메뉴 건너뛰기




Volumn 20, Issue 2, 2010, Pages 210-216

Virus particle maturation: Insights into elegantly programmed nanomachines

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOPHAGE DNA; CAPSID PROTEIN; DOUBLE STRANDED DNA;

EID: 77951298327     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2010.01.004     Document Type: Review
Times cited : (83)

References (38)
  • 1
    • 0019075292 scopus 로고
    • Movement and self-control in protein assemblies. Quasi-equivalence revisited
    • Caspar D.L. Movement and self-control in protein assemblies. Quasi-equivalence revisited. Biophys J 1980, 32:103-138.
    • (1980) Biophys J , vol.32 , pp. 103-138
    • Caspar, D.L.1
  • 3
    • 0026757341 scopus 로고
    • Maturation cleavage required for infectivity of a nodavirus
    • Schneemann A., Zhong W., Gallagher T.M., Rueckert R.R. Maturation cleavage required for infectivity of a nodavirus. J Virol 1992, 66:6728-6734.
    • (1992) J Virol , vol.66 , pp. 6728-6734
    • Schneemann, A.1    Zhong, W.2    Gallagher, T.M.3    Rueckert, R.R.4
  • 5
    • 58149517675 scopus 로고    scopus 로고
    • Characterization of large conformational changes and autoproteolysis in the maturation of a T=4 virus capsid
    • Matsui T., Lander G., Johnson J.E. Characterization of large conformational changes and autoproteolysis in the maturation of a T=4 virus capsid. J Virol 2009, 83:1126-1134.
    • (2009) J Virol , vol.83 , pp. 1126-1134
    • Matsui, T.1    Lander, G.2    Johnson, J.E.3
  • 6
    • 17044440108 scopus 로고    scopus 로고
    • Virus maturation: dynamics and mechanism of a stabilizing structural transition that leads to infectivity
    • Steven A.C., Heymann J.B., Cheng N., Trus B.L., Conway J.F. Virus maturation: dynamics and mechanism of a stabilizing structural transition that leads to infectivity. Curr Opin Struct Biol 2005, 15:227-236.
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 227-236
    • Steven, A.C.1    Heymann, J.B.2    Cheng, N.3    Trus, B.L.4    Conway, J.F.5
  • 7
    • 50849118817 scopus 로고    scopus 로고
    • Bacteriophage lambda stabilization by auxiliary protein gpD: timing, location, and mechanism of attachment determined by cryo-EM
    • Lander G.C., Evilevitch A., Jeembaeva M., Potter C.S., Carragher B., Johnson J.E. Bacteriophage lambda stabilization by auxiliary protein gpD: timing, location, and mechanism of attachment determined by cryo-EM. Structure 2008, 16:1399-1406.
    • (2008) Structure , vol.16 , pp. 1399-1406
    • Lander, G.C.1    Evilevitch, A.2    Jeembaeva, M.3    Potter, C.S.4    Carragher, B.5    Johnson, J.E.6
  • 8
    • 32544460955 scopus 로고    scopus 로고
    • Time-resolved molecular dynamics of bacteriophage HK97 capsid maturation interpreted by electron cryo-microscopy and X-ray crystallography
    • Wikoff W.R., Conway J.F., Tang J., Lee K.K., Gan L., Cheng N., Duda R.L., Hendrix R.W., Steven A.C., Johnson J.E. Time-resolved molecular dynamics of bacteriophage HK97 capsid maturation interpreted by electron cryo-microscopy and X-ray crystallography. J Struct Biol 2006, 153:300-306.
    • (2006) J Struct Biol , vol.153 , pp. 300-306
    • Wikoff, W.R.1    Conway, J.F.2    Tang, J.3    Lee, K.K.4    Gan, L.5    Cheng, N.6    Duda, R.L.7    Hendrix, R.W.8    Steven, A.C.9    Johnson, J.E.10
  • 10
    • 0037313264 scopus 로고    scopus 로고
    • Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions
    • Jiang W., Li Z., Zhang Z., Baker M.L., Prevelige P.E., Chiu W. Coat protein fold and maturation transition of bacteriophage P22 seen at subnanometer resolutions. Nat Struct Biol 2003, 10:131-135.
    • (2003) Nat Struct Biol , vol.10 , pp. 131-135
    • Jiang, W.1    Li, Z.2    Zhang, Z.3    Baker, M.L.4    Prevelige, P.E.5    Chiu, W.6
  • 12
    • 52949115267 scopus 로고    scopus 로고
    • Assembly architecture and DNA binding of the bacteriophage P22 terminase small subunit
    • Nemecek D., Lander G.C., Johnson J.E., Casjens S.R., Thomas J.G.J. Assembly architecture and DNA binding of the bacteriophage P22 terminase small subunit. J Mol Biol 2008, 383:494-501.
    • (2008) J Mol Biol , vol.383 , pp. 494-501
    • Nemecek, D.1    Lander, G.C.2    Johnson, J.E.3    Casjens, S.R.4    Thomas, J.G.J.5
  • 14
    • 33947281384 scopus 로고    scopus 로고
    • The structure of the ATPase that powers DNA packaging into bacteriophage T4 procapsids
    • Sun S., Kondabagil K., Gentz P.M., Rossmann M.G., Rao V.B. The structure of the ATPase that powers DNA packaging into bacteriophage T4 procapsids. Mol Cell 2007, 25:943-949.
    • (2007) Mol Cell , vol.25 , pp. 943-949
    • Sun, S.1    Kondabagil, K.2    Gentz, P.M.3    Rossmann, M.G.4    Rao, V.B.5
  • 15
    • 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., Grimes S., Smith D.E. Measurements of single DNA molecule packaging dynamics in bacteriophage lambda reveal high forces, high motor processivity, and capsid transformations. J Mol Biol 2007, 373:1113-1122.
    • (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    Grimes, S.7    Smith, D.E.8
  • 16
    • 0042326090 scopus 로고    scopus 로고
    • Mechanism of scaffolding-assisted viral assembly
    • Fane B.A., Prevelige P.E. Mechanism of scaffolding-assisted viral assembly. Adv Protein Chem 2003, 64:259-299.
    • (2003) Adv Protein Chem , vol.64 , pp. 259-299
    • Fane, B.A.1    Prevelige, P.E.2
  • 17
    • 0027320418 scopus 로고
    • Conformational transformations in the protein lattice of phage P22 procapsids
    • Galisteo M.L., King J. Conformational transformations in the protein lattice of phage P22 procapsids. Biophys J 1993, 65:227-235.
    • (1993) Biophys J , vol.65 , pp. 227-235
    • Galisteo, M.L.1    King, J.2
  • 18
    • 0027638730 scopus 로고
    • Conformational change, an alternative energy source?: exothermic phase transition in phage capsid maturation
    • Stevens A. Conformational change, an alternative energy source?: exothermic phase transition in phage capsid maturation. Biophys J 1993, 65:5-6.
    • (1993) Biophys J , vol.65 , pp. 5-6
    • Stevens, A.1
  • 19
    • 0032544102 scopus 로고    scopus 로고
    • Mechanism of capsid maturation in a double-stranded DNA virus
    • Tuma R., Prevelige P.E., Thomas G.J. Mechanism of capsid maturation in a double-stranded DNA virus. Proc Natl Acad Sci U S A 1998, 95:9885-9890.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 9885-9890
    • Tuma, R.1    Prevelige, P.E.2    Thomas, G.J.3
  • 20
    • 0031606857 scopus 로고    scopus 로고
    • Bacteriophage HK97 head assembly: a protein ballet
    • Hendrix R.W., Duda R.L. Bacteriophage HK97 head assembly: a protein ballet. Adv Virus Res 1998, 50:235-288.
    • (1998) Adv Virus Res , vol.50 , pp. 235-288
    • Hendrix, R.W.1    Duda, R.L.2
  • 21
    • 0034703226 scopus 로고    scopus 로고
    • Topologically linked protein rings in the bacteriophage HK97 capsid
    • Wikoff W., Liljas L., Duda R., Tsuruta H., Hendrix R., Johnson J. Topologically linked protein rings in the bacteriophage HK97 capsid. Science 2000, 289:2129-2133.
    • (2000) Science , vol.289 , pp. 2129-2133
    • Wikoff, W.1    Liljas, L.2    Duda, R.3    Tsuruta, H.4    Hendrix, R.5    Johnson, J.6
  • 23
    • 34248384340 scopus 로고    scopus 로고
    • A thermally induced phase transition in a viral capsid transforms the hexamers, leaving the pentamers unchanged
    • Conway J.F., Cheng N., Ross P.D., Hendrix R.W., Duda R.L., Steven A.C. A thermally induced phase transition in a viral capsid transforms the hexamers, leaving the pentamers unchanged. J Struct Biol 2007, 158:224-232.
    • (2007) J Struct Biol , vol.158 , pp. 224-232
    • Conway, J.F.1    Cheng, N.2    Ross, P.D.3    Hendrix, R.W.4    Duda, R.L.5    Steven, A.C.6
  • 28
    • 0028847173 scopus 로고
    • Proteolytic and conformational control of virus capsid maturation: the bacteriophage HK97 system
    • Conway J.F., Duda R.L., Cheng N., Hendrix R.W., Steven A.C. Proteolytic and conformational control of virus capsid maturation: the bacteriophage HK97 system. J Mol Biol 1995, 253:86-99.
    • (1995) J Mol Biol , vol.253 , pp. 86-99
    • Conway, J.F.1    Duda, R.L.2    Cheng, N.3    Hendrix, R.W.4    Steven, A.C.5
  • 29
    • 2942720746 scopus 로고    scopus 로고
    • Evidence that a local refolding event triggers maturation of HK97 bacteriophage capsid
    • Lee K.K., Gan L., Tsuruta H., Hendrix R.W., Duda R.L., Johnson J.E. Evidence that a local refolding event triggers maturation of HK97 bacteriophage capsid. J Mol Biol 2004, 340:419-433.
    • (2004) J Mol Biol , vol.340 , pp. 419-433
    • Lee, K.K.1    Gan, L.2    Tsuruta, H.3    Hendrix, R.W.4    Duda, R.L.5    Johnson, J.E.6
  • 30
    • 60049084630 scopus 로고    scopus 로고
    • Mutational analysis of a conserved glutamic acid required for self-catalyzed cross-linking of bacteriophage HK97 capsids
    • Dierkes L.E., Peebles C.L., Firek B.A., Hendrix R.W., Duda R.L. Mutational analysis of a conserved glutamic acid required for self-catalyzed cross-linking of bacteriophage HK97 capsids. J Virol 2009, 83:2088-2098.
    • (2009) J Virol , vol.83 , pp. 2088-2098
    • Dierkes, L.E.1    Peebles, C.L.2    Firek, B.A.3    Hendrix, R.W.4    Duda, R.L.5
  • 33
    • 32344436397 scopus 로고    scopus 로고
    • Identification of subunit-subunit interactions in bacteriophage P22 procapsids by chemical cross-linking and mass spectrometry
    • Kang S., Hawkridge A.M., Johnson K.L., Muddiman D.C., Prevelige P.E. Identification of subunit-subunit interactions in bacteriophage P22 procapsids by chemical cross-linking and mass spectrometry. J Proteome Res 2006, 5:370-377.
    • (2006) J Proteome Res , vol.5 , pp. 370-377
    • Kang, S.1    Hawkridge, A.M.2    Johnson, K.L.3    Muddiman, D.C.4    Prevelige, P.E.5
  • 34
    • 0032566932 scopus 로고    scopus 로고
    • Electrostatic interactions drive scaffolding/coat protein binding and procapsid maturation in bacteriophage P22
    • Parker M.H., Prevelige P.E. Electrostatic interactions drive scaffolding/coat protein binding and procapsid maturation in bacteriophage P22. Virology 1998, 250:337-349.
    • (1998) Virology , vol.250 , pp. 337-349
    • Parker, M.H.1    Prevelige, P.E.2
  • 35
    • 67650697753 scopus 로고    scopus 로고
    • Structure and energetics of encapsidated DNA in bacteriophage HK97 studied by scanning calorimetry and cryo-electron microscopy
    • Duda R.L., Ross P.D., Cheng N., Firek B.A., Hendrix R.W., Conway J.F., Steven A.C. Structure and energetics of encapsidated DNA in bacteriophage HK97 studied by scanning calorimetry and cryo-electron microscopy. J Mol Biol 2009, 391:471-483.
    • (2009) J Mol Biol , vol.391 , pp. 471-483
    • Duda, R.L.1    Ross, P.D.2    Cheng, N.3    Firek, B.A.4    Hendrix, R.W.5    Conway, J.F.6    Steven, A.C.7
  • 36
    • 0027526593 scopus 로고
    • Characterization of the protease and other products of amino-terminus-proximal cleavage of the herpes simplex virus 1 UL26 protein
    • Liu F., Roizman B. Characterization of the protease and other products of amino-terminus-proximal cleavage of the herpes simplex virus 1 UL26 protein. J Virol 1993, 67:1300-1309.
    • (1993) J Virol , vol.67 , pp. 1300-1309
    • Liu, F.1    Roizman, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.