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Volumn 36, Issue 12, 2008, Pages 4032-4037

Structural change in a B-DNA helix with hydrostatic pressure

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE; CYTOSINE; DNA B; GUANINE; THYMINE; WATER;

EID: 47249155339     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkn350     Document Type: Article
Times cited : (49)

References (41)
  • 1
    • 0037171133 scopus 로고    scopus 로고
    • The interactions of nucleic acids at elevated hydrostatic pressure
    • Macgregor,R.B. (2002) The interactions of nucleic acids at elevated hydrostatic pressure. Biochim. Biophys. Acta, 1595, 266-276.
    • (2002) Biochim. Biophys. Acta , vol.1595 , pp. 266-276
    • Macgregor, R.B.1
  • 2
    • 0006467940 scopus 로고    scopus 로고
    • Effect of hydrostatic pressure on nucleic acids
    • Macgregor,R.B. (1998) Effect of hydrostatic pressure on nucleic acids. Biopolymers, 48, 253-263.
    • (1998) Biopolymers , vol.48 , pp. 253-263
    • Macgregor, R.B.1
  • 3
    • 8744233998 scopus 로고    scopus 로고
    • Differential pressure resistance in the activity of RNA polymerase isolated from Shewanella violacea and Escherichia coli
    • Kawano,H., Nakasone,K., Matsumoto,M., Yoshida,Y., Usami,R., Kato,C. and Abe,F. (2004) Differential pressure resistance in the activity of RNA polymerase isolated from Shewanella violacea and Escherichia coli. Extremophiles, 8, 367-375.
    • (2004) Extremophiles , vol.8 , pp. 367-375
    • Kawano, H.1    Nakasone, K.2    Matsumoto, M.3    Yoshida, Y.4    Usami, R.5    Kato, C.6    Abe, F.7
  • 4
    • 23944502345 scopus 로고    scopus 로고
    • Protein-DNA interactions under high-pressure conditions, studied by capillary narrow-tube electrophoresis
    • Kawano,H., Nakasone,K., Abe,F., Kato,C., Yoshida,Y., Usami,R. and Horikoshi,K. (2005) Protein-DNA interactions under high-pressure conditions, studied by capillary narrow-tube electrophoresis. Biosci. Biotechnol. Biochem., 69, 1415-1417.
    • (2005) Biosci. Biotechnol. Biochem , vol.69 , pp. 1415-1417
    • Kawano, H.1    Nakasone, K.2    Abe, F.3    Kato, C.4    Yoshida, Y.5    Usami, R.6    Horikoshi, K.7
  • 5
    • 0028210538 scopus 로고
    • Hydrostatic pressure reverses osmotic pressure effects on the specificity of E. coli DNA interactions
    • Robinson,C.R. and Sligar,S.G. (1994) Hydrostatic pressure reverses osmotic pressure effects on the specificity of E. coli DNA interactions. Biochemistry, 33, 3787-3793.
    • (1994) Biochemistry , vol.33 , pp. 3787-3793
    • Robinson, C.R.1    Sligar, S.G.2
  • 6
    • 0028944994 scopus 로고
    • Heterogeneity in molecular recognition by restriction endonucleases: Osmotic and hydrostatic pressure effects on BamHI, PvuLI, and EcoRV specificity
    • Robinson,C.R. and Sligar,S.G. (1995) Heterogeneity in molecular recognition by restriction endonucleases: Osmotic and hydrostatic pressure effects on BamHI, PvuLI, and EcoRV specificity. Proc. Natl Acad. Sci. USA, 92, 3444-3448.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 3444-3448
    • Robinson, C.R.1    Sligar, S.G.2
  • 7
    • 0032522139 scopus 로고    scopus 로고
    • DNA bending: The prevalence of kinkiness and the virtues of normality
    • Dickerson,R.E. (1998) DNA bending: The prevalence of kinkiness and the virtues of normality. Nucleic Acids Res., 26, 1906-1926.
    • (1998) Nucleic Acids Res , vol.26 , pp. 1906-1926
    • Dickerson, R.E.1
  • 8
    • 3843117972 scopus 로고    scopus 로고
    • The effects of hydrostatic pressure change on DNA integrity in the hydrothermalvent mussel Bathymodiolus azoricus: Implications for future deep-sea mutagenicity studies
    • Dixon,D.R., Pruski,A.M. and Dixon,L.R.J. (2004) The effects of hydrostatic pressure change on DNA integrity in the hydrothermalvent mussel Bathymodiolus azoricus: Implications for future deep-sea mutagenicity studies. Mutat. Res., 552, 235-246.
    • (2004) Mutat. Res , vol.552 , pp. 235-246
    • Dixon, D.R.1    Pruski, A.M.2    Dixon, L.R.J.3
  • 9
    • 14644414887 scopus 로고    scopus 로고
    • Analysis of hydrostatic pressure effects on transcription in Escherichia coli by DNA microarray procedure
    • Ishii,A., Oshima,T., Sato,T., Nakasone,K., Mori,H. and Kato,C. (2005) Analysis of hydrostatic pressure effects on transcription in Escherichia coli by DNA microarray procedure. Extremophiles, 9, 65-73.
    • (2005) Extremophiles , vol.9 , pp. 65-73
    • Ishii, A.1    Oshima, T.2    Sato, T.3    Nakasone, K.4    Mori, H.5    Kato, C.6
  • 11
    • 0000725483 scopus 로고
    • Thermodynamic fluctuations in protein molecules
    • Cooper,A. (1976) Thermodynamic fluctuations in protein molecules. Proc. Natl Acad. Sci. USA, 73, 2740-2741.
    • (1976) Proc. Natl Acad. Sci. USA , vol.73 , pp. 2740-2741
    • Cooper, A.1
  • 12
    • 0034194198 scopus 로고    scopus 로고
    • Structural basis for uracil DNA glycosylase interaction with uracil: NMR study
    • Ghosh,M., Kumar,N.V., Varshney,U. and Chary,K.V.R. (2000) Structural basis for uracil DNA glycosylase interaction with uracil: NMR study. Nucleic Acids Res., 28, 1906-1912.
    • (2000) Nucleic Acids Res , vol.28 , pp. 1906-1912
    • Ghosh, M.1    Kumar, N.V.2    Varshney, U.3    Chary, K.V.R.4
  • 13
    • 0035247443 scopus 로고    scopus 로고
    • Pressure-resisting cell for high-pressure, high-resolution nuclear magnetic resonance measurements at very high magnetic fields
    • Yamada,H., Nishikawa,K., Honda,M., Shimura,T., Akasaka,K. and Tabayashi,K. (2001) Pressure-resisting cell for high-pressure, high-resolution nuclear magnetic resonance measurements at very high magnetic fields. Rev. Sci. Instrum., 72, 1463-1471.
    • (2001) Rev. Sci. Instrum , vol.72 , pp. 1463-1471
    • Yamada, H.1    Nishikawa, K.2    Honda, M.3    Shimura, T.4    Akasaka, K.5    Tabayashi, K.6
  • 14
    • 0042511922 scopus 로고    scopus 로고
    • The solution structure of bovine pancreatic trypsin inhibitor at high pressure
    • Williamson,M.P., Akasaka,K. and Refaee,M. (2003) The solution structure of bovine pancreatic trypsin inhibitor at high pressure. Protein Sci. 12, 1971-1979.
    • (2003) Protein Sci , vol.12 , pp. 1971-1979
    • Williamson, M.P.1    Akasaka, K.2    Refaee, M.3
  • 15
    • 0344406172 scopus 로고    scopus 로고
    • Pressure-dependent changes in the solution structure of hen egg-white lysozyme
    • Refaee,M., Tezuka, T., Akasaka,K. and Williamson,M.P. (2003) Pressure-dependent changes in the solution structure of hen egg-white lysozyme. J. Mol. Biol., 327, 857-865.
    • (2003) J. Mol. Biol , vol.327 , pp. 857-865
    • Refaee, M.1    Tezuka, T.2    Akasaka, K.3    Williamson, M.P.4
  • 16
    • 42449128777 scopus 로고    scopus 로고
    • Pressure induced changes in the solution structure of the GB1 domain of protein G
    • Wilton,D.J., Tunnicliffe,R.B., Kamatari,Y.O., Akasaka,K. and Williamson,M.P. (2008) Pressure induced changes in the solution structure of the GB1 domain of protein G. Proteins, 71, 1432-1440.
    • (2008) Proteins , vol.71 , pp. 1432-1440
    • Wilton, D.J.1    Tunnicliffe, R.B.2    Kamatari, Y.O.3    Akasaka, K.4    Williamson, M.P.5
  • 17
    • 44949269218 scopus 로고
    • Empirical comparisons of models for chemical shift calculation in proteins
    • Williamson,M.P. and Asakura, T. (1993) Empirical comparisons of models for chemical shift calculation in proteins. J. Magn. Reson. Ser. B 101, 63-71.
    • (1993) J. Magn. Reson. Ser. B , vol.101 , pp. 63-71
    • Williamson, M.P.1    Asakura, T.2
  • 18
    • 0000635348 scopus 로고
    • The relationship between amide proton chemical shifts and secondary structure in proteins
    • Asakura, T., Taoka,K., Demura,M. and Williamson,M.P. (1995) The relationship between amide proton chemical shifts and secondary structure in proteins. J. Biomol. NMR, 6, 227-236.
    • (1995) J. Biomol. NMR , vol.6 , pp. 227-236
    • Asakura, T.1    Taoka, K.2    Demura, M.3    Williamson, M.P.4
  • 19
    • 0029437665 scopus 로고
    • Calibration of ring-current effects in proteins and nucleic acids
    • Case,D.A. (1995) Calibration of ring-current effects in proteins and nucleic acids. J. Biomol. NMR, 6, 341-346.
    • (1995) J. Biomol. NMR , vol.6 , pp. 341-346
    • Case, D.A.1
  • 20
    • 0043211092 scopus 로고    scopus 로고
    • Complexation-induced chemical shifts: Ab initio parameterization of transferable bond anisotropies
    • Packer,M.J., Zonta,C. and Hunter,C.A. (2003) Complexation-induced chemical shifts: ab initio parameterization of transferable bond anisotropies. J. Magn. Reson., 162, 102-112.
    • (2003) J. Magn. Reson , vol.162 , pp. 102-112
    • Packer, M.J.1    Zonta, C.2    Hunter, C.A.3
  • 23
    • 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
  • 24
    • 0027995683 scopus 로고
    • Detection, delineation, measurement and display of cavities in macromolecular structures
    • Kleywegt,G.J. and Jones,T.A. (1994) Detection, delineation, measurement and display of cavities in macromolecular structures. Acta Crystallogr., D50, 178-185.
    • (1994) Acta Crystallogr , vol.D50 , pp. 178-185
    • Kleywegt, G.J.1    Jones, T.A.2
  • 25
    • 0242362190 scopus 로고    scopus 로고
    • Many residues in cytochrome c populate alternative states under equilibrium conditions
    • Williamson,M.P. (2003) Many residues in cytochrome c populate alternative states under equilibrium conditions. Proteins, 53 731-739.
    • (2003) Proteins , vol.53 , pp. 731-739
    • Williamson, M.P.1
  • 26
    • 27644503431 scopus 로고    scopus 로고
    • An experimental investigation of conformational fluctuations in proteins G and L
    • Tunnicliffe,R.B., Waby,J.L., Williams,R.J. and Williamson,M.P. (2005) An experimental investigation of conformational fluctuations in proteins G and L. Structure, 13, 1677-1684.
    • (2005) Structure , vol.13 , pp. 1677-1684
    • Tunnicliffe, R.B.1    Waby, J.L.2    Williams, R.J.3    Williamson, M.P.4
  • 27
    • 0028222102 scopus 로고
    • Influence of base composition, base sequence, and duplex structure on DNA hydration: Apparent molar volumes and apparent molar adiabatic compressibilities of synthetic and natural DNA duplexes at 25 °C
    • Chalikian,T.V., Sarvazyan,A.P., Plum,G.E. and Breslauer,K.J. (1994) Influence of base composition, base sequence, and duplex structure on DNA hydration: Apparent molar volumes and apparent molar adiabatic compressibilities of synthetic and natural DNA duplexes at 25 °C. Biochemistry, 33, 2394-2401.
    • (1994) Biochemistry , vol.33 , pp. 2394-2401
    • Chalikian, T.V.1    Sarvazyan, A.P.2    Plum, G.E.3    Breslauer, K.J.4
  • 28
    • 0000137680 scopus 로고    scopus 로고
    • Volumetric properties of nucleic acids
    • Chalikian,T.V. and Breslauer,K.J. (1998) Volumetric properties of nucleic acids. Biopolymers, 48, 264-280.
    • (1998) Biopolymers , vol.48 , pp. 264-280
    • Chalikian, T.V.1    Breslauer, K.J.2
  • 30
    • 0033104772 scopus 로고    scopus 로고
    • The role of water structure in conformational changes of nucleic acids in ambient and high-pressure conditions
    • Barciszewski,J., Jurczak,J., Porowski,S., Specht,T. and Erdmann,V.A. (1999) The role of water structure in conformational changes of nucleic acids in ambient and high-pressure conditions. Eur. J. Biochem., 260, 293-307.
    • (1999) Eur. J. Biochem , vol.260 , pp. 293-307
    • Barciszewski, J.1    Jurczak, J.2    Porowski, S.3    Specht, T.4    Erdmann, V.A.5
  • 31
    • 0024384598 scopus 로고
    • Acoustical investigation of poly(dA).poly(dT), poly[d(A-T)]. Poly [d(A-T)], poly(A).poly(U) and DNA hydration in dilute aqueous solutions
    • Buckin,V.A., Kankiya,B.I., Sarvazyan,A.P. and Uedaira,H. (1989) Acoustical investigation of poly(dA).poly(dT), poly[d(A-T)]. Poly [d(A-T)], poly(A).poly(U) and DNA hydration in dilute aqueous solutions. Nucleic Acids Res., 17, 4189-4203.
    • (1989) Nucleic Acids Res , vol.17 , pp. 4189-4203
    • Buckin, V.A.1    Kankiya, B.I.2    Sarvazyan, A.P.3    Uedaira, H.4
  • 32
    • 0027993455 scopus 로고
    • Hydration and partial compressibility of biological compounds
    • Chalikian,T.V., Sarvazyan,A.P. and Breslauer,K.J. (1994) Hydration and partial compressibility of biological compounds. Biophys. Chem., 51, 89-109.
    • (1994) Biophys. Chem , vol.51 , pp. 89-109
    • Chalikian, T.V.1    Sarvazyan, A.P.2    Breslauer, K.J.3
  • 34
    • 0023644307 scopus 로고
    • Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres
    • Kundrot,C.E. and Richards,F.M. (1987) Crystal structure of hen egg-white lysozyme at a hydrostatic pressure of 1000 atmospheres. J. Mol. Biol. 193, 157-170.
    • (1987) J. Mol. Biol , vol.193 , pp. 157-170
    • Kundrot, C.E.1    Richards, F.M.2
  • 35
    • 33847308554 scopus 로고    scopus 로고
    • Structural rigidity of a large cavity-containing protein revealed by high-pressure crystallography
    • Collins,M.D., Quillin,M.L., Hummer,G., Matthews,B.W. and Gruner,S.M. (2007) Structural rigidity of a large cavity-containing protein revealed by high-pressure crystallography. J. Mol. Biol., 367, 752-763.
    • (2007) J. Mol. Biol , vol.367 , pp. 752-763
    • Collins, M.D.1    Quillin, M.L.2    Hummer, G.3    Matthews, B.W.4    Gruner, S.M.5
  • 36
    • 0036154017 scopus 로고    scopus 로고
    • Probing substates in sperm whale myoglobin using high-pressure crystallography
    • Urayama,P., Phillips,G.N. and Gruner,S.M. (2002) Probing substates in sperm whale myoglobin using high-pressure crystallography. Structure 10, 51-60.
    • (2002) Structure , vol.10 , pp. 51-60
    • Urayama, P.1    Phillips, G.N.2    Gruner, S.M.3
  • 37
    • 33646490977 scopus 로고    scopus 로고
    • High pressure macromolecular crystallography: The 140-MPa crystal structure at 2.3 Å resolution of urate oxidase, a 135-kDa tetrameric assembly
    • Colloc'h,N., Girard,E., Dhaussy,A.C., Kahn,R., Ascone,I., Mezouar,M. and Fourme,R. (2006) High pressure macromolecular crystallography: The 140-MPa crystal structure at 2.3 Å resolution of urate oxidase, a 135-kDa tetrameric assembly. Biochim. Biophys. Acta, 1764, 391-397.
    • (2006) Biochim. Biophys. Acta , vol.1764 , pp. 391-397
    • Colloc'h, N.1    Girard, E.2    Dhaussy, A.C.3    Kahn, R.4    Ascone, I.5    Mezouar, M.6    Fourme, R.7
  • 38
    • 17844397457 scopus 로고    scopus 로고
    • The first crystal structure of a macromolecular assembly under high pressure: CpMV at 330 MPa
    • Girard,E., Kahn,R., Mezouar,M., Dhaussy,A.C., Lin,T.W., Johnson,J.E. and Fourme,R. (2005) The first crystal structure of a macromolecular assembly under high pressure: CpMV at 330 MPa. Biophys. J., 88 3562-3571.
    • (2005) Biophys. J , vol.88 , pp. 3562-3571
    • Girard, E.1    Kahn, R.2    Mezouar, M.3    Dhaussy, A.C.4    Lin, T.W.5    Johnson, J.E.6    Fourme, R.7
  • 39
    • 14644424521 scopus 로고    scopus 로고
    • NMR snapshots of a fluctuating protein structure: Ubiquitin at 30 bar-3 kbar
    • Kitahara,R., Yokoyama,S. and Akasaka,K. (2005) NMR snapshots of a fluctuating protein structure: Ubiquitin at 30 bar-3 kbar. J. Mol. Biol., 347, 277-285.
    • (2005) J. Mol. Biol , vol.347 , pp. 277-285
    • Kitahara, R.1    Yokoyama, S.2    Akasaka, K.3
  • 41
    • 0027762355 scopus 로고
    • Pressure stability of proteins
    • Silva,J.L. and Weber,G. (1993) Pressure stability of proteins. Ann. Rev. Phys. Chem., 44, 89-113.
    • (1993) Ann. Rev. Phys. Chem , vol.44 , pp. 89-113
    • Silva, J.L.1    Weber, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.