메뉴 건너뛰기




Volumn 49, Issue 3, 2002, Pages 747-756

Functionality versus strength - Has functional selection taken place in the case of the ecdysteroid receptor response element?

Author keywords

20 hydroxyecdysone; Drosophila; Ecdysteroid receptor; Nuclear receptor; Protein DNA interaction; Ultraspiracle

Indexed keywords

EUKARYOTA;

EID: 0041375245     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.2002_3783     Document Type: Article
Times cited : (7)

References (39)
  • 1
    • 0027347114 scopus 로고
    • Structural features critical to the activity of an ecdysone receptor binding site
    • Antoniewski C, Lavai M, Lepesant JA. (1993) Structural features critical to the activity of an ecdysone receptor binding site. Insect Biochem Mol Biol.; 23: 105-14.
    • (1993) Insect Biochem Mol Biol , vol.23 , pp. 105-114
    • Antoniewski, C.1    Lavai, M.2    Lepesant, J.A.3
  • 2
    • 0028304668 scopus 로고
    • The ecdysone response enhancer of the Fbp1 gene of Drosophila melanogaster is a direct target for the EcR/USP nuclear receptor
    • Antoniewski C, Laval M, Dahan A, Lepesant JA. (1994) The ecdysone response enhancer of the Fbp1 gene of Drosophila melanogaster is a direct target for the EcR/USP nuclear receptor. Mol Cell Biol.; 14: 4465-74.
    • (1994) Mol Cell Biol , vol.14 , pp. 4465-4474
    • Antoniewski, C.1    Laval, M.2    Dahan, A.3    Lepesant, J.A.4
  • 3
    • 0029591830 scopus 로고
    • Characterization of an EcR/USP heterodimer target site that mediates ecdysone responsiveness of the Drosophila Lsp-2 gene
    • Antoniewski C, O'Grady MS, Edmondson RG, Lassieur SM, Benes H. (1995) Characterization of an EcR/USP heterodimer target site that mediates ecdysone responsiveness of the Drosophila Lsp-2 gene. Mol Gen Genet.; 249: 545-56.
    • (1995) Mol Gen Genet. , vol.249 , pp. 545-556
    • Antoniewski, C.1    O'Grady, M.S.2    Edmondson, R.G.3    Lassieur, S.M.4    Benes, H.5
  • 4
    • 0029245364 scopus 로고
    • Site-directed mutagenesis by double polymerase chain reaction
    • Barik S. (1995) Site-directed mutagenesis by double polymerase chain reaction. Mol Biotechnol.; 3: 1-7.
    • (1995) Mol Biotechnol , vol.3 , pp. 1-7
    • Barik, S.1
  • 5
    • 0026069609 scopus 로고
    • Identification of ecdysone response elements by analysis of the Drosophila Eip28/29 gene
    • Cherbas L, Lee K, Cherbas P. (1991) Identification of ecdysone response elements by analysis of the Drosophila Eip28/29 gene. Genes Dev.; 5: 120-31.
    • (1991) Genes Dev , vol.5 , pp. 120-131
    • Cherbas, L.1    Lee, K.2    Cherbas, P.3
  • 6
    • 0023913120 scopus 로고
    • The steroid and thyroid hormone receptor superfamily
    • Evans RM. (1988) The steroid and thyroid hormone receptor superfamily. Science.; 240: 889-95.
    • (1988) Science , vol.240 , pp. 889-895
    • Evans, R.M.1
  • 7
    • 0023769378 scopus 로고
    • The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain
    • Freedman LP, Luisi BF, Korszun ZR, Basavappa R, Sigler PB, Yamamoto KR. (1988) The function and structure of the metal coordination sites within the glucocorticoid receptor DNA binding domain. Nature.; 334: 543-46.
    • (1988) Nature , vol.334 , pp. 543-546
    • Freedman, L.P.1    Luisi, B.F.2    Korszun, Z.R.3    Basavappa, R.4    Sigler, P.B.5    Yamamoto, K.R.6
  • 8
    • 0019878376 scopus 로고
    • Equilibria and kinetics of lac represser-operator interactions by polyacrylamide gel electrophoresis
    • Fried M, Crothers DM. (1981) Equilibria and kinetics of lac represser-operator interactions by polyacrylamide gel electrophoresis. Nucleic Acids Res.; 9: 6505-25.
    • (1981) Nucleic Acids Res , vol.9 , pp. 6505-6525
    • Fried, M.1    Crothers, D.M.2
  • 9
    • 0031612706 scopus 로고    scopus 로고
    • Steroid hormone receptors and heat shock proteins
    • Gehring U. (1998) Steroid hormone receptors and heat shock proteins. Vitam Horm.; 54: 167-205.
    • (1998) Vitam Horm , vol.54 , pp. 167-205
    • Gehring, U.1
  • 10
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill SC, von Hippel PH. (1989) Calculation of protein extinction coefficients from amino acid sequence data. Anal Biochem.; 182: 319-26.
    • (1989) Anal Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    Von Hippel, P.H.2
  • 11
    • 0034826007 scopus 로고    scopus 로고
    • Analysis of Usp DNA-binding domain targeting reveals critical determinants of the ecdysone receptor complex interaction with the response element
    • Grad I, Niedziela-Majka A, Kochman M, Ożyhar A. (2001) Analysis of Usp DNA-binding domain targeting reveals critical determinants of the ecdysone receptor complex interaction with the response element. Eur J Biochem.; 268: 3751-8.
    • (2001) Eur J Biochem , vol.268 , pp. 3751-3758
    • Grad, I.1    Niedziela-Majka, A.2    Kochman, M.3    Ozyhar, A.4
  • 12
    • 0024095250 scopus 로고
    • The N-terminal DNA-binding 'zinc finger' of the oestrogen and glucocorticoid receptors determines target gene specificity
    • Green S, Kumar V, Theulaz I, Wahli W, Chambon P. (1988) The N-terminal DNA-binding 'zinc finger' of the oestrogen and glucocorticoid receptors determines target gene specificity. EMBO J.; 7: 3037-44.
    • (1988) EMBO J , vol.7 , pp. 3037-3044
    • Green, S.1    Kumar, V.2    Theulaz, I.3    Wahli, W.4    Chambon, P.5
  • 13
    • 0029440036 scopus 로고
    • Transcription factors 3: Nuclear receptors
    • Gronemeyer H, Laudet V. (1995) Transcription factors 3: nuclear receptors. Protein Profile.; 2: 1173-308.
    • (1995) Protein Profile , vol.2 , pp. 1173-1308
    • Gronemeyer, H.1    Laudet, V.2
  • 14
    • 0026416169 scopus 로고
    • The Drosophila EcR gene encodes an ecdysone receptor, a new member of the steroid receptor superfamily
    • Koelle MR, Talbot WS, Segraves WA, Bender MT, Cherbas P, Hogness DS. (1991) The Drosophila EcR gene encodes an ecdysone receptor, a new member of the steroid receptor superfamily. Cell.; 67: 59-77.
    • (1991) Cell , vol.67 , pp. 59-77
    • Koelle, M.R.1    Talbot, W.S.2    Segraves, W.A.3    Bender, M.T.4    Cherbas, P.5    Hogness, D.S.6
  • 15
    • 0033846989 scopus 로고    scopus 로고
    • Steroid regulation of postembryonic development and reproduction in Drosophila
    • Kozlova T, Thummel CS. (2000) Steroid regulation of postembryonic development and reproduction in Drosophila. Trends Endocrin Metab.; 11: 276-80.
    • (2000) Trends Endocrin Metab , vol.11 , pp. 276-280
    • Kozlova, T.1    Thummel, C.S.2
  • 16
    • 0028962370 scopus 로고
    • Ecdysone regulation of the Drosophila Sgs-4 gene is mediated by the synergistic action of ecdysone receptor and SEBP 3
    • Lehmann M, Korge G. (1995) Ecdysone regulation of the Drosophila Sgs-4 gene is mediated by the synergistic action of ecdysone receptor and SEBP 3. EMBO J.; 14: 716-26.
    • (1995) EMBO J , vol.14 , pp. 716-726
    • Lehmann, M.1    Korge, G.2
  • 17
    • 0031079790 scopus 로고    scopus 로고
    • Two new regulatory elements controlling the Drosophila Sgs-3 gene are potential ecdysone receptor and fork head binding sites
    • Lehmann M, Wattler F, Korge G. (1997) Two new regulatory elements controlling the Drosophila Sgs-3 gene are potential ecdysone receptor and fork head binding sites. Mech Dev.; 62: 15-27.
    • (1997) Mech Dev , vol.62 , pp. 15-27
    • Lehmann, M.1    Wattler, F.2    Korge, G.3
  • 18
    • 0024600621 scopus 로고
    • Three amino acids of the oestrogen receptor are essential to its ability to distinguish an oestrogen from a glucocorticoid-responsive element
    • Mader S, Kumar V, de Verneuil H, Chambon P. (1989) Three amino acids of the oestrogen receptor are essential to its ability to distinguish an oestrogen from a glucocorticoid-responsive element. Nature.; 338: 271-4.
    • (1989) Nature , vol.338 , pp. 271-274
    • Mader, S.1    Kumar, V.2    De Verneuil, H.3    Chambon, P.4
  • 19
    • 0032964122 scopus 로고    scopus 로고
    • DNA-binding mechanism of the monomeric orphan nuclear receptor NGFI-B
    • Meinke G, Sigler PB. (1999) DNA-binding mechanism of the monomeric orphan nuclear receptor NGFI-B. Nat Struct Biol.; 6: 471-7.
    • (1999) Nat Struct Biol , vol.6 , pp. 471-477
    • Meinke, G.1    Sigler, P.B.2
  • 20
    • 0033342984 scopus 로고    scopus 로고
    • Determinants of DNA sequence specificity of the androgen, progesterone, and glucocorticoid receptors: Evidence for differential steroid receptor response elements
    • Nelson CC, Hendy SC, Shukin RJ, Cheng H, Bruchovsky N, Koop BF, Rennie PS. (1999) Determinants of DNA sequence specificity of the androgen, progesterone, and glucocorticoid receptors: evidence for differential steroid receptor response elements. Mol Endocrinol.; 13: 2090-107.
    • (1999) Mol Endocrinol , vol.13 , pp. 2090-2107
    • Nelson, C.C.1    Hendy, S.C.2    Shukin, R.J.3    Cheng, H.4    Bruchovsky, N.5    Koop, B.F.6    Rennie, P.S.7
  • 21
    • 0032209665 scopus 로고    scopus 로고
    • Pure, bacterially expressed DNA-binding domains of the functional ecdysteroid receptor capable of interacting synergistically with the hsp27 20-hydroxyecdysone response element. GST-Induced dimerization of DNA-binding domains alters characteristics of their interaction with DNA
    • Niedziela-Majka A, Rymarczyk G, Kochman M, Ożyhar A. (1998) Pure, bacterially expressed DNA-binding domains of the functional ecdysteroid receptor capable of interacting synergistically with the hsp27 20-hydroxyecdysone response element. GST-Induced dimerization of DNA-binding domains alters characteristics of their interaction with DNA. Protein Expr Purif.; 14: 208-20.
    • (1998) Protein Expr Purif , vol.14 , pp. 208-220
    • Niedziela-Majka, A.1    Rymarczyk, G.2    Kochman, M.3    Ozyhar, A.4
  • 22
    • 0033956886 scopus 로고    scopus 로고
    • Polarity of the ecdysone receptor complex interaction with the palindromic response element from the hsp27 gene promoter
    • Niedziela-Majka A, Kochman M, Ożyhar A. (2000) Polarity of the ecdysone receptor complex interaction with the palindromic response element from the hsp27 gene promoter. Eur J Biochem.; 267: 507-19.
    • (2000) Eur J Biochem , vol.267 , pp. 507-519
    • Niedziela-Majka, A.1    Kochman, M.2    Ozyhar, A.3
  • 23
    • 0025091575 scopus 로고
    • Relationship between the product of the Drosophila ultraspiracle locus and the vertebrate retinoid X receptor
    • Oro AE, McKeown M, Evans RM. (1990) Relationship between the product of the Drosophila ultraspiracle locus and the vertebrate retinoid X receptor. Nature.; 347: 298-301.
    • (1990) Nature , vol.347 , pp. 298-301
    • Oro, A.E.1    McKeown, M.2    Evans, R.M.3
  • 24
    • 0025819918 scopus 로고
    • Characterization of a specific ecdysteroid receptor-DNa complex reveals common properties for invertebrate and vertebrate hormone-receptor/DNa interactions
    • Ożyhar A, Strangmann-Diekmann M, Kiltz HH, Pongs O. (1991) Characterization of a specific ecdysteroid receptor-DNA complex reveals common properties for invertebrate and vertebrate hormone-receptor/DNA interactions. Eur J Biochem.; 200: 329-35.
    • (1991) Eur J Biochem , vol.200 , pp. 329-335
    • Ozyhar, A.1    Strangmann-Diekmann, M.2    Kiltz, H.H.3    Pongs, O.4
  • 25
    • 0029044997 scopus 로고
    • Structural determinants of nuclear receptor assembly on DNA direct repeats
    • Rastinejad F, Perlmann T, Evans RM, Sigler PB. (1995) Structural determinants of nuclear receptor assembly on DNA direct repeats. Nature.; 375: 203-11.
    • (1995) Nature , vol.375 , pp. 203-211
    • Rastinejad, F.1    Perlmann, T.2    Evans, R.M.3    Sigler, P.B.4
  • 26
    • 0034161266 scopus 로고    scopus 로고
    • Structure of the RXR-RAR DNA-binding complex on the retinoic acid response element DR1
    • Rastinejad F, Wagner T, Zhao Q, Khorasanizadeh S. (2000) Structure of the RXR-RAR DNA-binding complex on the retinoic acid response element DR1. EMBO J.; 19: 1045-54.
    • (2000) EMBO J , vol.19 , pp. 1045-1054
    • Rastinejad, F.1    Wagner, T.2    Zhao, Q.3    Khorasanizadeh, S.4
  • 27
    • 0033711971 scopus 로고    scopus 로고
    • Structural studies on nuclear receptors
    • Renaud JP, Moras D. (2000) Structural studies on nuclear receptors. Cell Mol Life Sci.; 57: 1748-69.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1748-1769
    • Renaud, J.P.1    Moras, D.2
  • 28
    • 0001606007 scopus 로고
    • An ecdysone response element in the Drosophila hsp27 promoter
    • Riddihough G, Pelham HRB. (1987) An ecdysone response element in the Drosophila hsp27 promoter. EMBO J.; 6: 3729-34.
    • (1987) EMBO J , vol.6 , pp. 3729-3734
    • Riddihough, G.1    Pelham, H.R.B.2
  • 29
    • 0027365669 scopus 로고
    • The crystal structure of the estrogen receptor DNA-binding domain bound to DNA: How receptors discriminate between their response elements
    • Schwabe JW, Chapman L, Finch JT, 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: 567-78.
    • (1993) Cell , vol.75 , pp. 567-578
    • Schwabe, J.W.1    Chapman, L.2    Finch, J.T.3    Rhodes, D.4
  • 30
    • 0035313496 scopus 로고    scopus 로고
    • Nuclear receptors in nematodes: Themes and variations
    • Sluder AE, Maina CV. (2001) Nuclear receptors in nematodes: themes and variations. Trends Genet.; 17: 206-13.
    • (2001) Trends Genet , vol.17 , pp. 206-213
    • Sluder, A.E.1    Maina, C.V.2
  • 31
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith DB, Johnson KS. (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene.; 67: 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 32
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • Studier FW. (1991) Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J Mol Biol.; 219: 37-44.
    • (1991) J Mol Biol , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 33
    • 0027340093 scopus 로고
    • Heterodimerization of the Drosophila ecdysone receptor with retinoid X receptor and ultraspiracle
    • Thomas HE, Stunnenberg HG, Stewart AF. (1993) Heterodimerization of the Drosophila ecdysone receptor with retinoid X receptor and ultraspiracle. Nature.; 362: 471-5.
    • (1993) Nature , vol.362 , pp. 471-475
    • Thomas, H.E.1    Stunnenberg, H.G.2    Stewart, A.F.3
  • 34
    • 0031835267 scopus 로고    scopus 로고
    • Co-activators and co-repressors in the integration of transcriptional responses
    • Torchia J, Glass C, Rosenfeld MG. (1998) Co-activators and co-repressors in the integration of transcriptional responses. Curr Opin Cell Biol.; 10: 373-83.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 373-383
    • Torchia, J.1    Glass, C.2    Rosenfeld, M.G.3
  • 35
    • 0024337858 scopus 로고
    • Determinants of target gene specificity for steroid/thyroid hormone receptors
    • Umesono K, Evans RM. (1989) Determinants of target gene specificity for steroid/thyroid hormone receptors. Cell.; 57: 1139-46.
    • (1989) Cell , vol.57 , pp. 1139-1146
    • Umesono, K.1    Evans, R.M.2
  • 36
    • 2642624626 scopus 로고    scopus 로고
    • High level transactivation by the ecdysone receptor complex at the core recognition motif
    • Vögtli M, Elke C, Imhof MO, Lezzi M. (1998) High level transactivation by the ecdysone receptor complex at the core recognition motif. Nucleic Acids Res.; 26: 2407-14.
    • (1998) Nucleic Acids Res , vol.26 , pp. 2407-2414
    • Vögtli, M.1    Elke, C.2    Imhof, M.O.3    Lezzi, M.4
  • 37
    • 0026646635 scopus 로고
    • Drosophila ultraspiracle modulates ecdysone receptor function via heterodimer formation
    • Yao TP, Segraves WA, Oro AE, McKeown M, Evans RM. (1992) Drosophila ultraspiracle modulates ecdysone receptor function via heterodimer formation. Cell.; 71: 63-72.
    • (1992) Cell , vol.71 , pp. 63-72
    • Yao, T.P.1    Segraves, W.A.2    Oro, A.E.3    McKeown, M.4    Evans, R.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.