메뉴 건너뛰기




Volumn 8, Issue 4, 2000, Pages

Nonsequence-specific DNA recognition: A structural perspective

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CURVED DNA; DNA FRAGMENT; HIGH MOBILITY GROUP PROTEIN; HISTONE;

EID: 0034655961     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00126-X     Document Type: Review
Times cited : (123)

References (39)
  • 1
    • 0000127073 scopus 로고
    • Sequence-specific recognition of double helical nucleic acids by proteins
    • Seeman N.C., Rosenberg J.M., Rich A. Sequence-specific recognition of double helical nucleic acids by proteins. Proc. Natl Acad. Sci. USA. 73:1976;804-805.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 804-805
    • Seeman, N.C.1    Rosenberg, J.M.2    Rich, A.3
  • 2
    • 0026682657 scopus 로고
    • Transcription factors: Structural families and principles of DNA recognition
    • Pabo C., Sauer R. Transcription factors: structural families and principles of DNA recognition. Annu. Rev. Biochem. 61:1992;1053-1095.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 1053-1095
    • Pabo, C.1    Sauer, R.2
  • 3
    • 0031830815 scopus 로고    scopus 로고
    • Minor groove-binding architectural proteins: Structure, function, and DNA recognition
    • Bewley C., Gronenborn A.M., Clore M.G. Minor groove-binding architectural proteins: structure, function, and DNA recognition. Annu. Rev. Biophys. Biomol. Struct. 27:1998;105-131.
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 105-131
    • Bewley, C.1    Gronenborn, A.M.2    Clore, M.G.3
  • 4
    • 0028210087 scopus 로고
    • Protein-DNA recognition: New perspectives and underlying themes
    • von Hippel P.H. Protein-DNA recognition: new perspectives and underlying themes. Science. 263:1994;769-770.
    • (1994) Science , vol.263 , pp. 769-770
    • Von Hippel, P.H.1
  • 5
    • 0033529565 scopus 로고    scopus 로고
    • Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome
    • Kornberg R.D. Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome. Cell. 98:1999;285-295.
    • (1999) Cell , vol.98 , pp. 285-295
    • Kornberg, R.D.1
  • 6
    • 0030358586 scopus 로고    scopus 로고
    • High-mobility-group chromosomal proteins: Architectural components that facilitate chromatin function
    • Bustin M., Reeves R. High-mobility-group chromosomal proteins: architectural components that facilitate chromatin function. Prog. Nuc. Acid Res. Mol. Biol. 54:1996;35-100.
    • (1996) Prog. Nuc. Acid Res. Mol. Biol. , vol.54 , pp. 35-100
    • Bustin, M.1    Reeves, R.2
  • 7
    • 0033485515 scopus 로고    scopus 로고
    • The structure of a chromosomal high mobility group protein-DNA complex reveals sequence-neutral mechanisms important for non-sequence-specific DNA recognition
    • Murphy F.V. IV, Sweet R.M., Churchill M.E.A. The structure of a chromosomal high mobility group protein-DNA complex reveals sequence-neutral mechanisms important for non-sequence-specific DNA recognition. EMBO J. 18:1999;6610-6618.
    • (1999) EMBO J. , vol.18 , pp. 6610-6618
    • Murphy F.V. IV1    Sweet, R.M.2    Churchill, M.E.A.3
  • 9
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 Å resolution
    • Luger K., Mader A.W., Richmond R.K., Sargent D.F., Richmond T.J. Crystal structure of the nucleosome core particle at 2.8 Å resolution. Nature. 389:1997;251-260.
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 10
    • 0029070956 scopus 로고
    • The HMG-1 box protein family: Classification and functional relationships
    • Baxevanis A.D., Landsman D. The HMG-1 box protein family: classification and functional relationships. Nucleic Acids Res. 23:1995;1604-1613.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1604-1613
    • Baxevanis, A.D.1    Landsman, D.2
  • 11
    • 0026264203 scopus 로고
    • DNA-binding properties of the HMG-domain of the lymphoid-specific transcriptional regulator LEF-1
    • Giese K., Amsterdam A., Grosschedl R. DNA-binding properties of the HMG-domain of the lymphoid-specific transcriptional regulator LEF-1. Genes Dev. 5:1991;2567-2578.
    • (1991) Genes Dev. , vol.5 , pp. 2567-2578
    • Giese, K.1    Amsterdam, A.2    Grosschedl, R.3
  • 12
    • 0030064348 scopus 로고    scopus 로고
    • Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin
    • Nightingale K., Dimitrov S., Reeves R., Wolffe A. Evidence for a shared structural role for HMG1 and linker histones B4 and H1 in organizing chromatin. EMBO J. 15:1996;548-561.
    • (1996) EMBO J. , vol.15 , pp. 548-561
    • Nightingale, K.1    Dimitrov, S.2    Reeves, R.3    Wolffe, A.4
  • 13
    • 0032814140 scopus 로고    scopus 로고
    • Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins
    • Bustin M. Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins. Mol. Cell Biol. 19:1999;5237-5246.
    • (1999) Mol. Cell Biol. , vol.19 , pp. 5237-5246
    • Bustin, M.1
  • 16
    • 0028773902 scopus 로고
    • The solution structure and dynamics of the DNA-binding domain of HMG-D from Drosophila Melanogaster
    • Jones D.N.M., Neuhaus D.et al. The solution structure and dynamics of the DNA-binding domain of HMG-D from Drosophila Melanogaster. Structure. 2:1994;609-627.
    • (1994) Structure , vol.2 , pp. 609-627
    • Jones, D.N.M.1    Neuhaus, D.2
  • 17
    • 0029131298 scopus 로고
    • Structural basis for DNA bending by the architectural transcription factor LEF-1
    • Love J.J., Li X., Case D.A., Giese K., Grosschedl R., Wright P.E. Structural basis for DNA bending by the architectural transcription factor LEF-1. Nature. 376:1995;791-795.
    • (1995) Nature , vol.376 , pp. 791-795
    • Love, J.J.1    Li, X.2    Case, D.A.3    Giese, K.4    Grosschedl, R.5    Wright, P.E.6
  • 18
    • 0029075461 scopus 로고
    • Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex
    • Werner M.H., Huth J.R., Gronenborn A.M., Clore G.M. Molecular basis of human 46X,Y sex reversal revealed from the three-dimensional solution structure of the human SRY-DNA complex. Cell. 81:1995;705-714.
    • (1995) Cell , vol.81 , pp. 705-714
    • Werner, M.H.1    Huth, J.R.2    Gronenborn, A.M.3    Clore, G.M.4
  • 19
    • 0033578010 scopus 로고    scopus 로고
    • Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins
    • Ohndorf U-M., Rould M.A., He Q., Pabo C.O., Lippard S.J. Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins. Nature. 399:1999;708-712.
    • (1999) Nature , vol.399 , pp. 708-712
    • Ohndorf, U.-M.1    Rould, M.A.2    He, Q.3    Pabo, C.O.4    Lippard, S.J.5
  • 20
    • 0028197368 scopus 로고
    • HMG domain proteins - architectural elements in the assembly of nucleoprotein structures
    • Grosschedl R., Giese K., Pagel J. HMG domain proteins - architectural elements in the assembly of nucleoprotein structures. Trends Genet. 10:1994;94-100.
    • (1994) Trends Genet. , vol.10 , pp. 94-100
    • Grosschedl, R.1    Giese, K.2    Pagel, J.3
  • 21
    • 0030471480 scopus 로고    scopus 로고
    • Crystal structure of the anticancer drug cisplatin bound to duplex DNA
    • Takahara P.M., Frederick C.A., Lippard S.J. Crystal structure of the anticancer drug cisplatin bound to duplex DNA. J. Am. Chem. Soc. 118:1996;12309-12321.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 12309-12321
    • Takahara, P.M.1    Frederick, C.A.2    Lippard, S.J.3
  • 22
    • 0033522480 scopus 로고    scopus 로고
    • Solution structure of the HMG protein NHP6A and its interaction with DNA reveals the structural determinants for non-sequence-specific binding
    • Allain F.H-T., Feigon J.et al. Solution structure of the HMG protein NHP6A and its interaction with DNA reveals the structural determinants for non-sequence-specific binding. EMBO J. 18:1999;2563-2579.
    • (1999) EMBO J. , vol.18 , pp. 2563-2579
    • Allain, F.H.-T.1    Feigon, J.2
  • 23
    • 0032006926 scopus 로고    scopus 로고
    • Structure prediction of a complex between the chromosomal protein HMG-D and DNA
    • Balaeff A., Churchill M.E.A., Schulten K. Structure prediction of a complex between the chromosomal protein HMG-D and DNA. Proteins. 30:1998;113-135.
    • (1998) Proteins , vol.30 , pp. 113-135
    • Balaeff, A.1    Churchill, M.E.A.2    Schulten, K.3
  • 24
    • 0033584886 scopus 로고    scopus 로고
    • The recognition of distorted DNA structures by HMG-D: A footprinting and molecular modeling study
    • Payet D., Hillisch A., Lowe N., Diekmann S., Travers A. The recognition of distorted DNA structures by HMG-D: a footprinting and molecular modeling study. J. Mol. Biol. 294:1999;79-91.
    • (1999) J. Mol. Biol. , vol.294 , pp. 79-91
    • Payet, D.1    Hillisch, A.2    Lowe, N.3    Diekmann, S.4    Travers, A.5
  • 25
    • 0026569275 scopus 로고
    • Specific binding of chromosomal protein HMG-1 to DNA damaged by the anticancer drug cisplatin
    • Pil P., Lippard S.J. Specific binding of chromosomal protein HMG-1 to DNA damaged by the anticancer drug cisplatin. Science. 256:1992;234-237.
    • (1992) Science , vol.256 , pp. 234-237
    • Pil, P.1    Lippard, S.J.2
  • 26
    • 0030984494 scopus 로고    scopus 로고
    • DNA sequence context and protein composition modulate HMG-domain protein recognition of cisplatin-modified DNA
    • Dunham S.U., Lippard S.J. DNA sequence context and protein composition modulate HMG-domain protein recognition of cisplatin-modified DNA. Biochemistry. 36:1997;11428-11436.
    • (1997) Biochemistry , vol.36 , pp. 11428-11436
    • Dunham, S.U.1    Lippard, S.J.2
  • 27
    • 0029883976 scopus 로고    scopus 로고
    • Equilibrium DNA binding of Sac7d protein from the hyperthermophile Sulfolobus acidocaldarius: Fluorescence and circular dichroism studies
    • McAfee J.G., Edmondson S.P., Zegar I., Shriver J.W. Equilibrium DNA binding of Sac7d protein from the hyperthermophile Sulfolobus acidocaldarius: fluorescence and circular dichroism studies. Biochemistry. 35:1996;4034-4045.
    • (1996) Biochemistry , vol.35 , pp. 4034-4045
    • McAfee, J.G.1    Edmondson, S.P.2    Zegar, I.3    Shriver, J.W.4
  • 28
    • 0028533719 scopus 로고
    • Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus
    • Bauman H., Knapp S., Lundbäck T., Ladenstein R., Härd T. Solution structure and DNA-binding properties of a thermostable protein from the archaeon Sulfolobus solfataricus. Nat. Struct. Biol. 1:1994;808-819.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 808-819
    • Bauman, H.1    Knapp, S.2    Lundbäck, T.3    Ladenstein, R.4    Härd, T.5
  • 29
    • 0031718377 scopus 로고    scopus 로고
    • The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA
    • Gao Y-G., Wang A.H-J.et al. The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA. Nat. Struct. Biol. 5:1998;782-786.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 782-786
    • Gao, Y.-G.1    Wang, A.H.-J.2
  • 32
    • 0031047683 scopus 로고    scopus 로고
    • The role of water in protein-DNA interactions
    • Schwabe J.W. The role of water in protein-DNA interactions. Curr. Opin. Struct. Biol. 7:1997;126-134.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 126-134
    • Schwabe, J.W.1
  • 34
    • 0029910813 scopus 로고    scopus 로고
    • Differences in water release for the binding of EcoRI to specific and nonspecific DNA sequences
    • Sidorova N.Y., Rau D.C. Differences in water release for the binding of EcoRI to specific and nonspecific DNA sequences. Proc. Natl Acad. Sci. USA. 93:1996;12272-12277.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 12272-12277
    • Sidorova, N.Y.1    Rau, D.C.2
  • 35
    • 0030841706 scopus 로고    scopus 로고
    • Thermodynamic analysis of monoclonal antibody binding to duplex DNA
    • Tanha J., Lee J.S. Thermodynamic analysis of monoclonal antibody binding to duplex DNA. Nucleic Acids Res. 7:1997;1442-1449.
    • (1997) Nucleic Acids Res. , vol.7 , pp. 1442-1449
    • Tanha, J.1    Lee, J.S.2
  • 36
    • 0032570633 scopus 로고    scopus 로고
    • Thermodynamics of specific and non-specific DNA binding by the c-Myb DNA-binding domain
    • Oda M., Furukawa K., Ogata K., Sarai A., Nakamura H. Thermodynamics of specific and non-specific DNA binding by the c-Myb DNA-binding domain. J. Mol. Biol. 276:1998;571-590.
    • (1998) J. Mol. Biol. , vol.276 , pp. 571-590
    • Oda, M.1    Furukawa, K.2    Ogata, K.3    Sarai, A.4    Nakamura, H.5
  • 37
    • 0032489503 scopus 로고    scopus 로고
    • Thermodynamic characterization of non-sequence-specific DNA-binding by the Sso7d protein from Sulfolobus solfataricus
    • Lündback T., Hansson H., Knapp S., Ladenstein R., Härd T. Thermodynamic characterization of non-sequence-specific DNA-binding by the Sso7d protein from Sulfolobus solfataricus. J. Mol. Biol. 276:1998;775-786.
    • (1998) J. Mol. Biol. , vol.276 , pp. 775-786
    • Lündback, T.1    Hansson, H.2    Knapp, S.3    Ladenstein, R.4    Härd, T.5
  • 39
    • 0024539180 scopus 로고
    • Defining the structure of irregular nucleic acids: Conventions and principles
    • Lavery R., Sklenar H. Defining the structure of irregular nucleic acids: conventions and principles. J. Biomol. Struct. Dyn. 6:1989;655-667.
    • (1989) J. Biomol. Struct. Dyn. , vol.6 , pp. 655-667
    • Lavery, R.1    Sklenar, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.