor. Biochem. J. 282 (1992) 697-702.
    • (1992) Biochem. J. , vol.282 , pp. 697-702
    • Couette, B.1    Lombes, M.2    Baulieu, E.E.3    Rafestin-Oblin, M.E.4
  • 26
    • 0028284571 scopus 로고
    • Assisting spontaneity: The role of hsp90 and small hsps as molecular chaperones
    • Jakob U. and Buchner J.: Assisting spontaneity: the role of hsp90 and small hsps as molecular chaperones. TIBS 19 (1994) 205-211.
    • (1994) TIBS , vol.19 , pp. 205-211
    • Jakob, U.1    Buchner, J.2
  • 27
    • 0027954495 scopus 로고
    • Heat-shock proteins as molecular chaperones
    • Becker J. and Craig A.: Heat-shock proteins as molecular chaperones. Eur. J. Biochem. 219 (1994) 11-23.
    • (1994) Eur. J. Biochem. , vol.219 , pp. 11-23
    • Becker, J.1    Craig, A.2
  • 28
    • 0027429134 scopus 로고
    • Interaction of glucocorticosteroid receptor and wild-type or mutated 90-kDa heat shock protein coexpressed in baculovirus-infected Sf9 cells
    • Cadepond F., Binart B., Chambraud B., Jibard N., Schweizer-Groyer G., Segard-Maurel I. and Baulieu E. E.: Interaction of glucocorticosteroid receptor and wild-type or mutated 90-kDa heat shock protein coexpressed in baculovirus-infected Sf9 cells. Proc. Natn. Acad. Sci. 90 (1993) 10,434-10,438.
    • (1993) Proc. Natn. Acad. Sci. , vol.90 , pp. 10434-10438
    • Cadepond, F.1    Binart, B.2    Chambraud, B.3    Jibard, N.4    Schweizer-Groyer, G.5    Segard-Maurel, I.6    Baulieu, E.E.7
  • 29
    • 0024554231 scopus 로고
    • Purification and properties of the Escherichia coli heat shock protein, HtpG
    • Spence J. and Georgopoulos C.: Purification and properties of the Escherichia coli heat shock protein, HtpG. J. Biol. Chem. 264 (1989) 4398-4403.
    • (1989) J. Biol. Chem. , vol.264 , pp. 4398-4403
    • Spence, J.1    Georgopoulos, C.2


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