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Volumn 108, Issue 4, 2011, Pages 1373-1378

Atomic model of a cypovirus built from cryo-EM structure provides insight into the mechanism of mRNA capping

Author keywords

[No Author keywords available]

Indexed keywords

2' O METHYLTRANSFERASE; 7 N METHYLTRANSFERASE; GUANYLYLTRANSFERASE; MESSENGER RNA; PROTEIN VP1; TRANSFERASE; UNCLASSIFIED DRUG;

EID: 79952178436     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1014995108     Document Type: Article
Times cited : (64)

References (45)
  • 1
    • 1542328804 scopus 로고    scopus 로고
    • The dsRNA viruses
    • Mertens P (2004) The dsRNA viruses. Virus Res 101:3-13.
    • (2004) Virus Res , vol.101 , pp. 3-13
    • Mertens, P.1
  • 2
    • 0034720237 scopus 로고    scopus 로고
    • Structure of the reovirus core at 3.6 Å resolution
    • DOI 10.1038/35010041
    • Reinisch KM, Nibert M, Harrison SC (2000) Structure of the reovirus core at 3.6 Å resolution. Nature 404:960-967. (Pubitemid 30243583)
    • (2000) Nature , vol.404 , Issue.6781 , pp. 960-967
    • Reinisch, K.M.1    Nibert, M.L.2    Harrison, S.C.3
  • 3
    • 0025320720 scopus 로고
    • Active site localization in a viral mRNA capping enzyme
    • Fausnaugh J, Shatkin AJ (1990) Active site localization in a viral mRNA capping enzyme. J Biol Chem 265:7669-7672.
    • (1990) J Biol Chem , vol.265 , pp. 7669-7672
    • Fausnaugh, J.1    Shatkin, A.J.2
  • 4
    • 0034723208 scopus 로고    scopus 로고
    • Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein lambda2
    • DOI 10.1074/jbc.275.4.2804
    • Luongo CL, Reinisch KM, Harrison SC, Nibert ML (2000) Identification of the guanylyltransferase region and active site in reovirus mRNA capping protein lambda 2. J Biol Chem 275:2804-2810. (Pubitemid 30082052)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.4 , pp. 2804-2810
    • Luongo, C.L.1    Reinisch, K.M.2    Harrison, S.C.3    Nibert, M.L.4
  • 5
    • 0032508690 scopus 로고    scopus 로고
    • Binding site for S-adenosyl-L-methionine in a central region of mammalian reovirus lambda2 protein. Evidence for activities in mRNA cap methylation
    • DOI 10.1074/jbc.273.37.23773
    • Luongo CL, Contreras CM, Farsetta DL, Nibert ML (1998) Binding site for S-adenosyl-Lmethionine in a central region of mammalian reovirus lambda 2 protein - Evidence for activities in mRNA CAP methylation. J Biol Chem 273:23773-23780. (Pubitemid 28435710)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.37 , pp. 23773-23780
    • Luongo, C.L.1    Contreras, C.M.2    Farsetta, D.L.3    Nibert, M.L.4
  • 6
    • 43749092377 scopus 로고    scopus 로고
    • 3.88 Å structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy
    • DOI 10.1038/nature06893, PII NATURE06893
    • Yu XK, Jin L, Zhou ZH (2008) 3.88 Å structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy. Nature 453:415-419. (Pubitemid 351693126)
    • (2008) Nature , vol.453 , Issue.7193 , pp. 415-419
    • Yu, X.1    Jin, L.2    Zhou, Z.H.3
  • 7
    • 55549091725 scopus 로고    scopus 로고
    • Structural evolution of Reoviridae revealed by Oryzavirus in acquiring the second capsid shell
    • Miyazaki N, et al. (2008) Structural evolution of Reoviridae revealed by Oryzavirus in acquiring the second capsid shell. J Virol 82:11344-11353.
    • (2008) J Virol , vol.82 , pp. 11344-11353
    • Miyazaki, N.1
  • 8
    • 77951912692 scopus 로고    scopus 로고
    • 3.3 Å Cryo-EM structure of a non-enveloped virus reveals a priming mechanism for cell entry
    • Zhang X, Jin L, Fang Q, Hui WH, Zhou ZH (2010) 3.3 Å Cryo-EM structure of a non-enveloped virus reveals a priming mechanism for cell entry. Cell 141:472-482.
    • (2010) Cell , vol.141 , pp. 472-482
    • Zhang, X.1    Jin, L.2    Fang, Q.3    Hui, W.H.4    Zhou, Z.H.5
  • 9
    • 77649336015 scopus 로고    scopus 로고
    • Backbone model of an Aquareovirus virion by Cryo-electron microscopy and bioinformatics
    • Cheng LP, et al. (2010) Backbone model of an Aquareovirus virion by Cryo-electron microscopy and bioinformatics. J Mol Biol 397:852-863.
    • (2010) J Mol Biol , vol.397 , pp. 852-863
    • Cheng, L.P.1
  • 11
    • 0142134875 scopus 로고    scopus 로고
    • CPV, a stable and symmetrical machine for mRNA synthesis
    • DOI 10.1016/S0969-2126(03)00099-6
    • Nibert ML, Baker TS (2003) CPV, a stable and symmetrical machine for mRNA synthesis. Structure 11:605-607. (Pubitemid 37281172)
    • (2003) Structure , vol.11 , Issue.6 , pp. 605-607
    • Nibert, M.L.1    Baker, T.S.2
  • 14
    • 79952134753 scopus 로고    scopus 로고
    • Cypovirus structure at 8 Å by electron cryomicroscopy - Structural basis of capsid stability and multifunctional RNA processing apparatus
    • Zhou ZH, Zhang H, Jakana J, Lu XY, Zhang JQ (2003) Cypovirus structure at 8 Å by electron cryomicroscopy - Structural basis of capsid stability and multifunctional RNA processing apparatus. Biophys J 84:281a.
    • (2003) Biophys J , vol.84
    • Zhou, Z.H.1    Zhang, H.2    Jakana, J.3    Lu, X.Y.4    Zhang, J.Q.5
  • 15
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • DOI 10.1016/j.jmb.2003.07.013
    • Rosenthal PB, Henderson R (2003) Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J Mol Biol 333:721-745. (Pubitemid 37268015)
    • (2003) Journal of Molecular Biology , vol.333 , Issue.4 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 16
    • 0141960927 scopus 로고    scopus 로고
    • Cytoplasmic polyhedrosis virus structure at 8 Å by electron cryomicroscopy: Structural basis of capsid stability and mRNA processing regulation
    • DOI 10.1016/S0969-2126(03)00091-1
    • Zhou ZH, Zhang H, Jakana J, Lu XY, Zhang JQ (2003) Cytoplasmic polyhedrosis virus structure at 8 Å by electron cryomicroscopy: Structural basis of capsid stability and mRNA processing regulation. Structure 11:651-663. (Pubitemid 37281181)
    • (2003) Structure , vol.11 , Issue.6 , pp. 651-663
    • Zhou, Z.H.1    Zhang, H.2    Jakana, J.3    Lu, X.-Y.4    Zhang, J.-Q.5
  • 17
    • 0037428437 scopus 로고    scopus 로고
    • Structural comparisons of empty and full cytoplasmic polyhedrosis virus: Protein-RNA interactions and implications for endogenous RNA transcription mechanism
    • DOI 10.1074/jbc.M205964200
    • Xia Q, Jakana J, Zhang JQ, Zhou ZH (2003) Structural comparisons of empty and full cytoplasmic polyhedrosis virus - Protein-RNA interactions and implications for endogenous RNA transcription mechanism. J Biol Chem 278:1094-1100. (Pubitemid 36790789)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.2 , pp. 1094-1100
    • Xia, Q.1    Jakana, J.2    Zhang, J.-Q.3    Zhou, Z.H.4
  • 19
    • 77349116567 scopus 로고    scopus 로고
    • X-ray crystal structure of the Rotavirus inner capsid particle at 3.8 Å resolution
    • McClain B, Settembre E, Temple BRS, Bellamy AR, Harrison SC (2010) X-ray crystal structure of the Rotavirus inner capsid particle at 3.8 Å resolution. J Mol Biol 397:587-599.
    • (2010) J Mol Biol , vol.397 , pp. 587-599
    • McClain, B.1    Settembre, E.2    Temple, B.R.S.3    Bellamy, A.R.4    Harrison, S.C.5
  • 20
    • 49349112116 scopus 로고    scopus 로고
    • Subnanometer-resolution structures of the grass carp reovirus core and virion
    • Cheng LP, Fang Q, Shah S, Atanasov IC, Zhou ZH (2008) Subnanometer-resolution structures of the grass carp reovirus core and virion. J Mol Biol 382:213-222.
    • (2008) J Mol Biol , vol.382 , pp. 213-222
    • Cheng, L.P.1    Fang, Q.2    Shah, S.3    Atanasov, I.C.4    Zhou, Z.H.5
  • 22
    • 0037169362 scopus 로고    scopus 로고
    • Structure of the reovirus membrane-penetration protein, mu1, in a complex with its protector protein, sigma3
    • DOI 10.1016/S0092-8674(02)00612-8
    • Liemann S, Chandran K, Baker TS, Nibert ML, Harrison SC (2002) Structure of the reovirus membrane-penetration protein,mu 1, in a complex with its protector protein, sigma 3. Cell 108:283-295. (Pubitemid 34161147)
    • (2002) Cell , vol.108 , Issue.2 , pp. 283-295
    • Liemann, S.1    Chandran, K.2    Baker, T.S.3    Nibert, M.L.4    Harrison, S.C.5
  • 24
    • 0042353701 scopus 로고    scopus 로고
    • Assembly into single-shelled virus-like particles by major capsid protein VP1 encoded by genome segment S1 of Bombyx mori cypovirus 1
    • DOI 10.1099/vir.0.19216-0
    • Hagiwara K, Naitow H (2003) Assembly into single-shelled virus-like particles by major capsid protein VP1 encoded by genome segment S1 of Bombyx mori cypovirus 1. J Gen Virol 84:2439-2441. (Pubitemid 37063133)
    • (2003) Journal of General Virology , vol.84 , Issue.9 , pp. 2439-2441
    • Hagiwara, K.1    Naitow, H.2
  • 25
    • 0036889158 scopus 로고    scopus 로고
    • The hydrophilic amino-terminal arm of reovirus core shell protein lambda1 is dispensable for particle assembly
    • DOI 10.1128/JVI.76.23.12211-12222.2002
    • Kim J, et al. (2002) The hydrophilic amino-terminal arm of reovirus core shell protein lambda 1 is dispensable for particle assembly. J Virol 76:12211-12222. (Pubitemid 35304318)
    • (2002) Journal of Virology , vol.76 , Issue.23 , pp. 12211-12222
    • Kim, J.1    Zhang, X.2    Centonze, V.E.3    Bowman, V.D.4    Noble, S.5    Baker, T.S.6    Nibert, M.L.7
  • 26
    • 0031259835 scopus 로고    scopus 로고
    • Molecular dissection of the reovirus lambda 1 protein nucleic acids binding site
    • DOI 10.1016/S0168-1702(97)00092-0, PII S0168170297000920
    • Bisaillon M, Lemay G (1997) Molecular dissection of the reovirus lambda 1 protein nucleic acids binding site. Virus Res 51:231-237. (Pubitemid 27483596)
    • (1997) Virus Research , vol.51 , Issue.2 , pp. 231-237
    • Bisaillon, M.1    Lemay, G.2
  • 27
    • 0030800967 scopus 로고    scopus 로고
    • Characterization of the nucleoside triphosphate phosphohydrolase and helicase activities of the reovirus lambda1 protein
    • DOI 10.1074/jbc.272.29.18298
    • Bisaillon M, Bergeron J, Lemay G (1997) Characterization of the nucleoside triphosphate phosphohydrolase and helicase activities of the reovirus lambda 1 protein. J Biol Chem 272:18298-18303. (Pubitemid 27306420)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.29 , pp. 18298-18303
    • Bisaillon, M.1    Bergeron, J.2    Lemay, G.3
  • 28
    • 34548567464 scopus 로고    scopus 로고
    • Genetic variation of the lambdaA and lambdaC protein encoding genes of avian reoviruses
    • DOI 10.1016/j.rvsc.2007.01.002, PII S0034528807000069
    • Shen PC, et al. (2007) Genetic variation of the lambda A and lambda C protein encoding genes of avian reoviruses. Res Vet Sci 83:394-402. (Pubitemid 47393436)
    • (2007) Research in Veterinary Science , vol.83 , Issue.3 , pp. 394-402
    • Shen, P.C.1    Chiou, Y.F.2    Liu, H.J.3    Song, C.H.4    Su, Y.P.5    Lee, L.H.6
  • 29
    • 0033602711 scopus 로고    scopus 로고
    • Mammalian reovirus L3 gene sequences and evidence for a distinct amino- Terminal region of the lambda1 protein
    • DOI 10.1006/viro.1999.9707
    • Harrison SJ, et al. (1999) Mammalian reovirus L3 gene sequences and evidence for a distinct amino-terminal region of the lambda 1 protein. Virology 258:54-64. (Pubitemid 29391780)
    • (1999) Virology , vol.258 , Issue.1 , pp. 54-64
    • Harrison, S.J.1    Farsetta, D.L.2    Kim, J.3    Noble, S.4    Broering, T.J.5    Nibert, M.L.6
  • 30
    • 0035012982 scopus 로고    scopus 로고
    • STRAP: Editor for STRuctural alignments of proteins
    • Gille C, Frommel C (2001) STRAP: Editor for STRuctural Alignments of Proteins. Bioinformatics 17:377-378. (Pubitemid 32421936)
    • (2001) Bioinformatics , vol.17 , Issue.4 , pp. 377-378
    • Gille, C.1    Frommel, C.2
  • 31
    • 0345059374 scopus 로고    scopus 로고
    • Reovirus polymerase lambda3 localized by cryo-electron microscopy of virions at a resolution of 7.6 Å
    • DOI 10.1038/nsb1009
    • Zhang X, Walker SB, Chipman PR, Nibert ML, Baker TS (2003) Reovirus polymerase lambda 3 localized by cryo-electron microscopy of virions at a resolution of 7.6 Å. Nat Struct Biol 10:1011-1018. (Pubitemid 37500493)
    • (2003) Nature Structural Biology , vol.10 , Issue.12 , pp. 1011-1018
    • Zhang, X.1    Walker, S.B.2    Chipman, P.R.3    Nibert, M.L.4    Baker, T.S.5
  • 32
    • 0017141875 scopus 로고
    • Mechanism of formation of Reovirus messenger-RNA 5′-terminal blocked and methylated sequence, M7gpppgmpc
    • Furuichi Y, Muthukrishnan S, Tomasz J, Shatkin AJ (1976) Mechanism of formation of Reovirus messenger-RNA 5′-terminal blocked and methylated sequence, M7gpppgmpc. J Biol Chem 251:5043-5053.
    • (1976) J Biol Chem , vol.251 , pp. 5043-5053
    • Furuichi, Y.1    Muthukrishnan, S.2    Tomasz, J.3    Shatkin, A.J.4
  • 33
    • 0035036348 scopus 로고    scopus 로고
    • Complete in vitro assembly of the reovirus outer capsid produces highly infectious particles suitable for genetic studies of the receptor-binding protein
    • DOI 10.1128/JVI.75.11.5335-5342.2001
    • Chandran K, et al. (2001) Complete in vitro assembly of the reovirus outer capsid produces highly infectious particles suitable for genetic studies of the receptor-binding protein. J Virol 75:5335-5342. (Pubitemid 32448555)
    • (2001) Journal of Virology , vol.75 , Issue.11 , pp. 5335-5342
    • Chandran, K.1    Zhang, X.2    Olson, N.H.3    Walker, S.B.4    Chappell, J.D.5    Dermody, T.S.6    Baker, T.S.7    Nibert, M.L.8
  • 34
    • 0027162058 scopus 로고
    • Early steps in Reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation - Analysis of virions and subviral particles by cryoelectron microscopy and image-reconstruction
    • Dryden KA, et al. (1993) Early steps in Reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation - analysis of virions and subviral particles by cryoelectron microscopy and image-reconstruction. J Cell Biol 122:1023-1041.
    • (1993) J Cell Biol , vol.122 , pp. 1023-1041
    • Dryden, K.A.1
  • 35
    • 0033919812 scopus 로고    scopus 로고
    • Trypsin-induced structural transformation in aquareovirus
    • DOI 10.1128/JVI.74.14.6546-6555.2000
    • Nason EL, Samal SK, Prasad BVV (2000) Trypsin-induced structural transformation in aquareovirus. J Virol 74:6546-6555. (Pubitemid 30429823)
    • (2000) Journal of Virology , vol.74 , Issue.14 , pp. 6546-6555
    • Nason, E.L.1    Samal, S.K.2    Prasad, B.V.V.3
  • 36
    • 0034108895 scopus 로고    scopus 로고
    • Nucleotide sequences of genome segments 6 and 7 of Bombyx mori cypovirus 1, encoding the viral structural proteins V4 and V5, respectively
    • Hagiwara K, Matsumoto T (2000) Nucleotide sequences of genome segments 6 and 7 of Bombyx mori cypovirus 1, encoding the viral structural proteins V4 and V5, respectively. J Gen Virol 81:1143-1147. (Pubitemid 30189657)
    • (2000) Journal of General Virology , vol.81 , Issue.4 , pp. 1143-1147
    • Hagiwara, K.1    Matsumoto, T.2
  • 37
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • DOI 10.1006/jsbi.1999.4174
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: Semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128:82-97. (Pubitemid 30013436)
    • (1999) Journal of Structural Biology , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 38
    • 0036420061 scopus 로고    scopus 로고
    • IMIRS: A high-resolution 3D reconstruction package integrated with a relational image database
    • DOI 10.1016/S1047-8477(02)00014-X, PII S104784770200014X
    • Liang YY, Ke EY, Zhou ZH (2002) IMIRS: a high-resolution 3D reconstruction package integrated with a relational image database. J Struct Biol 137:292-304. (Pubitemid 35304474)
    • (2002) Journal of Structural Biology , vol.137 , Issue.3 , pp. 292-304
    • Liang, Y.1    Ke, E.Y.2    Zhou, Z.H.3
  • 39
    • 0029924120 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of icosahedral particles - The uncommon line
    • Fuller SD, Butcher SJ, Cheng RH, Baker TS (1996) Three-dimensional reconstruction of icosahedral particles - The uncommon line. J Struct Biol 116:48-55.
    • (1996) J Struct Biol , vol.116 , pp. 48-55
    • Fuller, S.D.1    Butcher, S.J.2    Cheng, R.H.3    Baker, T.S.4
  • 40
    • 37349116067 scopus 로고    scopus 로고
    • Symmetry-adapted spherical harmonics method for high-resolution 3D single-particle reconstructions
    • Liu HR, et al. (2008) Symmetry-adapted spherical harmonics method for high-resolution 3D single-particle reconstructions. J Struct Biol 161:64-73.
    • (2008) J Struct Biol , vol.161 , pp. 64-73
    • Liu, H.R.1
  • 42
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger AT, et al. (1998) Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr D 54:905-921.
    • (1998) Acta Crystallogr D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 43
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • DOI 10.1006/jmbi.1993.1351
    • Laskowski RA, Moss DS, Thornton JM (1993) Main-chain bond lengths and bond angles in protein structures. J Mol Biol 231:1049-1067. (Pubitemid 23209879)
    • (1993) Journal of Molecular Biology , vol.231 , Issue.4 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 44
    • 34547592557 scopus 로고    scopus 로고
    • MolProbity: All-atom contacts and structure validation for proteins and nucleic acids
    • Davis IW, et al. (2007) MolProbity: All-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 35:W375-W383.
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1
  • 45
    • 4444221565 scopus 로고    scopus 로고
    • UCSF chimera - A visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF chimera - A visualization system for exploratory research and analysis. J Comput Chem 25:1605-1612.
    • (2004) J Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1


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