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Volumn 15, Issue 3, 2009, Pages 391-399

Investigating the specificity and stoichiometry of RNA binding by the nucleocapsid protein of Bunyamwera virus

Author keywords

Bunyamwera; Encapsidation; Replication; RNA; Virus

Indexed keywords

GENOMIC RNA; GUANINE NUCLEOTIDE BINDING PROTEIN; MONOMER; NUCLEOCAPSID PROTEIN; NUCLEOTIDE; PROTEIN; RIBONUCLEOPROTEIN; RNA; VIRUS RNA;

EID: 60849134280     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.1367209     Document Type: Article
Times cited : (26)

References (32)
  • 2
    • 0037708016 scopus 로고    scopus 로고
    • Segment-specific terminal sequences of Bunyamwera bunyavirus regulate genome replication
    • Barr, J.N., Elliott, R.M., Dunn, E.F., and Wertz, G.W. 2003. Segment-specific terminal sequences of Bunyamwera bunyavirus regulate genome replication. Virology 311: 326-338.
    • (2003) Virology , vol.311 , pp. 326-338
    • Barr, J.N.1    Elliott, R.M.2    Dunn, E.F.3    Wertz, G.W.4
  • 3
    • 25144477418 scopus 로고    scopus 로고
    • The Bunyamwera virus mRNA transcription signal resides within both the 3′ and the 5′ terminal regions and allows ambisense transcription from a model RNA segment
    • Barr, J.N., Rodgers, J.W., and Wertz, G.W. 2005. The Bunyamwera virus mRNA transcription signal resides within both the 3′ and the 5′ terminal regions and allows ambisense transcription from a model RNA segment. J. Virol. 79: 12602-12607.
    • (2005) J. Virol , vol.79 , pp. 12602-12607
    • Barr, J.N.1    Rodgers, J.W.2    Wertz, G.W.3
  • 4
    • 0028275669 scopus 로고
    • Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent
    • Baudin, F., Bach, C., Cusack, S., and Ruigrok, R.W. 1994. Structure of influenza virus RNP. I. Influenza virus nucleoprotein melts secondary structure in panhandle RNA and exposes the bases to the solvent. EMBO J. 13: 3158-3165.
    • (1994) EMBO J , vol.13 , pp. 3158-3165
    • Baudin, F.1    Bach, C.2    Cusack, S.3    Ruigrok, R.W.4
  • 5
    • 0024549988 scopus 로고
    • The Sendai virus nucleocapsid exists in at least four different helical states
    • Egelman, E.H., Wu, S.S., Amrein, M., Portner, A., and Murti, G. 1989. The Sendai virus nucleocapsid exists in at least four different helical states. J. Virol. 63: 2233-2243.
    • (1989) J. Virol , vol.63 , pp. 2233-2243
    • Egelman, E.H.1    Wu, S.S.2    Amrein, M.3    Portner, A.4    Murti, G.5
  • 6
    • 0022003385 scopus 로고    scopus 로고
    • Elliott, R.M. 1985. Identification of nonstructural proteins encoded by viruses of the Bunyamwera serogroup (family Bunyaviridae). Virology 143: 119-126.
    • Elliott, R.M. 1985. Identification of nonstructural proteins encoded by viruses of the Bunyamwera serogroup (family Bunyaviridae). Virology 143: 119-126.
  • 7
    • 0024833414 scopus 로고
    • Nucleotide sequence analysis of the large (L) genomic RNA segment of Bunyamwera virus, the prototype of the family Bunyaviridae
    • Elliott, R.M. 1989a. Nucleotide sequence analysis of the large (L) genomic RNA segment of Bunyamwera virus, the prototype of the family Bunyaviridae. Virology 173: 426-436.
    • (1989) Virology , vol.173 , pp. 426-436
    • Elliott, R.M.1
  • 8
    • 0024598099 scopus 로고
    • Nucleotide sequence analysis of the small (S) RNA segment of Bunyamwera virus, the prototype of the family Bunyaviridae
    • Elliott, R.M. 1989b. Nucleotide sequence analysis of the small (S) RNA segment of Bunyamwera virus, the prototype of the family Bunyaviridae. J. Gen. Virol. 70: 1281-1285.
    • (1989) J. Gen. Virol , vol.70 , pp. 1281-1285
    • Elliott, R.M.1
  • 9
    • 0020051973 scopus 로고
    • Identification of virus-coded nonstructural polypeptides in bunyavirus-infected cells
    • Fuller, F. and Bishop, D.H. 1982. Identification of virus-coded nonstructural polypeptides in bunyavirus-infected cells. J. Virol. 41: 643-648.
    • (1982) J. Virol , vol.41 , pp. 643-648
    • Fuller, F.1    Bishop, D.H.2
  • 10
    • 0020966001 scopus 로고
    • Bunyavirus nucleo-protein, N, and a nonstructural protein, NSS, are coded by overlapping reading frames in the S RNA
    • Fuller, F., Bhown, A.S., and Bishop, D.H. 1983. Bunyavirus nucleo-protein, N, and a nonstructural protein, NSS, are coded by overlapping reading frames in the S RNA. J. Gen. Virol. 64: 1705-1714.
    • (1983) J. Gen. Virol , vol.64 , pp. 1705-1714
    • Fuller, F.1    Bhown, A.S.2    Bishop, D.H.3
  • 11
    • 0018357046 scopus 로고
    • M viral RNA segment of bunyaviruses codes for two glycoproteins, G1 and G2
    • Gentsch, J.R. and Bishop, D.L. 1979. M viral RNA segment of bunyaviruses codes for two glycoproteins, G1 and G2. J. Virol. 30: 767-770.
    • (1979) J. Virol , vol.30 , pp. 767-770
    • Gentsch, J.R.1    Bishop, D.L.2
  • 12
    • 33746516378 scopus 로고    scopus 로고
    • Structure of the vesicular stomatitis virus nucleoprotein-RNA complex
    • Green, T.J., Zhang, X., Wertz, G.W., and Luo, M. 2006. Structure of the vesicular stomatitis virus nucleoprotein-RNA complex. Science 313: 357-360.
    • (2006) Science , vol.313 , pp. 357-360
    • Green, T.J.1    Zhang, X.2    Wertz, G.W.3    Luo, M.4
  • 13
    • 0035196816 scopus 로고    scopus 로고
    • Sendai virus genome synthesis and assembly are coupled: A possible mechanism to promote viral RNA polymerase processivity
    • Gubbay, O., Curran, J., and Kolakofsky, D. 2001. Sendai virus genome synthesis and assembly are coupled: A possible mechanism to promote viral RNA polymerase processivity. J. Gen. Virol. 82: 2895-2903.
    • (2001) J. Gen. Virol , vol.82 , pp. 2895-2903
    • Gubbay, O.1    Curran, J.2    Kolakofsky, D.3
  • 14
    • 0024469581 scopus 로고
    • La Crosse virus nucleocapsid protein controls its own synthesis in mosquito cells by encapsidating its mRNA
    • Hacker, D., Raju, R., and Kolakofsky, D. 1989. La Crosse virus nucleocapsid protein controls its own synthesis in mosquito cells by encapsidating its mRNA. J. Virol. 63: 5166-5174.
    • (1989) J. Virol , vol.63 , pp. 5166-5174
    • Hacker, D.1    Raju, R.2    Kolakofsky, D.3
  • 15
    • 0025146960 scopus 로고
    • Anti-mRNAs in La Crosse bunyavirus-infected cells
    • Hacker, D., Rochat, S., and Kolakofsky, D. 1990. Anti-mRNAs in La Crosse bunyavirus-infected cells. J. Virol. 64: 5051-5057.
    • (1990) J. Virol , vol.64 , pp. 5051-5057
    • Hacker, D.1    Rochat, S.2    Kolakofsky, D.3
  • 16
    • 0033965262 scopus 로고    scopus 로고
    • Structure of the RNA inside the vesicular stomatitis virus nucleocapsid
    • Iseni, F., Baudin, F., Blondel, D., and Ruigrok, R.W. 2000. Structure of the RNA inside the vesicular stomatitis virus nucleocapsid. RNA 6: 270-281.
    • (2000) RNA , vol.6 , pp. 270-281
    • Iseni, F.1    Baudin, F.2    Blondel, D.3    Ruigrok, R.W.4
  • 17
    • 0036675180 scopus 로고    scopus 로고
    • Chemical modification of nucleotide bases and mRNA editing depend on hexamer or nucleoprotein phase in Sendai virus nucleocapsids
    • Iseni, F., Baudin, F., Garcin, D., Marq, J.B., Ruigrok, R.W., and Kolakofsky, D. 2002. Chemical modification of nucleotide bases and mRNA editing depend on hexamer or nucleoprotein phase in Sendai virus nucleocapsids. RNA 8: 1056-1067.
    • (2002) RNA , vol.8 , pp. 1056-1067
    • Iseni, F.1    Baudin, F.2    Garcin, D.3    Marq, J.B.4    Ruigrok, R.W.5    Kolakofsky, D.6
  • 18
    • 26444539802 scopus 로고    scopus 로고
    • Homotypic interaction of Bunyamwera virus nucleocapsid protein
    • Leonard, V.H., Kohl, A., Osborne, J.C., McLees, A., and Elliott, R.M. 2005. Homotypic interaction of Bunyamwera virus nucleocapsid protein. J. Virol. 79: 13166-13172.
    • (2005) J. Virol , vol.79 , pp. 13166-13172
    • Leonard, V.H.1    Kohl, A.2    Osborne, J.C.3    McLees, A.4    Elliott, R.M.5
  • 19
    • 3242713982 scopus 로고    scopus 로고
    • Trimeric hantavirus nucleo-capsid protein binds specifically to the viral RNA panhandle
    • Mir, M.A. and Panganiban, A.T. 2004. Trimeric hantavirus nucleo-capsid protein binds specifically to the viral RNA panhandle. J. Virol. 78: 8281-8288.
    • (2004) J. Virol , vol.78 , pp. 8281-8288
    • Mir, M.A.1    Panganiban, A.T.2
  • 20
    • 13744250185 scopus 로고    scopus 로고
    • The hantavirus nucleocapsid protein recognizes specific features of the viral RNA panhandle and is altered in conformation upon RNA binding
    • Mir, M.A. and Panganiban, A.T. 2005. The hantavirus nucleocapsid protein recognizes specific features of the viral RNA panhandle and is altered in conformation upon RNA binding. J. Virol. 79: 1824-1835.
    • (2005) J. Virol , vol.79 , pp. 1824-1835
    • Mir, M.A.1    Panganiban, A.T.2
  • 21
    • 0024974913 scopus 로고
    • Visualization of protein-nucleic acid interactions in a virus. Refined structure of intact tobacco mosaic virus at 2.9 Å resolution by x-ray fiber diffraction
    • Namba, K., Pattanayek, R., and Stubbs, G. 1989. Visualization of protein-nucleic acid interactions in a virus. Refined structure of intact tobacco mosaic virus at 2.9 Å resolution by x-ray fiber diffraction. J. Mol. Biol. 208: 307-325.
    • (1989) J. Mol. Biol , vol.208 , pp. 307-325
    • Namba, K.1    Pattanayek, R.2    Stubbs, G.3
  • 22
    • 0032889247 scopus 로고    scopus 로고
    • Functional coupling between replication and packaging of polio- virus replicon RNA
    • Nugent, C.I., Johnson, K.L., Sarnow, P., and Kirkegaard, K. 1999. Functional coupling between replication and packaging of polio- virus replicon RNA. J. Virol. 73: 427-435.
    • (1999) J. Virol , vol.73 , pp. 427-435
    • Nugent, C.I.1    Johnson, K.L.2    Sarnow, P.3    Kirkegaard, K.4
  • 23
    • 17644443084 scopus 로고    scopus 로고
    • Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification
    • Ortega, J., Martin-Benito, J., Zurcher, T., Valpuesta, J.M., Carrascosa, J.L., and Ortin, J. 2000. Ultrastructural and functional analyses of recombinant influenza virus ribonucleoproteins suggest dimerization of nucleoprotein during virus amplification. J. Virol. 74: 156-163.
    • (2000) J. Virol , vol.74 , pp. 156-163
    • Ortega, J.1    Martin-Benito, J.2    Zurcher, T.3    Valpuesta, J.M.4    Carrascosa, J.L.5    Ortin, J.6
  • 24
    • 0033771070 scopus 로고    scopus 로고
    • RNA binding properties of Bunyamwera virus nucleocapsid protein and selective binding to an element in the 5′ terminus of the negative-sense S segment
    • Osborne, J.C. and Elliott, R.M. 2000. RNA binding properties of Bunyamwera virus nucleocapsid protein and selective binding to an element in the 5′ terminus of the negative-sense S segment. J. Virol. 74: 9946-9952.
    • (2000) J. Virol , vol.74 , pp. 9946-9952
    • Osborne, J.C.1    Elliott, R.M.2
  • 25
    • 33645785092 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary x-ray crystallographic analysis of the nucleocapsid protein of Bunyamwera virus
    • Rodgers, J.W., Zhou, Q., Green, T.J., Barr, J.N., and Luo, M. 2006. Purification, crystallization and preliminary x-ray crystallographic analysis of the nucleocapsid protein of Bunyamwera virus. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62: 361-364.
    • (2006) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun , vol.62 , pp. 361-364
    • Rodgers, J.W.1    Zhou, Q.2    Green, T.J.3    Barr, J.N.4    Luo, M.5
  • 26
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck, P. 2000. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys. J. 78: 1606-1619.
    • (2000) Biophys. J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 27
    • 0035127603 scopus 로고    scopus 로고
    • cis-Acting signals in encapsidation of Hantaan virus S-segment viral genomic RNA by its N protein
    • Severson, W.E., Xu, X., and Jonsson, C.B. 2001. cis-Acting signals in encapsidation of Hantaan virus S-segment viral genomic RNA by its N protein. J. Virol. 75: 2646-2652.
    • (2001) J. Virol , vol.75 , pp. 2646-2652
    • Severson, W.E.1    Xu, X.2    Jonsson, C.B.3
  • 28
    • 1642368109 scopus 로고    scopus 로고
    • Analysis of heterologous interacting systems by sedimentation velocity: Curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants
    • Stafford, W.F. and Sherwood, P.J. 2004. Analysis of heterologous interacting systems by sedimentation velocity: Curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants. Biophys. Chem. 108: 231-243.
    • (2004) Biophys. Chem , vol.108 , pp. 231-243
    • Stafford, W.F.1    Sherwood, P.J.2
  • 29
    • 0027960331 scopus 로고
    • Crystal structure of an RNA bacteriophage coat protein-operator complex
    • Valegard, K., Murray, J.B., Stockley, P.G., Stonehouse, N.J., and Liljas, L. 1994. Crystal structure of an RNA bacteriophage coat protein-operator complex. Nature 371: 623-626.
    • (1994) Nature , vol.371 , pp. 623-626
    • Valegard, K.1    Murray, J.B.2    Stockley, P.G.3    Stonehouse, N.J.4    Liljas, L.5
  • 30
    • 18144391518 scopus 로고    scopus 로고
    • Capsid protein synthesis from replicating RNA directs specific packaging of the genome of a multipartite, positive-strand RNA virus
    • Venter, P.A., Krishna, N.K., and Schneemann, A. 2005. Capsid protein synthesis from replicating RNA directs specific packaging of the genome of a multipartite, positive-strand RNA virus. J. Virol. 79: 6239-6248.
    • (2005) J. Virol , vol.79 , pp. 6239-6248
    • Venter, P.A.1    Krishna, N.K.2    Schneemann, A.3
  • 31
    • 33845890539 scopus 로고    scopus 로고
    • The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA
    • Ye, Q., Krug, R.M., and Tao, Y.J. 2006. The mechanism by which influenza A virus nucleoprotein forms oligomers and binds RNA. Nature 444: 1078-1082.
    • (2006) Nature , vol.444 , pp. 1078-1082
    • Ye, Q.1    Krug, R.M.2    Tao, Y.J.3
  • 32
    • 0042121256 scopus 로고    scopus 로고
    • Mfold web server for nucleic acid folding and hybridization prediction
    • Zuker, M. 2003. Mfold web server for nucleic acid folding and hybridization prediction. Nucleic Acids Res. 31: 3406-3415.
    • (2003) Nucleic Acids Res , vol.31 , pp. 3406-3415
    • Zuker, M.1


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