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Volumn 414, Issue 2, 2011, Pages 260-271

Stepwise expansion of the bacteriophage φ6 procapsid: Possible packaging intermediates

Author keywords

capsid; cryo electron microscopy; Cystoviridae; segmented genome; virus

Indexed keywords

SODIUM CHLORIDE; VIRUS RNA;

EID: 81355160170     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.10.004     Document Type: Article
Times cited : (25)

References (38)
  • 1
    • 1542268889 scopus 로고    scopus 로고
    • Packaging, replication and recombination of the segmented genomes of bacteriophage Φ6 and its relatives
    • DOI 10.1016/j.virusres.2003.12.008, PII S0168170203003721
    • Mindich L. Packaging, replication and recombination of the segmented genome of bacteriophage φ6 and its relatives Virus Res. 101 2004 83 92 (Pubitemid 38317111)
    • (2004) Virus Research , vol.101 , Issue.1 , pp. 83-92
    • Mindich, L.1
  • 2
    • 79952101724 scopus 로고    scopus 로고
    • Assortment and packaging of the segmented rotavirus genome
    • McDonald S.M., and Patton J.T. Assortment and packaging of the segmented rotavirus genome Trends Microbiol. 19 2011 136 144
    • (2011) Trends Microbiol. , vol.19 , pp. 136-144
    • McDonald, S.M.1    Patton, J.T.2
  • 4
    • 77958569432 scopus 로고    scopus 로고
    • Structure of influenza virus ribonucleoprotein complexes and their packaging into virions
    • Noda T., and Kawaoka Y. Structure of influenza virus ribonucleoprotein complexes and their packaging into virions Rev. Med. Virol. 20 2010 380 391
    • (2010) Rev. Med. Virol. , vol.20 , pp. 380-391
    • Noda, T.1    Kawaoka, Y.2
  • 5
    • 0023278327 scopus 로고
    • The nucleocapsid of the lipid-containing double-stranded RNA bacteriophage Φ6 contains a protein skeleton consisting of a single polypeptide species
    • Olkkonen V.M., and Bamford D.H. The nucleocapsid of the lipid-containing double-stranded RNA bacteriophage phi 6 contains a protein skeleton consisting of a single polypeptide species J. Virol. 61 1987 2362 2367 (Pubitemid 17097546)
    • (1987) Journal of Virology , vol.61 , Issue.8 , pp. 2362-2367
    • Olkkonen, V.M.1    Bamford, B.H.2
  • 6
    • 0024314726 scopus 로고
    • Tentative identification of RNA-dependent RNA polymerase of dsRNA viruses and their relationship to positive strand RNA viral polymerases
    • DOI 10.1016/0014-5793(89)80886-5
    • Koonin E.V., Gorbalenya A.E., and Chumakov K.M. Tentative identification of RNA-dependent RNA polymerases of dsRNA viruses and their relationship to positive strand RNA viral polymerases FEBS Lett. 252 1989 42 46 (Pubitemid 19201073)
    • (1989) FEBS Letters , vol.252 , Issue.1-2 , pp. 42-46
    • Koonin, E.V.1    Gorbalenya, A.E.2    Chumakov, K.M.3
  • 7
    • 0028928032 scopus 로고
    • In vitro packaging of the single-stranded RNA genomic precursors of the segmented double-stranded RNA bacteriophage phi 6: The three segments modulate each other's packaging efficiency
    • Frilander M., and Bamford D.H. In vitro packaging of the single-stranded RNA genomic precursors of the segmented double-stranded RNA bacteriophage phi 6: the three segments modulate each other's packaging efficiency J. Mol. Biol. 246 1995 418 428
    • (1995) J. Mol. Biol. , vol.246 , pp. 418-428
    • Frilander, M.1    Bamford, D.H.2
  • 8
    • 0028805187 scopus 로고
    • Double-stranded RNA bacteriophage phi 6 protein P4 is an unspecific nucleoside triphosphatase activated by calcium ions
    • Paatero A.O., Syvaoja J.E., and Bamford D.H. Double-stranded RNA bacteriophage phi 6 protein P4 is an unspecific nucleoside triphosphatase activated by calcium ions J. Virol. 69 1995 6729 6734
    • (1995) J. Virol. , vol.69 , pp. 6729-6734
    • Paatero, A.O.1    Syvaoja, J.E.2    Bamford, D.H.3
  • 9
    • 0029060842 scopus 로고
    • RNA binding, packaging and polymerase activities of the different incomplete polymerase complex particles of dsRNA bacteriophage phi 6
    • Juuti J.T., and Bamford D.H. RNA binding, packaging and polymerase activities of the different incomplete polymerase complex particles of dsRNA bacteriophage phi 6 J. Mol. Biol. 249 1995 545 554
    • (1995) J. Mol. Biol. , vol.249 , pp. 545-554
    • Juuti, J.T.1    Bamford, D.H.2
  • 10
    • 0030887625 scopus 로고    scopus 로고
    • Stoichiometric packaging of the three genomic segments of double-stranded RNA bacteriophage φ6
    • Qiao X., Qiao J., and Mindich L. Stoichiometric packaging of the three genomic segments of double-stranded RNA bacteriophage φ6 Proc. Natl Acad. Sci. USA 94 1997 4074 4079
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 4074-4079
    • Qiao, X.1    Qiao, J.2    Mindich, L.3
  • 11
    • 0026627864 scopus 로고
    • Dependence of minus-strand synthesis on complete genomic packaging in the double-stranded RNA bacteriophage phi 6
    • Frilander M., Gottlieb P., Strassman J., Bamford D.H., and Mindich L. Dependence of minus-strand synthesis on complete genomic packaging in the double-stranded RNA bacteriophage phi 6 J. Virol. 66 1992 5013 5017
    • (1992) J. Virol. , vol.66 , pp. 5013-5017
    • Frilander, M.1    Gottlieb, P.2    Strassman, J.3    Bamford, D.H.4    Mindich, L.5
  • 12
    • 0033007294 scopus 로고    scopus 로고
    • Precise packaging of the three genomic segments of the double- stranded- RNA bacteriophage φ6
    • Mindich L. Precise packaging of the three genomic segments of the double-stranded-RNA bacteriophage φ6 Microbiol. Mol. Biol. Rev. 63 1999 149 160 (Pubitemid 29116090)
    • (1999) Microbiology and Molecular Biology Reviews , vol.63 , Issue.1 , pp. 149-160
    • Mindich, L.1
  • 13
    • 0030872369 scopus 로고    scopus 로고
    • Intermediates in the assembly pathway of the double-stranded RNA virus φ6
    • DOI 10.1093/emboj/16.14.4477
    • Butcher S.J., Dokland T., Ojala P.M., Bamford D.H., and Fuller S.D. Intermediates in the assembly pathway of the double-stranded RNA virus φ6 EMBO J. 16 1997 4477 4487 (Pubitemid 27298201)
    • (1997) EMBO Journal , vol.16 , Issue.14 , pp. 4477-4487
    • Butcher, S.J.1    Dokland, T.2    Ojala, P.M.3    Bamford, D.H.4    Fuller, S.D.5
  • 14
    • 0029330856 scopus 로고
    • The large genome segment of dsRNA bacteriophage φ6 is the key regulator in the in vitro minus and plus strand synthesis
    • Frilander M., Poranen M., and Bamford D.H. The large genome segment of dsRNA bacteriophage φ6 is the key regulator in the in vitro minus and plus strand synthesis RNA 1 1995 510 518
    • (1995) RNA , vol.1 , pp. 510-518
    • Frilander, M.1    Poranen, M.2    Bamford, D.H.3
  • 15
    • 0035002345 scopus 로고    scopus 로고
    • Self-assembly of a viral molecular machine from purified protein and RNA constituents
    • DOI 10.1016/S1097-2765(01)00228-3
    • Poranen M.M., Paatero A.O., Tuma R., and Bamford D.H. Self-assembly of a viral molecular machine from purified protein and RNA constituents Mol. Cell 7 2001 845 854 (Pubitemid 32436444)
    • (2001) Molecular Cell , vol.7 , Issue.4 , pp. 845-854
    • Poranen, M.M.1    Paatero, A.O.2    Tuma, R.3    Bamford, D.H.4
  • 18
    • 77649128082 scopus 로고    scopus 로고
    • P22 coat protein structures reveal a novel mechanism for capsid maturation: Stability without auxiliary proteins or chemical crosslinks
    • Parent K.N., Khayat R., Tu L.H., Suhanovsky M.M., Cortines J.R., and Teschke C.M. P22 coat protein structures reveal a novel mechanism for capsid maturation: stability without auxiliary proteins or chemical crosslinks Structure 18 2010 390 401
    • (2010) Structure , vol.18 , pp. 390-401
    • Parent, K.N.1    Khayat, R.2    Tu, L.H.3    Suhanovsky, M.M.4    Cortines, J.R.5    Teschke, C.M.6
  • 19
    • 0142245619 scopus 로고    scopus 로고
    • Analysis of Specific Binding Involved in Genomic Packaging of the Double-Stranded-RNA Bacteriophage φ6
    • DOI 10.1128/JB.185.21.6409-6414.2003
    • Qiao X., Qiao J., and Mindich L. Analysis of specific binding involved in genomic packaging of the double-stranded-RNA bacteriophage φ6 J. Bacteriol. 185 2003 6409 6414 (Pubitemid 37305541)
    • (2003) Journal of Bacteriology , vol.185 , Issue.21 , pp. 6409-6414
    • Qiao, X.1    Qiao, J.2    Mindich, L.3
  • 20
    • 45549097253 scopus 로고    scopus 로고
    • Initial location of the RNA-dependent RNA polymerase in the bacteriophage φ6 procapsid determined by cryo-electron microscopy
    • Sen A., Heymann J.B., Cheng N., Qiao J., Mindich L., and Steven A.C. Initial location of the RNA-dependent RNA polymerase in the bacteriophage φ6 procapsid determined by cryo-electron microscopy J. Biol. Chem. 283 2008 12227 12231
    • (2008) J. Biol. Chem. , vol.283 , pp. 12227-12231
    • Sen, A.1    Heymann, J.B.2    Cheng, N.3    Qiao, J.4    Mindich, L.5    Steven, A.C.6
  • 21
    • 0027320418 scopus 로고
    • Conformational transformations in the protein lattice of phage P22 procapsids
    • Galisteo M.L., and King J. Conformational transformations in the protein lattice of phage P22 procapsids Biophys. J. 65 1993 227 235 (Pubitemid 23206056)
    • (1993) Biophysical Journal , vol.65 , Issue.1 , pp. 227-235
    • Galisteo, M.L.1    King, J.2
  • 22
    • 17044437232 scopus 로고    scopus 로고
    • Crosslinking renders bacteriophage HK97 capsid maturation irreversible and effects an essential stabilization
    • DOI 10.1038/sj.emboj.7600613
    • Ross P.D., Cheng N., Conway J.F., Firek B.A., Hendrix R.W., Duda R.L., and Steven A.C. Crosslinking renders bacteriophage HK97 capsid maturation irreversible and effects an essential stabilization EMBO J. 24 2005 1352 1363 (Pubitemid 40593056)
    • (2005) EMBO Journal , vol.24 , Issue.7 , pp. 1352-1363
    • Ross, P.D.1    Cheng, N.2    Conway, J.F.3    Firek, B.A.4    Hendrix, R.W.5    Duda, R.L.6    Steven, A.C.7
  • 23
    • 0033607480 scopus 로고    scopus 로고
    • A symmetry mismatch at the site of RNA packaging in the polymerase complex of dsRNA bacteriophage φ6
    • de Haas F., Paatero A.O., Mindich L., Bamford D.H., and Fuller S.D. A symmetry mismatch at the site of RNA packaging in the polymerase complex of dsRNA bacteriophage φ6 J. Mol. Biol. 294 1999 357 372
    • (1999) J. Mol. Biol. , vol.294 , pp. 357-372
    • De Haas, F.1    Paatero, A.O.2    Mindich, L.3    Bamford, D.H.4    Fuller, S.D.5
  • 24
    • 77955085566 scopus 로고    scopus 로고
    • Cryo-electron tomography of bacteriophage φ6 procapsids shows random occupancy of the binding sites for RNA polymerase and packaging NTPase
    • Nemecek D., Heymann J.B., Qiao J., Mindich L., and Steven A.C. Cryo-electron tomography of bacteriophage φ6 procapsids shows random occupancy of the binding sites for RNA polymerase and packaging NTPase J. Struct. Biol. 171 2010 389 396
    • (2010) J. Struct. Biol. , vol.171 , pp. 389-396
    • Nemecek, D.1    Heymann, J.B.2    Qiao, J.3    Mindich, L.4    Steven, A.C.5
  • 25
    • 55249085352 scopus 로고    scopus 로고
    • The role of host protein YajQ in the temporal control of transcription in bacteriophage φ6
    • Qiao X., Sun Y., Qiao J., and Mindich L. The role of host protein YajQ in the temporal control of transcription in bacteriophage φ6 Proc. Natl Acad. Sci. USA 105 2008 15956 15960
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 15956-15960
    • Qiao, X.1    Sun, Y.2    Qiao, J.3    Mindich, L.4
  • 26
    • 33744821066 scopus 로고    scopus 로고
    • Structure of the Bacteriophage φ{symbol}6 Nucleocapsid Suggests a Mechanism for Sequential RNA Packaging
    • DOI 10.1016/j.str.2006.03.018, PII S096921260600219X
    • Huiskonen J.T., de Haas F., Bubeck D., Bamford D.H., Fuller S.D., and Butcher S.J. Structure of the bacteriophage φ6 nucleocapsid suggests a mechanism for sequential RNA packaging Structure 14 2006 1039 1048 (Pubitemid 43831662)
    • (2006) Structure , vol.14 , Issue.6 , pp. 1039-1048
    • Huiskonen, J.T.1    De Haas, F.2    Bubeck, D.3    Bamford, D.H.4    Fuller, S.D.5    Butcher, S.J.6
  • 28
    • 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., and Steven A.C. Structure and energetics of encapsidated DNA in bacteriophage HK97 studied by scanning calorimetry and cryo-electron microscopy J. Mol. Biol. 391 2009 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
  • 29
    • 34248583632 scopus 로고    scopus 로고
    • Allosteric Signaling and a Nuclear Exit Strategy: Binding of UL25/UL17 Heterodimers to DNA-Filled HSV-1 Capsids
    • DOI 10.1016/j.molcel.2007.04.010, PII S1097276507002250
    • Trus B.L., Newcomb W.W., Cheng N., Cardone G., Marekov L., and Homa F.L. Allosteric signaling and a nuclear exit strategy: binding of UL25/UL17 heterodimers to DNA-filled HSV-1 capsids Mol. Cell 26 2007 479 489 (Pubitemid 46765180)
    • (2007) Molecular Cell , vol.26 , Issue.4 , pp. 479-489
    • Trus, B.L.1    Newcomb, W.W.2    Cheng, N.3    Cardone, G.4    Marekov, L.5    Homa, F.L.6    Brown, J.C.7    Steven, A.C.8
  • 30
    • 0037767481 scopus 로고    scopus 로고
    • Isolation and analysis of mutants of double-stranded-RNA bacteriophage φ6 with altered packaging specificity
    • DOI 10.1128/JB.185.15.4572-4577.2003
    • Qiao J., Qiao X., Sun Y., and Mindich L. Isolation and analysis of mutants of double-stranded-RNA bacteriophage φ6 with altered packaging specificity J. Bacteriol. 185 2003 4572 4577 (Pubitemid 36890505)
    • (2003) Journal of Bacteriology , vol.185 , Issue.15 , pp. 4572-4577
    • Qiao, J.1    Qiao, X.2    Sun, Y.3    Mindich, L.4
  • 31
    • 1342300740 scopus 로고    scopus 로고
    • Construction of carrier state viruses with partial genomes of the segmented dsRNA bacteriophages
    • DOI 10.1016/j.virol.2003.10.022
    • Sun Y., Qiao X., and Mindich L. Construction of carrier state viruses with partial genomes of the segmented dsRNA bacteriophages Virology 319 2004 274 279 (Pubitemid 38251268)
    • (2004) Virology , vol.319 , Issue.2 , pp. 274-279
    • Sun, Y.1    Qiao, X.2    Mindich, L.3
  • 32
    • 33845336533 scopus 로고    scopus 로고
    • Bsoft: Image processing and molecular modeling for electron microscopy
    • DOI 10.1016/j.jsb.2006.06.006, PII S1047847706001997, Software Tools for Macromolecular Microscopy
    • Heymann J.B., and Belnap D.M. Bsoft: image processing and molecular modeling for electron microscopy J. Struct. Biol. 157 2007 3 18 (Pubitemid 44880789)
    • (2007) Journal of Structural Biology , vol.157 , Issue.1 , pp. 3-18
    • Heymann, J.B.1    Belnap, D.M.2
  • 33
    • 4344664583 scopus 로고    scopus 로고
    • Molecular dynamics of protein complexes from four-dimensional cryo-electron microscopy
    • DOI 10.1016/j.jsb.2004.02.006, PII S1047847704000425
    • Heymann J.B., Conway J.F., and Steven A.C. Molecular dynamics of protein complexes from four-dimensional cryo-electron microscopy J. Struct. Biol. 147 2004 291 301 (Pubitemid 39140736)
    • (2004) Journal of Structural Biology , vol.147 , Issue.3 , pp. 291-301
    • Heymann, J.B.1    Conway, J.F.2    Steven, A.C.3
  • 35
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • DOI 10.1016/j.jsb.2005.07.007, PII S1047847705001528
    • Mastronarde D.N. Automated electron microscope tomography using robust prediction of specimen movements J. Struct. Biol. 152 2005 36 51 (Pubitemid 41384176)
    • (2005) Journal of Structural Biology , vol.152 , Issue.1 , pp. 36-51
    • Mastronarde, D.N.1
  • 36
    • 40649123787 scopus 로고    scopus 로고
    • Computational resources for cryo-electron tomography in Bsoft
    • DOI 10.1016/j.jsb.2007.08.002, PII S1047847707001773
    • Heymann J.B., Cardone G., Winkler D.C., and Steven A.C. Computational resources for cryo-electron tomography in Bsoft J. Struct. Biol. 161 2008 232 242 (Pubitemid 351375091)
    • (2008) Journal of Structural Biology , vol.161 , Issue.3 , pp. 232-242
    • Heymann, J.B.1    Cardone, G.2    Winkler, D.C.3    Steven, A.C.4
  • 37
    • 0035783287 scopus 로고    scopus 로고
    • Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion
    • Frangakis A.S., and Hegerl R. Noise reduction in electron tomographic reconstructions using nonlinear anisotropic diffusion J. Struct. Biol. 135 2001 239 250
    • (2001) J. Struct. Biol. , vol.135 , pp. 239-250
    • Frangakis, A.S.1    Hegerl, R.2
  • 38
    • 23044510524 scopus 로고    scopus 로고
    • A resolution criterion for electron tomography based on cross-validation
    • DOI 10.1016/j.jsb.2005.04.006, PII S1047847705001085
    • Cardone G., Grünewald K., and Steven A.C. A resolution criterion for electron tomography based on cross-validation J. Struct. Biol. 151 2005 117 129 (Pubitemid 41074821)
    • (2005) Journal of Structural Biology , vol.151 , Issue.2 , pp. 117-129
    • Cardone, G.1    Grunewald, K.2    Steven, A.C.3


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