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Volumn 397, Issue 2, 2010, Pages 361-374

DNA Packaging-Associated Hyper-Capsid Expansion of Bacteriophage T3

Author keywords

bacteriophage DNA packaging motor; biological energy transduction; electron microscopy; mass spectrometry; two dimensional agarose gel electrophoresis

Indexed keywords

ADENOSINE TRIPHOSPHATE; CAPSID PROTEIN; CAPSID PROTEIN 1; CAPSID PROTEIN 2; DNA; INCOMPLETELY PACKAGED DNA; UNCLASSIFIED DRUG;

EID: 77349091984     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.01.058     Document Type: Article
Times cited : (13)

References (50)
  • 1
    • 57649226492 scopus 로고    scopus 로고
    • The bacteriophage DNA packaging motor
    • Rao V.B., and Feiss M. The bacteriophage DNA packaging motor. Annu. Rev. Genet. 42 (2008) 647-681
    • (2008) Annu. Rev. Genet. , vol.42 , pp. 647-681
    • Rao, V.B.1    Feiss, M.2
  • 4
    • 0031218420 scopus 로고    scopus 로고
    • Phage DNA packaging
    • Fujisawa H., and Morita M. Phage DNA packaging. Genes Cells 2 (1997) 537-545
    • (1997) Genes Cells , vol.2 , pp. 537-545
    • Fujisawa, H.1    Morita, M.2
  • 5
    • 58549118430 scopus 로고    scopus 로고
    • Correlation between the conformational states of F1-ATPase as determined from its crystal structure and single-molecule rotation
    • Okuno D., Fujisawa R., Iino R., Hirono-Hara Y., Imamura H., and Noji H. Correlation between the conformational states of F1-ATPase as determined from its crystal structure and single-molecule rotation. Proc. Natl Acad. Sci. USA 105 (2008) 20722-20727
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 20722-20727
    • Okuno, D.1    Fujisawa, R.2    Iino, R.3    Hirono-Hara, Y.4    Imamura, H.5    Noji, H.6
  • 6
    • 57149107555 scopus 로고    scopus 로고
    • Cooperative three-step motions in catalytic subunits of F(1)-ATPase correlate with 80° and 40° substep rotations
    • Masaike T., Koyama-Horibe F., Oiwa K., Yoshida M., and Nishizaka T. Cooperative three-step motions in catalytic subunits of F(1)-ATPase correlate with 80° and 40° substep rotations. Nat. Struct. Mol. Biol. 15 (2008) 1326-1333
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1326-1333
    • Masaike, T.1    Koyama-Horibe, F.2    Oiwa, K.3    Yoshida, M.4    Nishizaka, T.5
  • 7
    • 33947213307 scopus 로고    scopus 로고
    • Experimental test of connector rotation during DNA packaging into bacteriophage φ{symbol}29 capsids
    • Hugel T., Michaelis J., Hetherington C.L., Jardine P.J., Grimes S., Walter J.M., et al. Experimental test of connector rotation during DNA packaging into bacteriophage φ{symbol}29 capsids. PLoS Biol. 5 (2007) e59
    • (2007) PLoS Biol. , vol.5
    • Hugel, T.1    Michaelis, J.2    Hetherington, C.L.3    Jardine, P.J.4    Grimes, S.5    Walter, J.M.6
  • 8
    • 35148815738 scopus 로고    scopus 로고
    • Measurements of single DNA molecule packaging dynamics in bacteriophage lambda reveal high forces, high motor processivity, and capsid transformations
    • Fuller D.N., Raymer D.M., Rickgauer J.P., Robertson R.M., Catalano C.E., Anderson D.L., et al. Measurements of single DNA molecule packaging dynamics in bacteriophage lambda reveal high forces, high motor processivity, and capsid transformations. J. Mol. Biol. 373 (2007) 1113-1122
    • (2007) J. Mol. Biol. , vol.373 , pp. 1113-1122
    • Fuller, D.N.1    Raymer, D.M.2    Rickgauer, J.P.3    Robertson, R.M.4    Catalano, C.E.5    Anderson, D.L.6
  • 10
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage φ{symbol}29 portal motor can package DNA against a large internal force
    • Smith D.E., Tans S.J., Smith S.B., Grimes S., Anderson D.L., and Bustamante C. The bacteriophage φ{symbol}29 portal motor can package DNA against a large internal force. Nature 413 (2001) 748-752
    • (2001) Nature , vol.413 , pp. 748-752
    • Smith, D.E.1    Tans, S.J.2    Smith, S.B.3    Grimes, S.4    Anderson, D.L.5    Bustamante, C.6
  • 11
    • 13844267636 scopus 로고    scopus 로고
    • Analysis of biological motors via multidimensional fractionation: a strategy
    • Serwer P. Analysis of biological motors via multidimensional fractionation: a strategy. Electrophoresis 26 (2005) 494-499
    • (2005) Electrophoresis , vol.26 , pp. 494-499
    • Serwer, P.1
  • 13
    • 0037340654 scopus 로고    scopus 로고
    • Forces and pressures in DNA packaging and release from viral capsids
    • Tzlil S., Kindt J.T., Gelbart W.M., and Ben-Shaul A. Forces and pressures in DNA packaging and release from viral capsids. Biophys. J. 84 (2003) 1616-1627
    • (2003) Biophys. J. , vol.84 , pp. 1616-1627
    • Tzlil, S.1    Kindt, J.T.2    Gelbart, W.M.3    Ben-Shaul, A.4
  • 15
    • 33846113838 scopus 로고    scopus 로고
    • Structural and thermodynamic principles of viral packaging
    • Petrov A.S., and Harvey S.C. Structural and thermodynamic principles of viral packaging. Structure 15 (2007) 21-27
    • (2007) Structure , vol.15 , pp. 21-27
    • Petrov, A.S.1    Harvey, S.C.2
  • 16
    • 33745759318 scopus 로고    scopus 로고
    • Langevin dynamics simulations of genome packing in bacteriophage
    • Forrey C., and Muthukumar M. Langevin dynamics simulations of genome packing in bacteriophage. Biophys. J. 91 (2006) 25-41
    • (2006) Biophys. J. , vol.91 , pp. 25-41
    • Forrey, C.1    Muthukumar, M.2
  • 17
    • 22244483736 scopus 로고    scopus 로고
    • DNA packaging in bacteriophage: is twist important?
    • Spakowitz A.J., and Wang Z.G. DNA packaging in bacteriophage: is twist important?. Biophys. J. 88 (2005) 3912-3923
    • (2005) Biophys. J. , vol.88 , pp. 3912-3923
    • Spakowitz, A.J.1    Wang, Z.G.2
  • 18
    • 0037339538 scopus 로고    scopus 로고
    • Models of bacteriophage DNA packaging motors
    • Serwer P. Models of bacteriophage DNA packaging motors. J. Struct. Biol. 141 (2003) 179-188
    • (2003) J. Struct. Biol. , vol.141 , pp. 179-188
    • Serwer, P.1
  • 19
    • 0023390715 scopus 로고
    • Characterization of ATPase activity of a defined in vitro system for packaging of bacteriophage T3 DNA
    • Hamada K., Fujisawa H., and Minagawa T. Characterization of ATPase activity of a defined in vitro system for packaging of bacteriophage T3 DNA. Virology 159 (1987) 244-249
    • (1987) Virology , vol.159 , pp. 244-249
    • Hamada, K.1    Fujisawa, H.2    Minagawa, T.3
  • 20
    • 70549107627 scopus 로고    scopus 로고
    • Evidence for bacteriophage T7 tail extension during DNA injection
    • Serwer P., Wright E.T., Hakala K.W., and Weintraub S.T. Evidence for bacteriophage T7 tail extension during DNA injection. BMC Res. Notes 1 (2008) 36
    • (2008) BMC Res. Notes , vol.1 , pp. 36
    • Serwer, P.1    Wright, E.T.2    Hakala, K.W.3    Weintraub, S.T.4
  • 21
    • 50049135906 scopus 로고    scopus 로고
    • Proteome of the Escherichia coli envelope and technological challenges in membrane proteome analysis
    • Weiner J.H., and Li L. Proteome of the Escherichia coli envelope and technological challenges in membrane proteome analysis. Biochim. Biophys. Acta 1778 (2008) 1698-1713
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1698-1713
    • Weiner, J.H.1    Li, L.2
  • 22
    • 34748828756 scopus 로고    scopus 로고
    • Global proteomic profiling of native outer membrane vesicles derived from Escherichia coli
    • Lee E.Y., Bang J.Y., Park G.W., Choi D.S., Kang J.S., Kim H.J., et al. Global proteomic profiling of native outer membrane vesicles derived from Escherichia coli. Proteomics 7 (2007) 3143-3153
    • (2007) Proteomics , vol.7 , pp. 3143-3153
    • Lee, E.Y.1    Bang, J.Y.2    Park, G.W.3    Choi, D.S.4    Kang, J.S.5    Kim, H.J.6
  • 23
    • 43049125220 scopus 로고    scopus 로고
    • Impact of chemical and structural anisotropy on the electrophoretic mobility of spherical soft multilayer particles: the case of bacteriophage MS2
    • Langlet J., Gaboriaud F., Gantzer C., and Duval J.F. Impact of chemical and structural anisotropy on the electrophoretic mobility of spherical soft multilayer particles: the case of bacteriophage MS2. Biophys. J. 94 (2008) 3293-3312
    • (2008) Biophys. J. , vol.94 , pp. 3293-3312
    • Langlet, J.1    Gaboriaud, F.2    Gantzer, C.3    Duval, J.F.4
  • 24
    • 0003921375 scopus 로고
    • Academic Press, London, UK
    • Shaw D.J. Electrophoresis (1972), Academic Press, London, UK
    • (1972) Electrophoresis
    • Shaw, D.J.1
  • 25
    • 0018117327 scopus 로고
    • Electrophoresis of bacteriophage T7 and T7 capsids in agarose gels
    • Serwer P., and Pichler M.E. Electrophoresis of bacteriophage T7 and T7 capsids in agarose gels. J. Virol. 28 (1978) 917-928
    • (1978) J. Virol. , vol.28 , pp. 917-928
    • Serwer, P.1    Pichler, M.E.2
  • 26
    • 0032996698 scopus 로고    scopus 로고
    • Advances in the separation of bacteriophages and related particles
    • Serwer P., and Griess G.A. Advances in the separation of bacteriophages and related particles. J. Chromatogr., B: Biomed. Sci. Appl. 722 (1999) 179-190
    • (1999) J. Chromatogr., B: Biomed. Sci. Appl. , vol.722 , pp. 179-190
    • Serwer, P.1    Griess, G.A.2
  • 27
    • 33947103158 scopus 로고    scopus 로고
    • Computer-assisted 2-D agarose electrophoresis of Haemophilus influenzae type B meningitis vaccines and analysis of polydisperse particle populations in the size range of viruses: a review
    • Tietz D. Computer-assisted 2-D agarose electrophoresis of Haemophilus influenzae type B meningitis vaccines and analysis of polydisperse particle populations in the size range of viruses: a review. Electrophoresis 28 (2007) 512-524
    • (2007) Electrophoresis , vol.28 , pp. 512-524
    • Tietz, D.1
  • 28
    • 0034755960 scopus 로고    scopus 로고
    • The length dependence of translational diffusion, free solution electrophoretic mobility, and electrophoretic tether force of rigid rod-like model duplex DNA
    • Allison S., Chen C., and Stigter D. The length dependence of translational diffusion, free solution electrophoretic mobility, and electrophoretic tether force of rigid rod-like model duplex DNA. Biophys. J. 81 (2001) 2558-2568
    • (2001) Biophys. J. , vol.81 , pp. 2558-2568
    • Allison, S.1    Chen, C.2    Stigter, D.3
  • 29
    • 0018561189 scopus 로고
    • Fibrous projections form the core of a bacteriophage T7 procapsid
    • Serwer P. Fibrous projections form the core of a bacteriophage T7 procapsid. J. Supramol. Struct. 11 (1979) 321-326
    • (1979) J. Supramol. Struct. , vol.11 , pp. 321-326
    • Serwer, P.1
  • 30
    • 0018877016 scopus 로고
    • A technique for electrophoresis in multiple-concentration agarose gels
    • Serwer P. A technique for electrophoresis in multiple-concentration agarose gels. Anal. Biochem. 101 (1980) 154-159
    • (1980) Anal. Biochem. , vol.101 , pp. 154-159
    • Serwer, P.1
  • 31
    • 0021112697 scopus 로고
    • Comparison of the physical properties and assembly pathways of the related bacteriophages T7, T3 and φ{symbol}II
    • Serwer P., Watson R.H., Hayes S.J., and Allen J.L. Comparison of the physical properties and assembly pathways of the related bacteriophages T7, T3 and φ{symbol}II. J. Mol. Biol. 170 (1983) 447-469
    • (1983) J. Mol. Biol. , vol.170 , pp. 447-469
    • Serwer, P.1    Watson, R.H.2    Hayes, S.J.3    Allen, J.L.4
  • 32
    • 0017625998 scopus 로고
    • Flattening and shrinkage of bacteriophage T7 after preparation for electron microscopy by negative staining
    • Serwer P. Flattening and shrinkage of bacteriophage T7 after preparation for electron microscopy by negative staining. J. Ultrastruct. Res. 58 (1977) 243-245
    • (1977) J. Ultrastruct. Res. , vol.58 , pp. 243-245
    • Serwer, P.1
  • 33
    • 0025908787 scopus 로고
    • The maturation-dependent conformational change of phage T4 capsid involves the translocation of specific epitopes between the inner and the outer capsid surfaces
    • Steven A.C., Bauer A.C., Bisher M.E., Robey F.A., and Black L.W. The maturation-dependent conformational change of phage T4 capsid involves the translocation of specific epitopes between the inner and the outer capsid surfaces. J. Struct. Biol. 106 (1991) 221-236
    • (1991) J. Struct. Biol. , vol.106 , pp. 221-236
    • Steven, A.C.1    Bauer, A.C.2    Bisher, M.E.3    Robey, F.A.4    Black, L.W.5
  • 35
    • 0023660940 scopus 로고
    • Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage φ{symbol}29
    • Guo P., Peterson C., and Anderson D. Prohead and DNA-gp3-dependent ATPase activity of the DNA packaging protein gp16 of bacteriophage φ{symbol}29. J. Mol. Biol. 197 (1987) 229-236
    • (1987) J. Mol. Biol. , vol.197 , pp. 229-236
    • Guo, P.1    Peterson, C.2    Anderson, D.3
  • 36
    • 0023390715 scopus 로고
    • Characterization of ATPase activity of a defined in vitro system for packaging of bacteriophage T3 DNA
    • Hamada K., Fujisawa H., and Minagawa T. Characterization of ATPase activity of a defined in vitro system for packaging of bacteriophage T3 DNA. Virology 159 (1987) 244-249
    • (1987) Virology , vol.159 , pp. 244-249
    • Hamada, K.1    Fujisawa, H.2    Minagawa, T.3
  • 37
    • 14144256682 scopus 로고    scopus 로고
    • Bacteriophage lambda terminase: alterations of the high-affinity ATPase affect viral DNA packaging
    • Dhar A., and Feiss M. Bacteriophage lambda terminase: alterations of the high-affinity ATPase affect viral DNA packaging. J. Mol. Biol. 347 (2005) 71-80
    • (2005) J. Mol. Biol. , vol.347 , pp. 71-80
    • Dhar, A.1    Feiss, M.2
  • 38
    • 37749051185 scopus 로고    scopus 로고
    • Portal motor velocity and internal force resisting viral DNA packaging in bacteriophage φ{symbol}29
    • Rickgauer J.P., Fuller D.N., Grimes S., Jardine P.J., Anderson D.L., and Smith D.E. Portal motor velocity and internal force resisting viral DNA packaging in bacteriophage φ{symbol}29. Biophys. J. 94 (2008) 159-167
    • (2008) Biophys. J. , vol.94 , pp. 159-167
    • Rickgauer, J.P.1    Fuller, D.N.2    Grimes, S.3    Jardine, P.J.4    Anderson, D.L.5    Smith, D.E.6
  • 39
    • 7044227902 scopus 로고    scopus 로고
    • Improved isolation of undersampled bacteriophages: finding of distant terminase genes
    • Serwer P., Hayes S.J., Zaman S., Lieman K., Rolando M., and Hardies S.C. Improved isolation of undersampled bacteriophages: finding of distant terminase genes. Virology 329 (2004) 412-424
    • (2004) Virology , vol.329 , pp. 412-424
    • Serwer, P.1    Hayes, S.J.2    Zaman, S.3    Lieman, K.4    Rolando, M.5    Hardies, S.C.6
  • 40
    • 0026538238 scopus 로고
    • Bacteriophage P22 portal protein is part of the gauge that regulates packing density of intravirion DNA
    • Casjens S., Wyckoff E., Hayden M., Sampson L., Eppler K., Randall S., et al. Bacteriophage P22 portal protein is part of the gauge that regulates packing density of intravirion DNA. J. Mol. Biol. 224 (1992) 1055-1074
    • (1992) J. Mol. Biol. , vol.224 , pp. 1055-1074
    • Casjens, S.1    Wyckoff, E.2    Hayden, M.3    Sampson, L.4    Eppler, K.5    Randall, S.6
  • 41
    • 33745506037 scopus 로고    scopus 로고
    • The structure of an infectious P22 virion shows the signal for headful DNA packaging
    • Lander G.C., Tang L., Casjens S.R., Gilcrease E.B., Prevelige P., Poliakov A., et al. The structure of an infectious P22 virion shows the signal for headful DNA packaging. Science 312 (2006) 1791-1795
    • (2006) Science , vol.312 , pp. 1791-1795
    • Lander, G.C.1    Tang, L.2    Casjens, S.R.3    Gilcrease, E.B.4    Prevelige, P.5    Poliakov, A.6
  • 42
  • 43
    • 0025176610 scopus 로고
    • In vitro cleavage of the concatemer joint of bacteriophage T3 DNA
    • Fujisawa H., Kimura M., and Hashimoto C. In vitro cleavage of the concatemer joint of bacteriophage T3 DNA. Virology 174 (1990) 26-34
    • (1990) Virology , vol.174 , pp. 26-34
    • Fujisawa, H.1    Kimura, M.2    Hashimoto, C.3
  • 44
    • 32744469335 scopus 로고    scopus 로고
    • Viral genome packaging machines: an overview
    • Catalano C.E. (Ed), Landes Bioscience, Georgetown, TX
    • Catalano C.E. Viral genome packaging machines: an overview. In: Catalano C.E. (Ed). Viral Genome Packaging Machines: Genetics, Structure and Mechanism (2005), Landes Bioscience, Georgetown, TX 1-4
    • (2005) Viral Genome Packaging Machines: Genetics, Structure and Mechanism , pp. 1-4
    • Catalano, C.E.1
  • 45
    • 0036300304 scopus 로고    scopus 로고
    • The large subunit of bacteriophage lambda's terminase plays a role in DNA translocation and packaging termination
    • Duffy C., and Feiss M. The large subunit of bacteriophage lambda's terminase plays a role in DNA translocation and packaging termination. J. Mol. Biol. 316 (2002) 547-561
    • (2002) J. Mol. Biol. , vol.316 , pp. 547-561
    • Duffy, C.1    Feiss, M.2
  • 46
    • 0027983134 scopus 로고
    • Analysis of functional domains of the packaging proteins of bacteriophage T3 by site-directed mutagenesis
    • Morita M., Tasaka M., and Fujisawa H. Analysis of functional domains of the packaging proteins of bacteriophage T3 by site-directed mutagenesis. J. Mol. Biol. 235 (1994) 248-259
    • (1994) J. Mol. Biol. , vol.235 , pp. 248-259
    • Morita, M.1    Tasaka, M.2    Fujisawa, H.3
  • 47
    • 0028960132 scopus 로고
    • Structural and functional domains of the large subunit of the bacteriophage T3 DNA packaging enzyme: importance of the C-terminal region in prohead binding
    • Morita M., Tasaka M., and Fujisawa H. Structural and functional domains of the large subunit of the bacteriophage T3 DNA packaging enzyme: importance of the C-terminal region in prohead binding. J. Mol. Biol. 245 (1995) 635-644
    • (1995) J. Mol. Biol. , vol.245 , pp. 635-644
    • Morita, M.1    Tasaka, M.2    Fujisawa, H.3
  • 48
    • 33749561425 scopus 로고    scopus 로고
    • The DNA translocating ATPase of bacteriophage T4 packaging motor
    • Kondabagil K.R., Zhang Z., and Rao V.B. The DNA translocating ATPase of bacteriophage T4 packaging motor. J. Mol. Biol. 363 (2006) 786-799
    • (2006) J. Mol. Biol. , vol.363 , pp. 786-799
    • Kondabagil, K.R.1    Zhang, Z.2    Rao, V.B.3
  • 49
    • 85086690127 scopus 로고
    • SAMase gene of bacteriophage T3 is responsible for overcoming host restriction
    • Studier F.W., and Movva N.R. SAMase gene of bacteriophage T3 is responsible for overcoming host restriction. J. Virol. 19 (1976) 135-136
    • (1976) J. Virol. , vol.19 , pp. 135-136
    • Studier, F.W.1    Movva, N.R.2
  • 50
    • 0024720506 scopus 로고
    • The sieving of spheres during agarose gel electrophoresis: quantitation and modeling
    • Griess G.A., Moreno E.T., Easom R.A., and Serwer P. The sieving of spheres during agarose gel electrophoresis: quantitation and modeling. Biopolymers 28 (1989) 1475-1484
    • (1989) Biopolymers , vol.28 , pp. 1475-1484
    • Griess, G.A.1    Moreno, E.T.2    Easom, R.A.3    Serwer, P.4


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