메뉴 건너뛰기




Volumn 84, Issue 4, 2010, Pages 2169-2175

Coronavirus nucleocapsid protein facilitates template switching and is required for efficient transcription

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; COMPLEMENTARY DNA; DOUBLE STRANDED DNA; GLUTATHIONE TRANSFERASE; NUCLEIC ACID; NUCLEOCAPSID PROTEIN; RIBOZYME; SINGLE STRANDED DNA; VIRUS RNA;

EID: 75449101470     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.02011-09     Document Type: Article
Times cited : (162)

References (36)
  • 1
    • 7644242097 scopus 로고    scopus 로고
    • The nucleoprotein is required for efficient coronavirus genome replication
    • Almazan, F., C. Galan, and L. Enjuanes. 2004. The nucleoprotein is required for efficient coronavirus genome replication. J. Virol. 78:12683-12688.
    • (2004) J. Virol , vol.78 , pp. 12683-12688
    • Almazan, F.1    Galan, C.2    Enjuanes, L.3
  • 3
    • 34147113199 scopus 로고    scopus 로고
    • Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA
    • Chen, C. Y., C. Chang, Y. W. Chang, S. C. Sue, H. Bai, L. Riang, C. D. Hsiao, and T. Huang. 2007. Structure of the SARS coronavirus nucleocapsid protein RNA-binding dimerization domain suggests a mechanism for helical packaging of viral RNA. J. Mol. Biol. 368:1075-1086.
    • (2007) J. Mol. Biol , vol.368 , pp. 1075-1086
    • Chen, C.Y.1    Chang, C.2    Chang, Y.W.3    Sue, S.C.4    Bai, H.5    Riang, L.6    Hsiao, C.D.7    Huang, T.8
  • 5
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H. J., and P. E. Wright. 2005. Intrinsically unstructured proteins and their functions. Nat. Rev. 6:197-208.
    • (2005) Nat. Rev , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 6
    • 33750333638 scopus 로고    scopus 로고
    • Biochemical aspects of coronavirus replication and virus-host interaction
    • Enjuanes, L., F. Almazan, I. Sola, and S. Zuñiga. 2006. Biochemical aspects of coronavirus replication and virus-host interaction. Annu. Rev. Microbiol. 60:211-230.
    • (2006) Annu. Rev. Microbiol , vol.60 , pp. 211-230
    • Enjuanes, L.1    Almazan, F.2    Sola, I.3    Zuñiga, S.4
  • 7
    • 84883273220 scopus 로고    scopus 로고
    • The Nidovirales
    • B. W. J. Mahy, M. Van Regenmortel, P. Walker, and D. Majumder-Russell ed, 3rd ed. Elsevier Ltd, Oxford, United Kingdom
    • Enjuanes, L., A. E. Gorbalenya, R. J. de Groot, J. A. Cowley, J. Ziebuhr, and E. J. Snijder. 2008. The Nidovirales, p. 419-430. In B. W. J. Mahy, M. Van Regenmortel, P. Walker, and D. Majumder-Russell (ed.), Encyclopedia of virology, 3rd ed. Elsevier Ltd., Oxford, United Kingdom.
    • (2008) Encyclopedia of virology , pp. 419-430
    • Enjuanes, L.1    Gorbalenya, A.E.2    de Groot, R.J.3    Cowley, J.A.4    Ziebuhr, J.5    Snijder, E.J.6
  • 8
    • 59749091822 scopus 로고    scopus 로고
    • Coronavirus RNA synthesis: Transcription
    • V. Thiel ed, Caister Academic Press, Norfolk, United Kingdom
    • Enjuanes, L., I. Sola, S. Zuñiga, and J. L. Moreno. 2007. Coronavirus RNA synthesis: transcription, p. 81-107. In V. Thiel (ed.), Coronaviruses: molecular and cellular biology. Caister Academic Press, Norfolk, United Kingdom.
    • (2007) Coronaviruses: Molecular and cellular biology , pp. 81-107
    • Enjuanes, L.1    Sola, I.2    Zuñiga, S.3    Moreno, J.L.4
  • 9
    • 28844505975 scopus 로고    scopus 로고
    • The nucleocapsid protein of coronavirus infectious bronchitis virus: Crystal structure of its N-terminal domain and multimerization properties
    • Fan, H., A. Ooi, Y. W. Tan, S. Wang, S. Fang, D. X. Liu, and J. Lescar. 2005. The nucleocapsid protein of coronavirus infectious bronchitis virus: crystal structure of its N-terminal domain and multimerization properties. Structure 13:1859-1868.
    • (2005) Structure , vol.13 , pp. 1859-1868
    • Fan, H.1    Ooi, A.2    Tan, Y.W.3    Wang, S.4    Fang, S.5    Liu, D.X.6    Lescar, J.7
  • 11
    • 0031007620 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 nucleocapsid protein promotes efficient strand transfer and specific viral DNA synthesis by inhibiting TAR-dependent self-priming from minus-strand strong-stop DNA
    • Guo, J., L. E. Henderson, J. Bess, B. Kane, and J. G. Levin. 1997. Human immunodeficiency virus type 1 nucleocapsid protein promotes efficient strand transfer and specific viral DNA synthesis by inhibiting TAR-dependent self-priming from minus-strand strong-stop DNA. J. Virol. 71:5178-5188.
    • (1997) J. Virol , vol.71 , pp. 5178-5188
    • Guo, J.1    Henderson, L.E.2    Bess, J.3    Kane, B.4    Levin, J.G.5
  • 12
    • 0029163563 scopus 로고
    • RNA chaperones and the RNA folding problem
    • Herschlag, D. 1995. RNA chaperones and the RNA folding problem. J. Biol. Chem. 270:20871-20874.
    • (1995) J. Biol. Chem , vol.270 , pp. 20871-20874
    • Herschlag, D.1
  • 14
    • 39449097872 scopus 로고    scopus 로고
    • RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae
    • Ivanyi-Nagy, R., J. Lavergne, C. Gabus, D. Ficheux, and J. Darlix. 2008. RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. Nucleic Acids Res. 36:2618-2633.
    • (2008) Nucleic Acids Res , vol.36 , pp. 2618-2633
    • Ivanyi-Nagy, R.1    Lavergne, J.2    Gabus, C.3    Ficheux, D.4    Darlix, J.5
  • 15
    • 23144448275 scopus 로고    scopus 로고
    • Nucleic acid chaperone activity of HIV-1 nucleocapsid protein: Critical role in reverse transcription and molecular mechanism
    • Levin, J. G., J. Guo, I. Rouzina, and K. Musier-Forsyth. 2005. Nucleic acid chaperone activity of HIV-1 nucleocapsid protein: critical role in reverse transcription and molecular mechanism. Prog. Nucleic. Acids Res. Mol. Biol. 80:217-286.
    • (2005) Prog. Nucleic. Acids Res. Mol. Biol , vol.80 , pp. 217-286
    • Levin, J.G.1    Guo, J.2    Rouzina, I.3    Musier-Forsyth, K.4
  • 17
    • 0033957603 scopus 로고    scopus 로고
    • High affinity interaction between nucleocapsid protein and leader/intergenic sequence of mouse hepatitis virus RNA
    • Nelson, G. W., S. A. Stohlman, and S. M. Tahara. 2000. High affinity interaction between nucleocapsid protein and leader/intergenic sequence of mouse hepatitis virus RNA. J. Gen. Virol. 81:181-188.
    • (2000) J. Gen. Virol , vol.81 , pp. 181-188
    • Nelson, G.W.1    Stohlman, S.A.2    Tahara, S.M.3
  • 18
    • 0025043193 scopus 로고
    • Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein
    • Parker, M. M., and P. S. Masters. 1990. Sequence comparison of the N genes of five strains of the coronavirus mouse hepatitis virus suggests a three domain structure for the nucleocapsid protein. Virology 179:463-468.
    • (1990) Virology , vol.179 , pp. 463-468
    • Parker, M.M.1    Masters, P.S.2
  • 20
    • 34247128339 scopus 로고    scopus 로고
    • Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein
    • Saikatendu, K. S., J. S. Joseph, V. Subramanian, B. W. Neuman, M. J. Buchmeier, R. C. Stevens, and P. Kuhn. 2007. Ribonucleocapsid formation of severe acute respiratory syndrome coronavirus through molecular action of the N-terminal domain of N protein. J. Virol. 81:3913-3921.
    • (2007) J. Virol , vol.81 , pp. 3913-3921
    • Saikatendu, K.S.1    Joseph, J.S.2    Subramanian, V.3    Neuman, B.W.4    Buchmeier, M.J.5    Stevens, R.C.6    Kuhn, P.7
  • 21
    • 33845750075 scopus 로고    scopus 로고
    • A contemporary view of coronavirus transcription
    • Sawicki, S. G., D. L. Sawicki, and S. G. Siddell. 2007. A contemporary view of coronavirus transcription. J. Virol. 81:20-29.
    • (2007) J. Virol , vol.81 , pp. 20-29
    • Sawicki, S.G.1    Sawicki, D.L.2    Siddell, S.G.3
  • 22
    • 18744366350 scopus 로고    scopus 로고
    • Selective replication of coronavirus genomes that express nucleocapsid protein
    • Schelle, B., N. Karl, B. Ludewig, S. G. Siddell, and V. Thiel. 2005. Selective replication of coronavirus genomes that express nucleocapsid protein. J. Virol. 79:6620-6630.
    • (2005) J. Virol , vol.79 , pp. 6620-6630
    • Schelle, B.1    Karl, N.2    Ludewig, B.3    Siddell, S.G.4    Thiel, V.5
  • 23
    • 13444304279 scopus 로고    scopus 로고
    • Role of nucleotides immediately flanking the transcription-regulating sequence core in coronavirus subgenomic mRNA synthesis
    • Sola, I., J. L. Moreno, S. Zuñiga, S. Alonso, and L. Enjuanes. 2005. Role of nucleotides immediately flanking the transcription-regulating sequence core in coronavirus subgenomic mRNA synthesis. J. Virol. 79:2506-2516.
    • (2005) J. Virol , vol.79 , pp. 2506-2516
    • Sola, I.1    Moreno, J.L.2    Zuñiga, S.3    Alonso, S.4    Enjuanes, L.5
  • 24
    • 33750083654 scopus 로고    scopus 로고
    • Characterisation of the RNA binding properties of the coronavirus infectious bronchitis virus nucleocapsid protein amino-terminal region
    • Spencer, K., and J. A. Hiscox. 2006. Characterisation of the RNA binding properties of the coronavirus infectious bronchitis virus nucleocapsid protein amino-terminal region. FEBS Lett. 580:5993-5998.
    • (2006) FEBS Lett , vol.580 , pp. 5993-5998
    • Spencer, K.1    Hiscox, J.A.2
  • 25
    • 45649085737 scopus 로고    scopus 로고
    • Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein solved by the SAIL-NMR method
    • Takeda, M., C. Chang, T. Ikeya, P. Güntert, Y. Chang, Y. I. Hsu, T. Huang, and M. Kainosho. 2008. Solution structure of the C-terminal dimerization domain of SARS coronavirus nucleocapsid protein solved by the SAIL-NMR method. J. Mol. Biol. 380:608-622.
    • (2008) J. Mol. Biol , vol.380 , pp. 608-622
    • Takeda, M.1    Chang, C.2    Ikeya, T.3    Güntert, P.4    Chang, Y.5    Hsu, Y.I.6    Huang, T.7    Kainosho, M.8
  • 26
    • 33750208365 scopus 로고    scopus 로고
    • Amino acid residues critical for RNA-binding in the N-terminal domain of the nucleocapsid protein are essential determinants for the infectivity of coronavirus in cultured cells
    • Tan, Y. W., S. Fang, H. Fan, J. Lescar, and D. X. Liu. 2006. Amino acid residues critical for RNA-binding in the N-terminal domain of the nucleocapsid protein are essential determinants for the infectivity of coronavirus in cultured cells. Nucleic Acids Res. 34:4816-4825.
    • (2006) Nucleic Acids Res , vol.34 , pp. 4816-4825
    • Tan, Y.W.1    Fang, S.2    Fan, H.3    Lescar, J.4    Liu, D.X.5
  • 27
    • 20144388640 scopus 로고    scopus 로고
    • Biochemical and immunological studies of nucleocapsid proteins of severe acute respiratory syndrome and 229E human coronaviruses
    • Tang, T. K., M. P. Wu, S. T. Chen, M. H. Hou, M. H. Hong, F. M. Pan, H. M. Yu, J. H. Chen, C. W. Yao, and A. H. Wang. 2005. Biochemical and immunological studies of nucleocapsid proteins of severe acute respiratory syndrome and 229E human coronaviruses. Proteomics 5:925-937.
    • (2005) Proteomics , vol.5 , pp. 925-937
    • Tang, T.K.1    Wu, M.P.2    Chen, S.T.3    Hou, M.H.4    Hong, M.H.5    Pan, F.M.6    Yu, H.M.7    Chen, J.H.8    Yao, C.W.9    Wang, A.H.10
  • 28
    • 33746526551 scopus 로고    scopus 로고
    • Prediction of RNA binding sites in proteins from amino acid sequence
    • Terribilini, M., J. H. Lee, C. Yan, R. L. Jernigan, V. Honavar, and D. Dobbs. 2006. Prediction of RNA binding sites in proteins from amino acid sequence. RNA 12:1450-1462.
    • (2006) RNA , vol.12 , pp. 1450-1462
    • Terribilini, M.1    Lee, J.H.2    Yan, C.3    Jernigan, R.L.4    Honavar, V.5    Dobbs, D.6
  • 30
    • 0034990084 scopus 로고    scopus 로고
    • Viral replicase gene products suffice for coronavirus discontinuous transcription
    • Thiel, V., J. Herold, B. Schelle, and S. G. Siddell. 2001. Viral replicase gene products suffice for coronavirus discontinuous transcription. J. Virol. 75: 6676-6681.
    • (2001) J. Virol , vol.75 , pp. 6676-6681
    • Thiel, V.1    Herold, J.2    Schelle, B.3    Siddell, S.G.4
  • 32
    • 3442902456 scopus 로고    scopus 로고
    • The role of structural disorder in the function of RNA and protein chaperones
    • Tompa, P., and P. Csermely. 2004. The role of structural disorder in the function of RNA and protein chaperones. FASEB J. 18:1169-1175.
    • (2004) FASEB J , vol.18 , pp. 1169-1175
    • Tompa, P.1    Csermely, P.2
  • 33
    • 44449098281 scopus 로고    scopus 로고
    • van Hemert, M. J., S. H. van den Worm, K. Knoops, A. M. Mommaas, A. E. Gorbalenya, and E. J. Snijder. 2008. SARS-coronavirus replication/ transcription complexes are membrane-protected and need a host factor for activity in vitro. PLoS Pathog. 4:e1000054.
    • van Hemert, M. J., S. H. van den Worm, K. Knoops, A. M. Mommaas, A. E. Gorbalenya, and E. J. Snijder. 2008. SARS-coronavirus replication/ transcription complexes are membrane-protected and need a host factor for activity in vitro. PLoS Pathog. 4:e1000054.
  • 35
    • 0347319103 scopus 로고    scopus 로고
    • Sequence motifs involved in the regulation of discontinuous coronavirus subgenomic RNA synthesis
    • Zuñiga, S., I. Sola, S. Alonso, and L. Enjuanes. 2004. Sequence motifs involved in the regulation of discontinuous coronavirus subgenomic RNA synthesis. J. Virol. 78:980-994.
    • (2004) J. Virol , vol.78 , pp. 980-994
    • Zuñiga, S.1    Sola, I.2    Alonso, S.3    Enjuanes, L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.