메뉴 건너뛰기




Volumn 22, Issue 1, 2012, Pages 65-71

Nucleic acid packaging in viruses

Author keywords

[No Author keywords available]

Indexed keywords

CAPSID PROTEIN; DOUBLE STRANDED DNA; SINGLE STRANDED DNA; SINGLE STRANDED RNA;

EID: 84862804467     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2011.11.002     Document Type: Review
Times cited : (81)

References (54)
  • 1
    • 33749462736 scopus 로고    scopus 로고
    • The structural and functional role of RNA in icosahedral virus assembly
    • Schneemann A. The structural and functional role of RNA in icosahedral virus assembly. Annu Rev Microbiol 2006, 60:51-67.
    • (2006) Annu Rev Microbiol , vol.60 , pp. 51-67
    • Schneemann, A.1
  • 2
    • 79960420311 scopus 로고    scopus 로고
    • Virus particle structure: nonenveloped viruses
    • Elsevier, B.W.J. Mahy, M.H.V. van Regenmortel (Eds.)
    • Speir J.A., Johnson JE Virus particle structure: nonenveloped viruses. Encyclopedia of Virology 2008, 380-393. Elsevier. edn 3. B.W.J. Mahy, M.H.V. van Regenmortel (Eds.).
    • (2008) Encyclopedia of Virology , pp. 380-393
    • Speir, J.A.1    Johnson, J.E.2
  • 3
    • 79551684299 scopus 로고    scopus 로고
    • Structure of Hibiscus latent Singapore virus by fiber diffraction: a nonconserved His122 contributes to coat protein stability
    • Tewary S.K., Oda T., Kendall A., Bian W., Stubbs G., Wong S.M., Swaminathan K. Structure of Hibiscus latent Singapore virus by fiber diffraction: a nonconserved His122 contributes to coat protein stability. J Mol Biol 2011, 406:516-526.
    • (2011) J Mol Biol , vol.406 , pp. 516-526
    • Tewary, S.K.1    Oda, T.2    Kendall, A.3    Bian, W.4    Stubbs, G.5    Wong, S.M.6    Swaminathan, K.7
  • 5
    • 79952424137 scopus 로고    scopus 로고
    • Access to RNA encapsidated in the nucleocapsid of vesicular stomatitis virus
    • Green T.J., Rowse M., Tsao J., Kang J., Ge P., Zhou Z.H., Luo M. Access to RNA encapsidated in the nucleocapsid of vesicular stomatitis virus. J Virol 2011, 85:2714-2722.
    • (2011) J Virol , vol.85 , pp. 2714-2722
    • Green, T.J.1    Rowse, M.2    Tsao, J.3    Kang, J.4    Ge, P.5    Zhou, Z.H.6    Luo, M.7
  • 6
    • 33746516378 scopus 로고    scopus 로고
    • Structure of the vesicular stomatitis virus nucleoprotein-RNA complex
    • Green T.J., Zhang X., Wertz G.W., Luo M. Structure of the vesicular stomatitis virus nucleoprotein-RNA complex. Science 2006, 313:357-360.
    • (2006) Science , vol.313 , pp. 357-360
    • Green, T.J.1    Zhang, X.2    Wertz, G.W.3    Luo, M.4
  • 7
    • 77955348510 scopus 로고    scopus 로고
    • Structure of the Rift Valley fever virus nucleocapsid protein reveals another architecture for RNA encapsidation
    • Raymond D.D., Piper M.E., Gerrard S.R., Smith J.L. Structure of the Rift Valley fever virus nucleocapsid protein reveals another architecture for RNA encapsidation. Proc Natl Acad Sci U S A 2010, 107:11769-11774.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 11769-11774
    • Raymond, D.D.1    Piper, M.E.2    Gerrard, S.R.3    Smith, J.L.4
  • 8
    • 67749094714 scopus 로고    scopus 로고
    • The structure of bacteriophage phiCb5 reveals a role of the RNA genome and metal ions in particle stability and assembly
    • Plevka P., Kazaks A., Voronkova T., Kotelovica S., Dishlers A., Liljas L., Tars K. The structure of bacteriophage phiCb5 reveals a role of the RNA genome and metal ions in particle stability and assembly. J Mol Biol 2009, 391:635-647.
    • (2009) J Mol Biol , vol.391 , pp. 635-647
    • Plevka, P.1    Kazaks, A.2    Voronkova, T.3    Kotelovica, S.4    Dishlers, A.5    Liljas, L.6    Tars, K.7
  • 9
    • 37849019313 scopus 로고    scopus 로고
    • Structural basis for the coevolution of a viral RNA-protein complex
    • Chao J.A., Patskovsky Y., Almo S.C., Singer R.H. Structural basis for the coevolution of a viral RNA-protein complex. Nat Struct Mol Biol 2008, 15:103-105.
    • (2008) Nat Struct Mol Biol , vol.15 , pp. 103-105
    • Chao, J.A.1    Patskovsky, Y.2    Almo, S.C.3    Singer, R.H.4
  • 10
    • 0025344593 scopus 로고
    • The three-dimensional structure of the bacterial virus MS2
    • Valegard K., Liljas L., Fridborg K., Unge T. The three-dimensional structure of the bacterial virus MS2. Nature 1990, 345:36-41.
    • (1990) Nature , vol.345 , pp. 36-41
    • Valegard, K.1    Liljas, L.2    Fridborg, K.3    Unge, T.4
  • 13
    • 77953579261 scopus 로고    scopus 로고
    • Evolution in action: N and C termini of subunits in related T=4 viruses exchange roles as molecular switches
    • Speir J.A., Taylor D.J., Natarajan P., Pringle F.M., Ball L.A., Johnson J.E. Evolution in action: N and C termini of subunits in related T=4 viruses exchange roles as molecular switches. Structure 2010, 18:700-709.
    • (2010) Structure , vol.18 , pp. 700-709
    • Speir, J.A.1    Taylor, D.J.2    Natarajan, P.3    Pringle, F.M.4    Ball, L.A.5    Johnson, J.E.6
  • 14
    • 77950789977 scopus 로고    scopus 로고
    • Structure and function of a genetically engineered mimic of a nonenveloped virus entry intermediate
    • Banerjee M., Speir J.A., Kwan M.H., Huang R., Aryanpur P.P., Bothner B., Johnson J.E. Structure and function of a genetically engineered mimic of a nonenveloped virus entry intermediate. J Virol 2010, 84:4737-4746.
    • (2010) J Virol , vol.84 , pp. 4737-4746
    • Banerjee, M.1    Speir, J.A.2    Kwan, M.H.3    Huang, R.4    Aryanpur, P.P.5    Bothner, B.6    Johnson, J.E.7
  • 15
    • 0027518457 scopus 로고
    • Ordered duplex RNA controls capsid architecture in an icosahedral animal virus
    • Fisher A.J., Johnson J.E. Ordered duplex RNA controls capsid architecture in an icosahedral animal virus. Nature 1993, 361:176-179.
    • (1993) Nature , vol.361 , pp. 176-179
    • Fisher, A.J.1    Johnson, J.E.2
  • 16
    • 0030576341 scopus 로고    scopus 로고
    • The 2.8Å structure of a T=4 animal virus and its implications for membrane translocation of RNA
    • Munshi S., Liljas L., Cavarelli J., Bomu W., McKinney B., Reddy V., Johnson J.E. The 2.8Å structure of a T=4 animal virus and its implications for membrane translocation of RNA. J Mol Biol 1996, 261:1-10.
    • (1996) J Mol Biol , vol.261 , pp. 1-10
    • Munshi, S.1    Liljas, L.2    Cavarelli, J.3    Bomu, W.4    McKinney, B.5    Reddy, V.6    Johnson, J.E.7
  • 17
    • 29144442284 scopus 로고    scopus 로고
    • Preliminary X-ray characterization of authentic Providence virus and attempts to express its coat protein gene in recombinant baculovirus
    • Taylor D.J., Speir J.A., Reddy V., Cingolani G., Pringle F.M., Ball L.A., Johnson J.E. Preliminary X-ray characterization of authentic Providence virus and attempts to express its coat protein gene in recombinant baculovirus. Arch Virol 2006, 151:155-165.
    • (2006) Arch Virol , vol.151 , pp. 155-165
    • Taylor, D.J.1    Speir, J.A.2    Reddy, V.3    Cingolani, G.4    Pringle, F.M.5    Ball, L.A.6    Johnson, J.E.7
  • 18
    • 0035909370 scopus 로고    scopus 로고
    • The bacteriophage phi29 portal motor can package DNA against a large internal force
    • Smith D.E., Tans S.J., Smith S.B., Grimes S., Anderson D.L., Bustamante C. The bacteriophage phi29 portal motor can package DNA against a large internal force. Nature 2001, 413:748-752.
    • (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
  • 19
    • 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
  • 20
    • 36749028241 scopus 로고    scopus 로고
    • Single phage T4 DNA packaging motors exhibit large force generation, high velocity, and dynamic variability
    • Fuller D.N, Raymer D.M., Kottadiel V.I., Rao V.B., Smith D.E. Single phage T4 DNA packaging motors exhibit large force generation, high velocity, and dynamic variability. Proc Natl Acad Sci U S A 2007, 104:16868-16873.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 16868-16873
    • Fuller, D.N.1    Raymer, D.M.2    Kottadiel, V.I.3    Rao, V.B.4    Smith, D.E.5
  • 22
    • 11244340515 scopus 로고    scopus 로고
    • Measurements of DNA lengths remaining in a viral capsid after osmotically suppressed partial ejection
    • Evilevitch A., Gober J.W., Phillips M., Knobler C.M., Gelbart W.M. Measurements of DNA lengths remaining in a viral capsid after osmotically suppressed partial ejection. Biophys J 2005, 88:751-756.
    • (2005) Biophys J , vol.88 , pp. 751-756
    • Evilevitch, A.1    Gober, J.W.2    Phillips, M.3    Knobler, C.M.4    Gelbart, W.M.5
  • 24
    • 63449094990 scopus 로고    scopus 로고
    • Virology. Pressurized viruses
    • Gelbart W.M., Knobler C.M. Virology. Pressurized viruses. Science 2009, 323:1682-1683.
    • (2009) Science , vol.323 , pp. 1682-1683
    • Gelbart, W.M.1    Knobler, C.M.2
  • 25
    • 75849141082 scopus 로고    scopus 로고
    • Gp15 and gp16 cooperate in translocating bacteriophage T7 DNA into the infected cell
    • Chang C.Y., Kemp P., Molineux I.J. Gp15 and gp16 cooperate in translocating bacteriophage T7 DNA into the infected cell. Virology 2010, 398:176-186.
    • (2010) Virology , vol.398 , pp. 176-186
    • Chang, C.Y.1    Kemp, P.2    Molineux, I.J.3
  • 26
    • 79551502787 scopus 로고    scopus 로고
    • Dynamics of bacteriophage genome ejection in vitro and in vivo
    • Panja D., Molineux I.J. Dynamics of bacteriophage genome ejection in vitro and in vivo. Phys Biol 2010, 7:045006.
    • (2010) Phys Biol , vol.7 , pp. 045006
    • Panja, D.1    Molineux, I.J.2
  • 27
    • 34147123766 scopus 로고    scopus 로고
    • DNA packaging and delivery machines in tailed bacteriophages
    • Johnson J.E., Chiu W. DNA packaging and delivery machines in tailed bacteriophages. Curr Opin Struct Biol 2007, 17:237-243.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 237-243
    • Johnson, J.E.1    Chiu, W.2
  • 28
    • 35148817067 scopus 로고    scopus 로고
    • The conformation of double-stranded DNA inside bacteriophages depends on capsid size and shape
    • Petrov A.S., Boz M.B., Harvey S.C. The conformation of double-stranded DNA inside bacteriophages depends on capsid size and shape. J Struct Biol 2007, 160:241-248.
    • (2007) J Struct Biol , vol.160 , pp. 241-248
    • Petrov, A.S.1    Boz, M.B.2    Harvey, S.C.3
  • 29
    • 33846113838 scopus 로고    scopus 로고
    • Structural and thermodynamic principles of viral packaging
    • Petrov A.S., Harvey S.C. Structural and thermodynamic principles of viral packaging. Structure 2007, 15:21-27.
    • (2007) Structure , vol.15 , pp. 21-27
    • Petrov, A.S.1    Harvey, S.C.2
  • 30
    • 47749092360 scopus 로고    scopus 로고
    • Packaging double-helical DNA into viral capsids: structures, forces, and energetics
    • Petrov A.S., Harvey S.C. Packaging double-helical DNA into viral capsids: structures, forces, and energetics. Biophys J 2008, 95:497-502.
    • (2008) Biophys J , vol.95 , pp. 497-502
    • Petrov, A.S.1    Harvey, S.C.2
  • 31
    • 79952437811 scopus 로고    scopus 로고
    • Role of DNA-DNA interactions on the structure and thermodynamics of bacteriophages Lambda and P4
    • Petrov A.S., Harvey S.C. Role of DNA-DNA interactions on the structure and thermodynamics of bacteriophages Lambda and P4. J Struct Biol 2011, 174:137-146.
    • (2011) J Struct Biol , vol.174 , pp. 137-146
    • Petrov, A.S.1    Harvey, S.C.2
  • 32
    • 34447260515 scopus 로고    scopus 로고
    • Packaging of DNA by bacteriophage epsilon15: structure, forces, and thermodynamics
    • Petrov A.S., Lim-Hing K., Harvey S.C. Packaging of DNA by bacteriophage epsilon15: structure, forces, and thermodynamics. Structure 2007, 15:807-812.
    • (2007) Structure , vol.15 , pp. 807-812
    • Petrov, A.S.1    Lim-Hing, K.2    Harvey, S.C.3
  • 37
    • 84862908674 scopus 로고    scopus 로고
    • Herpesvirus capsid assembly: insights from structural analysis
    • Brown J.C., Newcomb W.W. Herpesvirus capsid assembly: insights from structural analysis. Curr Opin Virol 2011, 1:142-149.
    • (2011) Curr Opin Virol , vol.1 , pp. 142-149
    • Brown, J.C.1    Newcomb, W.W.2
  • 38
    • 26444561955 scopus 로고    scopus 로고
    • Control of adenovirus packaging
    • Ostapchuk P., Hearing P. Control of adenovirus packaging. J Cell Biochem 2005, 96:25-35.
    • (2005) J Cell Biochem , vol.96 , pp. 25-35
    • Ostapchuk, P.1    Hearing, P.2
  • 40
    • 72949097270 scopus 로고    scopus 로고
    • Purification of adenoviral vectors by combined anion exchange and gel filtration chromatography
    • Eglon M.N., Duffy A.M., O'Brien T., Strappe P.M. Purification of adenoviral vectors by combined anion exchange and gel filtration chromatography. J Gene Med 2009, 11:978-989.
    • (2009) J Gene Med , vol.11 , pp. 978-989
    • Eglon, M.N.1    Duffy, A.M.2    O'Brien, T.3    Strappe, P.M.4
  • 42
    • 2442686734 scopus 로고    scopus 로고
    • The structure of a thermophilic archeal virus shows a dsDNA viral capsid type that spans all domains of life
    • Rice G., Tang L., Stedman K., Roberto F., Johnson J.E., Douglas T., Young M.J. The structure of a thermophilic archeal virus shows a dsDNA viral capsid type that spans all domains of life. Proc Natl Acad Sci U S A 2004, 101:7716-7720.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 7716-7720
    • Rice, G.1    Tang, L.2    Stedman, K.3    Roberto, F.4    Johnson, J.E.5    Douglas, T.6    Young, M.J.7
  • 44
    • 0031238076 scopus 로고    scopus 로고
    • Persistence length of single-stranded DNA
    • Tinland B.A.P., Sturm J., Weil G. Persistence length of single-stranded DNA. Macromolecules 1997, 30:5763-5765.
    • (1997) Macromolecules , vol.30 , pp. 5763-5765
    • Tinland, B.A.P.1    Sturm, J.2    Weil, G.3
  • 45
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews B.W. Solvent content of protein crystals. J Mol Biol 1968, 33:491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 46
    • 33744811672 scopus 로고    scopus 로고
    • Cryo-EM asymmetric reconstruction of bacteriophage P22 reveals organization of its DNA packaging and infecting machinery
    • Chang J., Weigele P., King J., Chiu W., Jiang W. Cryo-EM asymmetric reconstruction of bacteriophage P22 reveals organization of its DNA packaging and infecting machinery. Structure 2006, 14:1073-1082.
    • (2006) Structure , vol.14 , pp. 1073-1082
    • Chang, J.1    Weigele, P.2    King, J.3    Chiu, W.4    Jiang, W.5
  • 48
    • 39849102970 scopus 로고    scopus 로고
    • Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy
    • Jiang W., Baker M.L., Jakana J., Weigele P.R., King J., Chiu W. Backbone structure of the infectious epsilon15 virus capsid revealed by electron cryomicroscopy. Nature 2008, 451:1130-1134.
    • (2008) Nature , vol.451 , pp. 1130-1134
    • Jiang, W.1    Baker, M.L.2    Jakana, J.3    Weigele, P.R.4    King, J.5    Chiu, W.6
  • 49
    • 31844435708 scopus 로고    scopus 로고
    • Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus
    • Jiang W., Chang J., Jakana J., Weigele P., King J., Chiu W. Structure of epsilon15 bacteriophage reveals genome organization and DNA packaging/injection apparatus. Nature 2006, 439:612-616.
    • (2006) Nature , vol.439 , pp. 612-616
    • Jiang, W.1    Chang, J.2    Jakana, J.3    Weigele, P.4    King, J.5    Chiu, W.6
  • 54
    • 33746931256 scopus 로고    scopus 로고
    • Bacteriophage T5 structure reveals similarities with HK97 and T4 suggesting evolutionary relationships
    • Effantin G., Boulanger P., Neumann E., Letellier L., Conway J.F. Bacteriophage T5 structure reveals similarities with HK97 and T4 suggesting evolutionary relationships. J Mol Biol 2006, 361:993-1002.
    • (2006) J Mol Biol , vol.361 , pp. 993-1002
    • Effantin, G.1    Boulanger, P.2    Neumann, E.3    Letellier, L.4    Conway, J.F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.