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Volumn 78, Issue 5, 2000, Pages 2543-2559

Structural changes induced by binding of the high-mobility group I protein to a mouse satellite DNA sequence

Author keywords

[No Author keywords available]

Indexed keywords

DNA; HIGH MOBILITY GROUP PROTEIN;

EID: 0034121423     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(00)76799-3     Document Type: Article
Times cited : (23)

References (76)
  • 1
    • 0032443442 scopus 로고    scopus 로고
    • Three distinct sub-nuclear populations of HMG-I protein of different properties revealed by co-localization image analysis
    • Amirand, C., A. Viari, J. P. Ballini, H. Rezaei, N. Beaujean, D. Jullien, E. Käs, and P. Debey. 1998. Three distinct sub-nuclear populations of HMG-I protein of different properties revealed by co-localization image analysis. J. Cell Sci. 111:3551-3561.
    • (1998) J. Cell Sci. , vol.111 , pp. 3551-3561
    • Amirand, C.1    Viari, A.2    Ballini, J.P.3    Rezaei, H.4    Beaujean, N.5    Jullien, D.6    Käs, E.7    Debey, P.8
  • 2
    • 0032190230 scopus 로고    scopus 로고
    • AT-hook motifs identified in a wide variety of DNA-binding proteins
    • Aravind, L., and D. Landsman. 1998. AT-hook motifs identified in a wide variety of DNA-binding proteins. Nucleic Acids Res. 26:4413-4421.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4413-4421
    • Aravind, L.1    Landsman, D.2
  • 6
    • 0031830815 scopus 로고    scopus 로고
    • Minor groove-binding architectural proteins: Structure, function, and DNA recognition
    • Bewley, C. A., A. M. Gronenbom, and G. M. Clore. 1998. Minor groove-binding architectural proteins: structure, function, and DNA recognition. Annu. Rev. Biophys. Biomol. Struct. 27:105-131.
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 105-131
    • Bewley, C.A.1    Gronenbom, A.M.2    Clore, G.M.3
  • 7
    • 0024584528 scopus 로고
    • Specific recognition of cruciform DNA by nuclear protein HMG1
    • Bianchi, M. E., M. Beltrame, and G. Paonessa. 1989. Specific recognition of cruciform DNA by nuclear protein HMG1. Science. 243:1056-1059.
    • (1989) Science , vol.243 , pp. 1056-1059
    • Bianchi, M.E.1    Beltrame, M.2    Paonessa, G.3
  • 8
    • 0032915869 scopus 로고    scopus 로고
    • Specific binding of high-mobility group i (HMGI) protein and histone H1 upstream of the AT-rich region of the murine beta interferon promoter: HMGI protein acts as a potential antirepressor of the promoter
    • Bonnefoy, E., M. T. Bandu, and J. Doly. 1999. Specific binding of high-mobility group I (HMGI) protein and histone H1 upstream of the AT-rich region of the murine beta interferon promoter: HMGI protein acts as a potential antirepressor of the promoter. Mol. Cell. Biol. 19:2803-2816.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2803-2816
    • Bonnefoy, E.1    Bandu, M.T.2    Doly, J.3
  • 9
    • 0030358586 scopus 로고    scopus 로고
    • High-mobility-group chromosomal proteins: Architectural components that facilitate chromatin function
    • Bustin, M., and R. Reeves. 1996. High-mobility-group chromosomal proteins: architectural components that facilitate chromatin function. Prog. Nucleic Acids Res. 54:35-100.
    • (1996) Prog. Nucleic Acids Res. , vol.54 , pp. 35-100
    • Bustin, M.1    Reeves, R.2
  • 10
    • 0025941474 scopus 로고
    • Identification of sequence elements contributing to the intrinsic curvature of the mouse satellite DNA repeat
    • Carrera, P., A. Martinez-Balbas, and F. Azorin. 1991. Identification of sequence elements contributing to the intrinsic curvature of the mouse satellite DNA repeat. Nucleic Acids Res. 19:5639-5644.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5639-5644
    • Carrera, P.1    Martinez-Balbas, A.2    Azorin, F.3
  • 13
    • 0027394243 scopus 로고
    • Observing the helical geometry of double-stranded DNA in solution by fluorescence resonance energy transfer
    • Clegg, R. M., A. I. H. Murchie, A. Zechel, and D. M. J. Lilley. 1993. Observing the helical geometry of double-stranded DNA in solution by fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. USA. 90:2994-2998.
    • (1993) Proc. Natl. Acad. Sci. USA. , vol.90 , pp. 2994-2998
    • Clegg, R.M.1    Murchie, A.I.H.2    Zechel, A.3    Lilley, D.M.J.4
  • 14
    • 0027296741 scopus 로고
    • Mechanisms of transcriptional synergism between distinct virus-inducible enhancer elements
    • Du, W., D. Thanos, and T. Maniatis. 1993. Mechanisms of transcriptional synergism between distinct virus-inducible enhancer elements. Cell. 74:887-898.
    • (1993) Cell , vol.74 , pp. 887-898
    • Du, W.1    Thanos, D.2    Maniatis, T.3
  • 15
    • 0029398735 scopus 로고
    • Nucleic acid hybridization accompanied with excimer formation from two pyrene-labeled probes
    • Ebata, K., M. Masuko, H. Ohtani, and M. Kashiwasake-Jibu. 1995. Nucleic acid hybridization accompanied with excimer formation from two pyrene-labeled probes. Photochem. Photobiol. 62:836-839.
    • (1995) Photochem. Photobiol. , vol.62 , pp. 836-839
    • Ebata, K.1    Masuko, M.2    Ohtani, H.3    Kashiwasake-Jibu, M.4
  • 16
    • 0027751968 scopus 로고
    • Conformational distributions of a four-way junction revealed by time-resolved fluorescence resonance energy transfer
    • Eis, P. S., and D. P. Millar. 1993. Conformational distributions of a four-way junction revealed by time-resolved fluorescence resonance energy transfer. Biochemistry. 32:13852-13860.
    • (1993) Biochemistry , vol.32 , pp. 13852-13860
    • Eis, P.S.1    Millar, D.P.2
  • 17
    • 0025362431 scopus 로고
    • Repeat peptide motifs which contain β-turns and modulate DNA condensation in chromatin
    • Erard, M., F. Lakhdar-Ghazal, and F. Amalric. 1990. Repeat peptide motifs which contain β-turns and modulate DNA condensation in chromatin. Eur. J. Biochem. 191:19-26.
    • (1990) Eur. J. Biochem. , vol.191 , pp. 19-26
    • Erard, M.1    Lakhdar-Ghazal, F.2    Amalric, F.3
  • 19
    • 0029619641 scopus 로고
    • Reversal of intrinsic DNA bends in the IFNβ enhancer by transcription factors and the architectural protein HMG I(Y)
    • Falvo, J. V., D. Thanos, and T. Maniatis. 1995. Reversal of intrinsic DNA bends in the IFNβ enhancer by transcription factors and the architectural protein HMG I(Y). Cell. 83:1101-1111.
    • (1995) Cell , vol.83 , pp. 1101-1111
    • Falvo, J.V.1    Thanos, D.2    Maniatis, T.3
  • 20
    • 0031004162 scopus 로고    scopus 로고
    • HIV-1 cDNA integration: Requirement of HMGI(Y) protein for function of preintegration complexes in vitro
    • Farnet, C. M., and F. D. Bushman. 1997. HIV-1 cDNA integration: requirement of HMGI(Y) protein for function of preintegration complexes in vitro. Cell. 88:483-492.
    • (1997) Cell , vol.88 , pp. 483-492
    • Farnet, C.M.1    Bushman, F.D.2
  • 21
    • 0032493632 scopus 로고    scopus 로고
    • Protein footprinting reveals specific binding modes of a high mobility group protein i to DNAs of different conformation
    • Franck, O., R. Schwanbeck, and J. R. Wisniewski. 1998. Protein footprinting reveals specific binding modes of a high mobility group protein I to DNAs of different conformation. J. Biol. Chem. 273:20015-20020.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20015-20020
    • Franck, O.1    Schwanbeck, R.2    Wisniewski, J.R.3
  • 22
    • 0029813613 scopus 로고    scopus 로고
    • Involvement of a high-mobility-group protein in the transcriptional activity of herpes simplex virus latency-active promoter 2
    • French, S. W., M. C. Schmidt, and J. C. Glorioso. 1996. Involvement of a high-mobility-group protein in the transcriptional activity of herpes simplex virus latency-active promoter 2. Mol. Cell. Biol. 16:5393-5399.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5393-5399
    • French, S.W.1    Schmidt, M.C.2    Glorioso, J.C.3
  • 23
    • 0028303273 scopus 로고
    • Short peptide fragments derived from HMG-I/Y proteins bind specifically to the minor groove of DNA
    • Geierstanger, B. H., B. F. Volkman, W. Kremer, and D. E. Wemmer. 1994. Short peptide fragments derived from HMG-I/Y proteins bind specifically to the minor groove of DNA. Biochemistry. 33:5347-5355.
    • (1994) Biochemistry , vol.33 , pp. 5347-5355
    • Geierstanger, B.H.1    Volkman, B.F.2    Kremer, W.3    Wemmer, D.E.4
  • 24
    • 0032055120 scopus 로고    scopus 로고
    • In vivo analysis of scaffold-associated regions in Drosophila: A synthetic high-affinity SAR binding protein suppresses position effect variegation
    • Girard, F., B. Bello, U. K. Laemmli, and W. J. Gehring. 1998. In vivo analysis of scaffold-associated regions in Drosophila: a synthetic high-affinity SAR binding protein suppresses position effect variegation. EMBO J. 17:2079-2085.
    • (1998) EMBO J. , vol.17 , pp. 2079-2085
    • Girard, F.1    Bello, B.2    Laemmli, U.K.3    Gehring, W.J.4
  • 25
    • 0028072693 scopus 로고
    • Kinking of DNA and RNA helices by bulged nucleotides observed by fluorescence resonance energy transfer
    • Gohlke, C., A. I. H. Murchie, D. M. J. Lilley, and R. M. Clegg. 1994. Kinking of DNA and RNA helices by bulged nucleotides observed by fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. USA. 91:11660-11664.
    • (1994) Proc. Natl. Acad. Sci. USA. , vol.91 , pp. 11660-11664
    • Gohlke, C.1    Murchie, A.I.H.2    Lilley, D.M.J.3    Clegg, R.M.4
  • 26
    • 0017887055 scopus 로고
    • DNA condensation with polyamines. I. Spectroscopic studies
    • Gosule, L. C., and J. A. Schellman. 1978. DNA condensation with polyamines. I. Spectroscopic studies. J. Mol. Biol. 121:311-326.
    • (1978) J. Mol. Biol. , vol.121 , pp. 311-326
    • Gosule, L.C.1    Schellman, J.A.2
  • 27
    • 0028197368 scopus 로고
    • HMG domain proteins: Architectural elements in the assembly of nucleoprotein structures
    • Grosschedl, R., K. Giese, and J. Pagel. 1994. HMG domain proteins: architectural elements in the assembly of nucleoprotein structures. Trends Genet. 10:94-99.
    • (1994) Trends Genet. , vol.10 , pp. 94-99
    • Grosschedl, R.1    Giese, K.2    Pagel, J.3
  • 28
    • 0030877452 scopus 로고    scopus 로고
    • Conformational changes of DNA induced by the binding of Chironomus high mobility group protein 1a (cHMGla)
    • Heyduk, E., T. Heyduk, P. Claus, and J. R. Wisniewski. 1997. Conformational changes of DNA induced by the binding of Chironomus high mobility group protein 1a (cHMGla). J. Biol. Chem. 272:19763-19770.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19763-19770
    • Heyduk, E.1    Heyduk, T.2    Claus, P.3    Wisniewski, J.R.4
  • 29
    • 0030835937 scopus 로고    scopus 로고
    • Competition between HMG-I(Y), HMG-1 and histone HI on four-way junction DNA
    • Hill, D. A., and R. Reeves. 1997. Competition between HMG-I(Y), HMG-1 and histone HI on four-way junction DNA. Nucleic Acids Res. 25:3523-3531.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3523-3531
    • Hill, D.A.1    Reeves, R.2
  • 30
    • 0031453522 scopus 로고    scopus 로고
    • Effects of epidermal growth factor and estrogen on the regulation of the HMG-I/Y gene in human mammary epithelial cell lines
    • Holth, L. T., A. E. Thorlacius, and R. Reeves. 1997. Effects of epidermal growth factor and estrogen on the regulation of the HMG-I/Y gene in human mammary epithelial cell lines. DNA Cell Biol. 16:1299-1309.
    • (1997) DNA Cell Biol. , vol.16 , pp. 1299-1309
    • Holth, L.T.1    Thorlacius, A.E.2    Reeves, R.3
  • 32
    • 33646959383 scopus 로고
    • IUPAC Commission on Photochemistry. 1986. E. P. A. Newsletter. 21-29.
    • (1986) E. P. A. Newsletter , pp. 21-29
  • 33
    • 0029960811 scopus 로고    scopus 로고
    • Determination of DNA helical handedness by fluorescence resonance energy transfer
    • Jares-Erijman, E. A., and T. M. Jovin. 1996. Determination of DNA helical handedness by fluorescence resonance energy transfer. J. Mol. Biol. 257:597-617.
    • (1996) J. Mol. Biol. , vol.257 , pp. 597-617
    • Jares-Erijman, E.A.1    Jovin, T.M.2
  • 34
    • 0028889159 scopus 로고
    • Regulation of cell-type-specific interleukin-2 receptor α-chain gene expression: Potential role of physical interactions between Elf1, HMG-I(Y) and NF-κB family proteins
    • John, S., R. B. Reeves, J. X. Lin, R. Child, J. M. Leiden, C. B. Thomson, and W. J. Leonard. 1995. Regulation of cell-type-specific interleukin-2 receptor α-chain gene expression: potential role of physical interactions between Elf1, HMG-I(Y) and NF-κB family proteins. Mol. Cell. Biol. 15:1786-1796.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1786-1796
    • John, S.1    Reeves, R.B.2    Lin, J.X.3    Child, R.4    Leiden, J.M.5    Thomson, C.B.6    Leonard, W.J.7
  • 35
    • 0029853971 scopus 로고    scopus 로고
    • An IL-2 response element in the human IL-2 receptor α chain promoter is a composite element that binds Stat5, Elf-1, HMG-I(Y) and a GATA family protein
    • John, S., C. M. Robbins, and W. J. Leonard. 1996. An IL-2 response element in the human IL-2 receptor α chain promoter is a composite element that binds Stat5, Elf-1, HMG-I(Y) and a GATA family protein. EMBO J. 15:5627-5635.
    • (1996) EMBO J. , vol.15 , pp. 5627-5635
    • John, S.1    Robbins, C.M.2    Leonard, W.J.3
  • 36
    • 0030463173 scopus 로고    scopus 로고
    • HMGI(Y) interferes with the DNA binding of NF-AT factors and the induction of the interleukin 4 promoter in T cells
    • Kelin-Hessling, S., G. Schneider, A. Heinfling, S. Chuvpilo, and E. Serfling. 1996. HMGI(Y) interferes with the DNA binding of NF-AT factors and the induction of the interleukin 4 promoter in T cells. Proc. Natl. Acad. Sci. USA. 93:15311-15316.
    • (1996) Proc. Natl. Acad. Sci. USA. , vol.93 , pp. 15311-15316
    • Kelin-Hessling, S.1    Schneider, G.2    Heinfling, A.3    Chuvpilo, S.4    Serfling, E.5
  • 37
    • 0032514771 scopus 로고    scopus 로고
    • Trifluoroethanol promotes helix formation by destabilizing backbone exposure: Desolvation rather than native hydrogen bonding defines the kinetic pathway of dimeric coiled coil folding
    • Kentsis, A., and T. R. Sosnick. 1998. Trifluoroethanol promotes helix formation by destabilizing backbone exposure: desolvation rather than native hydrogen bonding defines the kinetic pathway of dimeric coiled coil folding. Biochemistry. 37:4613-14622.
    • (1998) Biochemistry. , vol.37 , pp. 4613-14622
    • Kentsis, A.1    Sosnick, T.R.2
  • 38
    • 0031046649 scopus 로고    scopus 로고
    • Condensation of DNA and chromatin by an SPKK-containing octapeptide repeat motif present in the C-terminus of histone HI
    • Khadake, J., and M. R. S. Rao. 1997. Condensation of DNA and chromatin by an SPKK-containing octapeptide repeat motif present in the C-terminus of histone HI. Biochemistry. 36:1041-1051.
    • (1997) Biochemistry , vol.36 , pp. 1041-1051
    • Khadake, J.1    Rao, M.R.S.2
  • 39
    • 0001313197 scopus 로고
    • 5′-Amino pyrene provides a sensitive, non-perturbing fluorescent probe of RNA secondary and tertiary structure formation
    • Kierzek, R., Y. Li, D. H. Turner, and P. Bevilacqua. 1993. 5′-Amino pyrene provides a sensitive, non-perturbing fluorescent probe of RNA secondary and tertiary structure formation. J. Am. Chem. Soc. 115:4985-4992.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4985-4992
    • Kierzek, R.1    Li, Y.2    Turner, D.H.3    Bevilacqua, P.4
  • 40
    • 0029974293 scopus 로고    scopus 로고
    • Human papillomavirus type 16 E6 protein up-regulates the expression of the high mobility group protein HMG-I(Y) gene in mouse 10T1/2 cells
    • Kinioshita, T., H. Shirasawa, Y. Shino, K. Shimizu, H. Moriya, and B. Simizu. 1996. Human papillomavirus type 16 E6 protein up-regulates the expression of the high mobility group protein HMG-I(Y) gene in mouse 10T1/2 cells. Virus Res. 42:119-125.
    • (1996) Virus Res. , vol.42 , pp. 119-125
    • Kinioshita, T.1    Shirasawa, H.2    Shino, Y.3    Shimizu, K.4    Moriya, H.5    Simizu, B.6
  • 41
    • 0017657874 scopus 로고
    • Pyrene derivatives as fluorescent probes of conformation near the 3′ termini of polyribonucleotides
    • Koenig, P., S. A. Reines, and C. R. Cantor. 1977. Pyrene derivatives as fluorescent probes of conformation near the 3′ termini of polyribonucleotides. Biopolymers. 16:2231-2242.
    • (1977) Biopolymers , vol.16 , pp. 2231-2242
    • Koenig, P.1    Reines, S.A.2    Cantor, C.R.3
  • 42
    • 0024539180 scopus 로고
    • Defining the structure of irregular nucleic acids: Conventions and principles
    • Lavery, R., and H. Sklenar. 1989. Defining the structure of irregular nucleic acids: conventions and principles. J. Biomol. Struct. Dyn. 6:655-667.
    • (1989) J. Biomol. Struct. Dyn. , vol.6 , pp. 655-667
    • Lavery, R.1    Sklenar, H.2
  • 43
  • 44
    • 0029017459 scopus 로고
    • Functional interaction between the POU domain protein Ets-1/Oct6 and the high-mobility-group protein HMG-I/Y
    • Leger, H., E. Sock, K. Renner, F. Grummt, and M. Wegner. 1995. Functional interaction between the POU domain protein Ets-1/Oct6 and the high-mobility-group protein HMG-I/Y. Mol. Cell. Biol. 15:3738-3747.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3738-3747
    • Leger, H.1    Sock, E.2    Renner, K.3    Grummt, F.4    Wegner, M.5
  • 45
    • 0024009983 scopus 로고
    • A conformational study of the sequence specific binding of HMG-I(Y) with the bovine interleukin-2 cDNA
    • Lehn, D. A., T. S. Elton, K. R. Johnson, and R. Reeves. 1988. A conformational study of the sequence specific binding of HMG-I(Y) with the bovine interleukin-2 cDNA. Biochem. Int. 16:963-971.
    • (1988) Biochem. Int. , vol.16 , pp. 963-971
    • Lehn, D.A.1    Elton, T.S.2    Johnson, K.R.3    Reeves, R.4
  • 46
    • 0031936603 scopus 로고    scopus 로고
    • Modulation of activity of Moloney murine leukemia virus preintegration complexes by host factors in vitro
    • Li, L., C. M. Farnet, W. F. Anderson, and F. D. Bushman. 1998. Modulation of activity of Moloney murine leukemia virus preintegration complexes by host factors in vitro. J. Virol. 72:2125-2131.
    • (1998) J. Virol. , vol.72 , pp. 2125-2131
    • Li, L.1    Farnet, C.M.2    Anderson, W.F.3    Bushman, F.D.4
  • 47
    • 0022384476 scopus 로고
    • Reconstitution experiments show that segment-specific histone-DNA interactions are the basis for nucleosome phasing on mouse satellite DNA
    • Linxweiler, W., and W. Hörz. 1985. Reconstitution experiments show that segment-specific histone-DNA interactions are the basis for nucleosome phasing on mouse satellite DNA. Cell. 42:281-290.
    • (1985) Cell , vol.42 , pp. 281-290
    • Linxweiler, W.1    Hörz, W.2
  • 48
    • 0025006448 scopus 로고
    • Binding characteristics of Hoechst 33258 with calf thymus DNA, poly[d(A-T)], and d(CCGGAATTCCGG): Multiple stoichiometries and determination of tight binding with a wide spectrum of site affinities
    • Loontiens, F. G., P. Regenfuss, A. Zechel, L. Dumortier, and R. M. Clegg. 1990. Binding characteristics of Hoechst 33258 with calf thymus DNA, poly[d(A-T)], and d(CCGGAATTCCGG): multiple stoichiometries and determination of tight binding with a wide spectrum of site affinities. Biochemistry. 29:9029-9039.
    • (1990) Biochemistry , vol.29 , pp. 9029-9039
    • Loontiens, F.G.1    Regenfuss, P.2    Zechel, A.3    Dumortier, L.4    Clegg, R.M.5
  • 49
    • 0019322666 scopus 로고
    • Contribution of light scattering to the circular dichroism of deoxyribonucleic acid films, deoxyribonucleic acid-polylysine complexes and deoxyribonucleic acid-particles in ethanolic buffers
    • Maestre, M. F., and C. Reich. 1980. Contribution of light scattering to the circular dichroism of deoxyribonucleic acid films, deoxyribonucleic acid-polylysine complexes and deoxyribonucleic acid-particles in ethanolic buffers. Biochemistry. 19:5214-5223.
    • (1980) Biochemistry , vol.19 , pp. 5214-5223
    • Maestre, M.F.1    Reich, C.2
  • 50
    • 0030011231 scopus 로고    scopus 로고
    • Multivalent DNA-binding properties of the HMG-I proteins
    • Maher, J. F., and D. Nathans. 1996. Multivalent DNA-binding properties of the HMG-I proteins. Proc. Natl. Acad. Sci. USA. 93:6716-6720.
    • (1996) Proc. Natl. Acad. Sci. USA. , vol.93 , pp. 6716-6720
    • Maher, J.F.1    Nathans, D.2
  • 53
    • 0026145797 scopus 로고
    • Fluorescence energy transfer between dimethyldiazaperopyrenium dication and ethidium intercalated in poly d(A-T)
    • Mergny, J. L., A. Slama-Schwok, T. Montenay-Garestier, M. Rougée, and C. Hélène. 1991. Fluorescence energy transfer between dimethyldiazaperopyrenium dication and ethidium intercalated in poly d(A-T). Photochem. Pholobiol. 53:555-558.
    • (1991) Photochem. Pholobiol. , vol.53 , pp. 555-558
    • Mergny, J.L.1    Slama-Schwok, A.2    Montenay-Garestier, T.3    Rougée, M.4    Hélène, C.5
  • 55
    • 0028958590 scopus 로고
    • Changes in superhelicity are introduced into closed circular DNA by binding of high mobility group protein I/Y
    • Nissen, M. S., and R. Reeves. 1995. Changes in superhelicity are introduced into closed circular DNA by binding of high mobility group protein I/Y. J. Biol. Chem. 270:4355-4360.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4355-4360
    • Nissen, M.S.1    Reeves, R.2
  • 57
    • 0023664977 scopus 로고
    • Curvature of mouse satellite DNA and condensation of heterochromatin
    • Radie, M. Z., K. Lundgren, and B. A. Hamkal. 1987. Curvature of mouse satellite DNA and condensation of heterochromatin. Cell. 50:1101-1108.
    • (1987) Cell , vol.50 , pp. 1101-1108
    • Radie, M.Z.1    Lundgren, K.2    Hamkal, B.A.3
  • 58
    • 0026662836 scopus 로고
    • Hoechst 33258, distamycin A, and high mobility group protein i (HMG-I) compete for binding to mouse satellite DNA
    • Radie, M. Z., M. Saghbini, T. S. Elton, R. Reeves, and B. A. Hamkalo. 1992. Hoechst 33258, distamycin A, and high mobility group protein I (HMG-I) compete for binding to mouse satellite DNA. Chromosoma. 101:602-608.
    • (1992) Chromosoma , vol.101 , pp. 602-608
    • Radie, M.Z.1    Saghbini, M.2    Elton, T.S.3    Reeves, R.4    Hamkalo, B.A.5
  • 59
    • 0032032120 scopus 로고    scopus 로고
    • Conformational interconversions in peptide β-turns: Discrimination between enantiomeric conformations by chiral perturbation
    • Raghothama, S., M. Chaddha, S. Banumathi, K. Ravikumar, D. Velmurugan, and P. Balaram. 1998. Conformational interconversions in peptide β-turns: discrimination between enantiomeric conformations by chiral perturbation. Biopolymers. 45:191-202.
    • (1998) Biopolymers , vol.45 , pp. 191-202
    • Raghothama, S.1    Chaddha, M.2    Banumathi, S.3    Ravikumar, K.4    Velmurugan, D.5    Balaram, P.6
  • 60
    • 0025196283 scopus 로고
    • The A-T-DNA binding domain of mammalian high mobility group i chromosomal proteins
    • Reeves, R., and M. S. Nissen. 1990. The A-T-DNA binding domain of mammalian high mobility group I chromosomal proteins. J. Biol. Chem. 265:8573-8582.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8573-8582
    • Reeves, R.1    Nissen, M.S.2
  • 61
    • 0029915384 scopus 로고    scopus 로고
    • Substrate structure influences binding of the non-histone protein HMG-I(Y) to free and nucleosomal DNA
    • Reeves, R., and A. P. Wolffe. 1996. Substrate structure influences binding of the non-histone protein HMG-I(Y) to free and nucleosomal DNA. Biochemistry. 35:5063-5074.
    • (1996) Biochemistry , vol.35 , pp. 5063-5074
    • Reeves, R.1    Wolffe, A.P.2
  • 62
    • 0026697386 scopus 로고
    • Alternating d(G-A) sequences form a parallel-stranded DNA homoduplex
    • Rippe, K., V. Fritsch, E. Westhof, and T. M. Jovin. 1992. Alternating d(G-A) sequences form a parallel-stranded DNA homoduplex. EMBO J. 11:3777-3786.
    • (1992) EMBO J. , vol.11 , pp. 3777-3786
    • Rippe, K.1    Fritsch, V.2    Westhof, E.3    Jovin, T.M.4
  • 63
    • 0344688469 scopus 로고
    • A mammalian high mobility group protein recognizes any stretch of six at base pairs in duplex DNA
    • Salomon, M. J., J. F. Strauss, and A. Varshavsky. 1986. A mammalian high mobility group protein recognizes any stretch of six AT base pairs in duplex DNA. Proc. Natl. Acad. Sci. USA. 83:1276-1280.
    • (1986) Proc. Natl. Acad. Sci. USA. , vol.83 , pp. 1276-1280
    • Salomon, M.J.1    Strauss, J.F.2    Varshavsky, A.3
  • 64
    • 34247489528 scopus 로고
    • Absorption and fluorescence properties of fluorescein
    • Sjöback, R., J. Nygren, and M. Kubista. 1995. Absorption and fluorescence properties of fluorescein. Spectrochim. Acta A. 51:7-21.
    • (1995) Spectrochim. Acta A. , vol.51 , pp. 7-21
    • Sjöback, R.1    Nygren, J.2    Kubista, M.3
  • 65
    • 23444450909 scopus 로고
    • Coupling of local folding to site-specific binding of proteins to DNA
    • Spolar, R. S., and M. T. Record. 1994. Coupling of local folding to site-specific binding of proteins to DNA. Science. 263:777-784.
    • (1994) Science , vol.263 , pp. 777-784
    • Spolar, R.S.1    Record, M.T.2
  • 66
    • 0021708253 scopus 로고
    • A protein binds to a satellite DNA repeat at three specific sites that would be brought into mutual proximity by DNA folding in the nucleosome
    • Strauss, F., and A. Varshavsky. 1984. A protein binds to a satellite DNA repeat at three specific sites that would be brought into mutual proximity by DNA folding in the nucleosome. Cell. 37:889-901.
    • (1984) Cell , vol.37 , pp. 889-901
    • Strauss, F.1    Varshavsky, A.2
  • 67
    • 0029561761 scopus 로고
    • SAR are cis DNA elements of chromosome dynamics: Synthesis of a SAR repressor protein
    • Strick, R., and U. K. Laemmli. 1995. SAR are cis DNA elements of chromosome dynamics: synthesis of a SAR repressor protein. Cell. 83:1137-1148.
    • (1995) Cell , vol.83 , pp. 1137-1148
    • Strick, R.1    Laemmli, U.K.2
  • 68
    • 0032562599 scopus 로고    scopus 로고
    • DNA bending by the chromosomal protein HMG1 and its high mobility group box domains. Effect of flanking sequences
    • Stros, M. 1998. DNA bending by the chromosomal protein HMG1 and its high mobility group box domains. Effect of flanking sequences. J. Biol. Chem. 273:10355-10361.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10355-10361
    • Stros, M.1
  • 69
    • 0029048796 scopus 로고
    • Structural variety of arginine-rich RNA-binding peptides
    • Tan, R., and A. D. Frankel. 1995. Structural variety of arginine-rich RNA-binding peptides. Proc. Natl. Acad. Sci. USA. 92:5282-5286.
    • (1995) Proc. Natl. Acad. Sci. USA. , vol.92 , pp. 5282-5286
    • Tan, R.1    Frankel, A.D.2
  • 70
    • 0029617947 scopus 로고
    • Virus induction of human IFNβ gene expression requires the assembly of an enhanceosome
    • Thanos, D., and T. Maniatis. 1995. Virus induction of human IFNβ gene expression requires the assembly of an enhanceosome. Cell. 83:1091-1100.
    • (1995) Cell , vol.83 , pp. 1091-1100
    • Thanos, D.1    Maniatis, T.2
  • 71
    • 0041829746 scopus 로고    scopus 로고
    • DNA curvature in solution measured by fluorescence resonance energy transfer
    • Toth, K., V. Sauermann, and J. Langovski. 1998. DNA curvature in solution measured by fluorescence resonance energy transfer. Biochemistry. 37:8173-8179.
    • (1998) Biochemistry , vol.37 , pp. 8173-8179
    • Toth, K.1    Sauermann, V.2    Langovski, J.3
  • 72
    • 0025113022 scopus 로고
    • β-Turns and their distortions: A proposed new nomenclature
    • Wilmot, C. M., and J. M. Thornton. 1990. β-Turns and their distortions: a proposed new nomenclature. Protein Eng. 3:479-493.
    • (1990) Protein Eng. , vol.3 , pp. 479-493
    • Wilmot, C.M.1    Thornton, J.M.2
  • 73
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J. T., C. S. Wu, and H. M. Martinez. 1986. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130:208-269.
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, J.T.1    Wu, C.S.2    Martinez, H.M.3
  • 74
    • 0030998258 scopus 로고    scopus 로고
    • Intra- And intermolecular cooperative binding of high mobility group protein I(Y) to the beta-interferon promoter
    • Yie, J., S. Liang, M. Merika, and D. Thanos. 1997. Intra- and intermolecular cooperative binding of high mobility group protein I(Y) to the beta-interferon promoter. Mol. Cell. Biol. 17:3649-3662.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3649-3662
    • Yie, J.1    Liang, S.2    Merika, M.3    Thanos, D.4
  • 75
    • 0033152497 scopus 로고    scopus 로고
    • The role of HMG I(Y) in the assembly and function of the IFN-β enhanceosome
    • Yie, J., M. Merika, N. Munshi, G. Chen, and D. Thanos. 1999. The role of HMG I(Y) in the assembly and function of the IFN-β enhanceosome. EMBO J. 18:3074-3089.
    • (1999) EMBO J. , vol.18 , pp. 3074-3089
    • Yie, J.1    Merika, M.2    Munshi, N.3    Chen, G.4    Thanos, D.5
  • 76
    • 0027306750 scopus 로고
    • SAR-dependent mobilization of histone H1 by HMG-I/Y in vitro: HMG-I/Y is enriched in H1-depleted chromatin
    • Zhao, K. E., E. Käs, E. Gonzalez, and U. K. Laemmli. 1993. SAR-dependent mobilization of histone H1 by HMG-I/Y in vitro: HMG-I/Y is enriched in H1-depleted chromatin. EMBO J. 12:3237-3247.
    • (1993) EMBO J. , vol.12 , pp. 3237-3247
    • Zhao, K.E.1    Käs, E.2    Gonzalez, E.3    Laemmli, U.K.4


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