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Volumn 45, Issue 3, 2006, Pages 668-675

The DNA-binding domain of the ultraspiracle drives deformation of the response element whereas the DNA-binding domain of the ecdysone receptor is responsible for a slight additional change of the preformed structure

Author keywords

[No Author keywords available]

Indexed keywords

DIMERS; ENZYMES; FLUORESCENCE; GELS; GENES; PROTEINS;

EID: 31044441892     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051354b     Document Type: Article
Times cited : (8)

References (43)
  • 1
    • 3142760881 scopus 로고    scopus 로고
    • DNA recognition by nuclear receptors
    • Claessens, F., and Gewirth, D. T. (2004) DNA recognition by nuclear receptors, Essays Biochem. 40, 59-72.
    • (2004) Essays Biochem. , vol.40 , pp. 59-72
    • Claessens, F.1    Gewirth, D.T.2
  • 2
    • 0026490544 scopus 로고
    • Use of gel retardation to analyze protein-nucleic acid interactions
    • Lane, D., Prentki, P., and Chandler, M. (1992) Use of gel retardation to analyze protein-nucleic acid interactions, Microbiol. Rev. 56, 509-528.
    • (1992) Microbiol. Rev. , vol.56 , pp. 509-528
    • Lane, D.1    Prentki, P.2    Chandler, M.3
  • 3
    • 0029757625 scopus 로고    scopus 로고
    • Effects of wild type and mutant estrogen receptors on DNA flexibility, DNA bending, and transcription activation
    • Potthoff, S. J., Romine, L. E., and Nardulli, A. M. (1996) Effects of wild type and mutant estrogen receptors on DNA flexibility, DNA bending, and transcription activation, Mol. Endocrinol. 10, 1095-1106.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 1095-1106
    • Potthoff, S.J.1    Romine, L.E.2    Nardulli, A.M.3
  • 4
    • 0028937343 scopus 로고
    • DNA bending by thyroid hormone receptor: Influence of half-site spacing and RXR
    • Shulemovich, K., Dimaculangan, D. D., Katz, D., and Lazar, M. A. (1995) DNA bending by thyroid hormone receptor: influence of half-site spacing and RXR, Nucleic Acids Res. 23, 811-818.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 811-818
    • Shulemovich, K.1    Dimaculangan, D.D.2    Katz, D.3    Lazar, M.A.4
  • 5
    • 0030995770 scopus 로고    scopus 로고
    • DNA bending is induced by binding of the glucocorticoid receptor DNA binding domain and progesterone receptors to their response element
    • Petz, L. N., Nardulli, A. M., Kim, J., Horwitz, K. B., Freedman, L. P., and Shapiro, D. J. (1997) DNA bending is induced by binding of the glucocorticoid receptor DNA binding domain and progesterone receptors to their response element, J. Steroid Biochem. Mol. Biol. 60, 31-41.
    • (1997) J. Steroid Biochem. Mol. Biol. , vol.60 , pp. 31-41
    • Petz, L.N.1    Nardulli, A.M.2    Kim, J.3    Horwitz, K.B.4    Freedman, L.P.5    Shapiro, D.J.6
  • 6
    • 0029879137 scopus 로고    scopus 로고
    • Progesterone receptor-induced bending of its target DNA: Distinct effects of the a and B receptor forms
    • Prendergast, P., Pan, Z., and Edwards, D. P. (1996) Progesterone receptor-induced bending of its target DNA: distinct effects of the A and B receptor forms, Mol. Endocrinol. 10, 393-407.
    • (1996) Mol. Endocrinol. , vol.10 , pp. 393-407
    • Prendergast, P.1    Pan, Z.2    Edwards, D.P.3
  • 8
    • 0026646635 scopus 로고
    • Drosophila ultraspiracle modulates ecdysone receptor function via heterodimer formation
    • Yao, T. P., Segraves, W. A., Oro, A. E., McKeown, M., and Evans, R. M. (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
  • 9
    • 0027340093 scopus 로고
    • Heterodimerization of the Drosophila ecdysone receptor with retinoid X receptor and ultraspiracle
    • Thomas, H. E., Stunnenberg, H. G., and Stewart, A. F. (1993) Heterodimerization of the Drosophila ecdysone receptor with retinoid X receptor and ultraspiracle, Nature 362, 471-475.
    • (1993) Nature , vol.362 , pp. 471-475
    • Thomas, H.E.1    Stunnenberg, H.G.2    Stewart, A.F.3
  • 10
    • 0027139855 scopus 로고
    • Molecular analysis of the initiation of insect metamorphosis: A comparative study of Drosophila ecdysteroid-regulated transcription
    • Andres, A. J., Fletcher, J. C., Karim, F. D., and Thummel, C. S. (1993) Molecular analysis of the initiation of insect metamorphosis: a comparative study of Drosophila ecdysteroid-regulated transcription, Dev. Biol. 160, 388-404.
    • (1993) Dev. Biol. , vol.160 , pp. 388-404
    • Andres, A.J.1    Fletcher, J.C.2    Karim, F.D.3    Thummel, C.S.4
  • 11
    • 0037385168 scopus 로고    scopus 로고
    • Transcription activation by the ecdysone receptor (EcR/USP): Identification of activation functions
    • Hu, X., Cherbas, L., and Cherbas, P. (2003) Transcription activation by the ecdysone receptor (EcR/USP): identification of activation functions, Mol. Endocrinol. 17, 716-731.
    • (2003) Mol. Endocrinol. , vol.17 , pp. 716-731
    • Hu, X.1    Cherbas, L.2    Cherbas, P.3
  • 12
    • 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., and Ożyhar, A. (2000) Polarity of the ecdysone receptor complex interaction with the palindromic response element from the hsp27 gene promoter, Eur. J. Biochem. 267, 507-519.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 507-519
    • Niedziela-Majka, A.1    Kochman, M.2    Ozyhar, A.3
  • 13
    • 0035369335 scopus 로고    scopus 로고
    • Nuclear-receptor interactions on DNA-response elements
    • Khorasanizadeh, S., and Rastinejad, F. (2001) Nuclear-receptor interactions on DNA-response elements, Trends Biochem. Sci. 26, 384-390.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 384-390
    • Khorasanizadeh, S.1    Rastinejad, F.2
  • 14
    • 0001606007 scopus 로고
    • An ecdysone response element in the Drosophila hsp27 promoter
    • Riddihough, G., and Pelham, H. R. B. (1987) An ecdysone response element in the Drosophila hsp27 promoter, EMBO J. 6, 3729-3734.
    • (1987) EMBO J. , vol.6 , pp. 3729-3734
    • Riddihough, G.1    Pelham, H.R.B.2
  • 15
    • 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, H. H., and 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, 329-335.
    • (1991) Eur. J. Biochem. , vol.200 , pp. 329-335
    • Ozyhar, A.1    Strangmann-Diekmann, M.2    Kiltz, H.H.3    Pongs, O.4
  • 17
    • 1342310507 scopus 로고    scopus 로고
    • Oligomerization of hydrophobin SC3 in solution: From soluble state to self-assembly
    • Wang, X., Graveland-Bikker, J. F., de Kruif, C. G., and Robillard, G. T. (2004) Oligomerization of hydrophobin SC3 in solution: from soluble state to self-assembly, Protein Sci. 13, 810-821.
    • (2004) Protein Sci. , vol.13 , pp. 810-821
    • Wang, X.1    Graveland-Bikker, J.F.2    De Kruif, C.G.3    Robillard, G.T.4
  • 18
    • 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., and 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, 3751-3758.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 3751-3758
    • Grad, I.1    Niedziela-Majka, A.2    Kochman, M.3    Ozyhar, A.4
  • 19
    • 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., and 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 Expression Purif. 14, 208-220.
    • (1998) Protein Expression Purif. , vol.14 , pp. 208-220
    • Niedziela-Majka, A.1    Rymarczyk, G.2    Kochman, M.3    Ozyhar, A.4
  • 20
    • 0024814234 scopus 로고
    • Bending of DNA by gene-regulatory proteins: Construction and use of a DNA bending vector
    • Kim, J., Zwieb, C., Wu, C., and Adhya, S. (1989) Bending of DNA by gene-regulatory proteins: construction and use of a DNA bending vector, Gene 85, 15-23.
    • (1989) Gene , vol.85 , pp. 15-23
    • Kim, J.1    Zwieb, C.2    Wu, C.3    Adhya, S.4
  • 21
    • 84981779372 scopus 로고
    • Intermolecular energy migration and fluorescence
    • Förster, T. (1948) Intermolecular energy migration and fluorescence, Ann. Phys. (Lepzig) 2, 55-75.
    • (1948) Ann. Phys. (Lepzig) , vol.2 , pp. 55-75
    • Förster, T.1
  • 22
    • 0017917406 scopus 로고
    • (Hirs, C. H. W., and Timasheff, S. N., Eds.), Academic Press, New York
    • Fairclough, R. H., and Cantor, C. R. (1977) in Methods in Enzymology (Hirs, C. H. W., and Timasheff, S. N., Eds.) pp 347-379, Academic Press, New York.
    • (1977) Methods in Enzymology , pp. 347-379
    • Fairclough, R.H.1    Cantor, C.R.2
  • 23
    • 0027394243 scopus 로고
    • Observing the helical geometry of double-stranded DNA in solution by fluorescence resonance energy transfer
    • Clegg, R. M., Murchie, A. I., Zechel, A., and Lilley, D. M. (1993) Observing the helical geometry of double-stranded DNA in solution by fluorescence resonance energy transfer, Proc. Natl. Acad. Sci. U.S.A. 90, 2994-2998.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 2994-2998
    • Clegg, R.M.1    Murchie, A.I.2    Zechel, A.3    Lilley, D.M.4
  • 24
    • 0028072693 scopus 로고
    • Kinking of DNA and RNA helices by bulged nucleotides observed by fluorescence resonance energy transfer
    • Gohlke, C., Murchie, A. I., Lilley, D. M., and Clegg, R. M. (1994) Kinking of DNA and RNA helices by bulged nucleotides observed by fluorescence resonance energy transfer, Proc. Natl. Acad. Sci. U.S.A. 91, 11660-11664.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 11660-11664
    • Gohlke, C.1    Murchie, A.I.2    Lilley, D.M.3    Clegg, R.M.4
  • 25
    • 0029737547 scopus 로고    scopus 로고
    • Fluorescence characteristics of 5-carboxytetramethylrhodamine linked covalently to the 5′ end of oligonucleotides: Multiple conformers of single-stranded and double-stranded dye-DNA complexes
    • Vamosi, G., Gohlke, C., and Clegg, R. M. (1996) Fluorescence characteristics of 5-carboxytetramethylrhodamine linked covalently to the 5′ end of oligonucleotides: multiple conformers of single-stranded and double-stranded dye-DNA complexes, Biophys. J. 71, 972-994.
    • (1996) Biophys. J. , vol.71 , pp. 972-994
    • Vamosi, G.1    Gohlke, C.2    Clegg, R.M.3
  • 26
    • 0033485813 scopus 로고    scopus 로고
    • Global structure similarities of intact and nicked DNA complexed with IHF measured in solution by fluorescence resonance energy transfer
    • Lorenz, M., Hillisch, A., Goodman, S. D., and Diekmann, S. (1999) Global structure similarities of intact and nicked DNA complexed with IHF measured in solution by fluorescence resonance energy transfer, Nucleic Acids Res. 27, 4619-4625.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4619-4625
    • Lorenz, M.1    Hillisch, A.2    Goodman, S.D.3    Diekmann, S.4
  • 28
    • 0035805499 scopus 로고    scopus 로고
    • DNA bends in TATA-binding protein-TATA complexes in solution are DNA sequence-dependent
    • Wu, J., Parkhurst, K. M., Powell, R. M., Brenowitz, M., and Parkhurst, L. J. (2001) DNA bends in TATA-binding protein-TATA complexes in solution are DNA sequence-dependent, J. Biol. Chem. 276, 14614-14622.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14614-14622
    • Wu, J.1    Parkhurst, K.M.2    Powell, R.M.3    Brenowitz, M.4    Parkhurst, L.J.5
  • 29
    • 0041375245 scopus 로고    scopus 로고
    • Functionality versus strength-Has functional selection taken place in the case of the ecdysteroid receptor response element?
    • Grad, I., Kochman, M., and Ożyhar, A. (2002) Functionality versus strength-Has functional selection taken place in the case of the ecdysteroid receptor response element?, Acta Biochim. Pol. 49, 747-756.
    • (2002) Acta Biochim. Pol. , vol.49 , pp. 747-756
    • Grad, I.1    Kochman, M.2    Ozyhar, A.3
  • 31
    • 0028970437 scopus 로고
    • A non-radioactive automated protocol to study protein-DNA interactions by DNase I footprinting
    • Mischati, C., Feriotto, G., Bianchi, N., and Gambari, R. (1995) A non-radioactive automated protocol to study protein-DNA interactions by DNase I footprinting, Int. J. Oncol. 6, 153-156.
    • (1995) Int. J. Oncol. , vol.6 , pp. 153-156
    • Mischati, C.1    Feriotto, G.2    Bianchi, N.3    Gambari, R.4
  • 32
    • 0038382863 scopus 로고    scopus 로고
    • The dynamic nature of the four-way junction of the hepatitis C virus IRES
    • Melcher, S. E., Wilson, T. J., and Lilley, D. M. (2003) The dynamic nature of the four-way junction of the hepatitis C virus IRES, RNA 9, 809-820.
    • (2003) RNA , vol.9 , pp. 809-820
    • Melcher, S.E.1    Wilson, T.J.2    Lilley, D.M.3
  • 33
    • 0021268779 scopus 로고
    • The locus of sequence-directed and protein-induced DNA bending
    • Wu, H. M., and Crothers, D. M. (1984) The locus of sequence-directed and protein-induced DNA bending, Nature 308, 509-513.
    • (1984) Nature , vol.308 , pp. 509-513
    • Wu, H.M.1    Crothers, D.M.2
  • 34
    • 0027250755 scopus 로고
    • Mutational analysis of the interaction between ecdysteroid receptor and its response element
    • Ożyhar, A., and Pongs, O. (1993) Mutational analysis of the interaction between ecdysteroid receptor and its response element, J. Steroid Biochem. Mol. Biol. 46, 135-145.
    • (1993) J. Steroid Biochem. Mol. Biol. , vol.46 , pp. 135-145
    • Ozyhar, A.1    Pongs, O.2
  • 35
    • 0242389799 scopus 로고    scopus 로고
    • Structure of the heterodimeric ecdysone receptor DNA-binding complex
    • Devarakonda, S., Harp, J. M., Kim, Y., Ożyhar, A., and Rastinejad, F. (2003) Structure of the heterodimeric ecdysone receptor DNA-binding complex, EMBO J. 22, 5827-5840.
    • (2003) EMBO J. , vol.22 , pp. 5827-5840
    • Devarakonda, S.1    Harp, J.M.2    Kim, Y.3    Ozyhar, A.4    Rastinejad, F.5
  • 36
    • 0242396923 scopus 로고    scopus 로고
    • 3DNA: A software package for the analysis, rebuilding and visualization of three-dimensional nucleic acid structures
    • Lu, X. J., and Olson, W. K. (2003) 3DNA: a software package for the analysis, rebuilding and visualization of three-dimensional nucleic acid structures, Nucleic Acids Res. 31, 5108-5121.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5108-5121
    • Lu, X.J.1    Olson, W.K.2
  • 37
    • 0034682870 scopus 로고    scopus 로고
    • A-Tract bending: Insights into experimental structures by computational models
    • Strahs, D., and Schlick, T. (2000) A-Tract bending: insights into experimental structures by computational models, J. Mol. Biol 301, 643-663.
    • (2000) J. Mol. Biol , vol.301 , pp. 643-663
    • Strahs, D.1    Schlick, T.2
  • 38
    • 4944226045 scopus 로고    scopus 로고
    • DNA-binding domain of GCN4 induces bending of both the ATF/ CREB and AP-1 binding sites of DNA
    • Dragan, A. I., Liu, Y., Makeyeva, E. N., and Privalov, P. L. (2004) DNA-binding domain of GCN4 induces bending of both the ATF/ CREB and AP-1 binding sites of DNA, Nucleic Acids Res. 32, 5192-5197.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5192-5197
    • Dragan, A.I.1    Liu, Y.2    Makeyeva, E.N.3    Privalov, P.L.4
  • 39
    • 0032749078 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins: Re-assessing the protein structure-function paradigm
    • Wright, P. E., and Dyson, H. J. (1999) Intrinsically unstructured proteins: re-assessing the protein structure-function paradigm, J. Mol. Biol. 293, 321-331.
    • (1999) J. Mol. Biol. , vol.293 , pp. 321-331
    • Wright, P.E.1    Dyson, H.J.2
  • 40
    • 0042819915 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins evolve by repeat expansion
    • Tompa, P. (2003) Intrinsically unstructured proteins evolve by repeat expansion, BioEssays 25, 847-855.
    • (2003) BioEssays , vol.25 , pp. 847-855
    • Tompa, P.1
  • 41
    • 20444376186 scopus 로고    scopus 로고
    • The interplay between structure and function in intrinsically unstructured proteins
    • Tompa, P. (2005) The interplay between structure and function in intrinsically unstructured proteins, FEBS Lett. 579, 3346-3354.
    • (2005) FEBS Lett. , vol.579 , pp. 3346-3354
    • Tompa, P.1
  • 43
    • 0042121115 scopus 로고    scopus 로고
    • DNA analysis servers: Plot.it, bend.it, model.it and IS
    • Vlahovicek, K., Kajan, L., and Pongor, S. (2003) DNA analysis servers: plot.it, bend.it, model.it and IS, Nucleic Acids Res. 31, 3686-3687.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3686-3687
    • Vlahovicek, K.1    Kajan, L.2    Pongor, S.3


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