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Volumn 407, Issue 1, 2010, Pages 33-42

Elucidation of functional domains of Chandipura virus Nucleocapsid protein involved in oligomerization and RNA binding: Implication in viral genome encapsidation

Author keywords

Chandipura virus (CHPV); Encapsidation; Leader RNA; Na deoxycholate (DOC); Nucleocapsid protein; Oligomerization

Indexed keywords

NUCLEOCAPSID PROTEIN; PROTEIN BINDING; RNA BINDING PROTEIN; VIRUS RNA;

EID: 77956898280     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2010.07.032     Document Type: Article
Times cited : (12)

References (45)
  • 2
    • 51649157089 scopus 로고
    • Effect of proteolytic digestion on the function of vesicular stomatitis virus ribonucleoprotein complex
    • Banerjee A.K., Roy J., Chattopadhyay D.J. Effect of proteolytic digestion on the function of vesicular stomatitis virus ribonucleoprotein complex. J. Biosci. 1987, 11(1-4):515-523.
    • (1987) J. Biosci. , vol.11 , Issue.1-4 , pp. 515-523
    • Banerjee, A.K.1    Roy, J.2    Chattopadhyay, D.J.3
  • 3
    • 0029926011 scopus 로고    scopus 로고
    • Domains of the measles virus N protein required for binding to P protein and self-assembly
    • Bankamp B., Horikami S.M., Thompson P.D., Huber M., Billeter M., Moyer S.A. Domains of the measles virus N protein required for binding to P protein and self-assembly. Virology 1996, 216(1):272-277.
    • (1996) Virology , vol.216 , Issue.1 , pp. 272-277
    • Bankamp, B.1    Horikami, S.M.2    Thompson, P.D.3    Huber, M.4    Billeter, M.5    Moyer, S.A.6
  • 4
    • 0037444188 scopus 로고    scopus 로고
    • Leader RNA binding ability of Chandipura virus P protein is regulated by its phosphorylation status: a possible role in genome transcription-replication switch
    • Basak S., Raha T., Chattopadhyay D., Majumder A., Shaila M.S., Chattopadhyay D.J. Leader RNA binding ability of Chandipura virus P protein is regulated by its phosphorylation status: a possible role in genome transcription-replication switch. Virology 2003, 307(2):372-385.
    • (2003) Virology , vol.307 , Issue.2 , pp. 372-385
    • Basak, S.1    Raha, T.2    Chattopadhyay, D.3    Majumder, A.4    Shaila, M.S.5    Chattopadhyay, D.J.6
  • 5
    • 3042675317 scopus 로고    scopus 로고
    • Monomer and dimer of Chandipura virus unphosphorylated P-protein binds leader RNA differently: implications for viral RNA synthesis
    • Basak S., Polley S., Basu M., Chattopadhyay D., Roy S. Monomer and dimer of Chandipura virus unphosphorylated P-protein binds leader RNA differently: implications for viral RNA synthesis. J. Mol. Biol. 2004, 339(5):1089-1101.
    • (2004) J. Mol. Biol. , vol.339 , Issue.5 , pp. 1089-1101
    • Basak, S.1    Polley, S.2    Basu, M.3    Chattopadhyay, D.4    Roy, S.5
  • 7
    • 33646535836 scopus 로고    scopus 로고
    • Initiation of encapsidation as evidenced by deoxycholate-treated Nucleocapsid protein in the Chandipura virus life cycle
    • Bhattacharya R., Basak S., Chattopadhyay D.J. Initiation of encapsidation as evidenced by deoxycholate-treated Nucleocapsid protein in the Chandipura virus life cycle. Virology 2006, 349(1):197-211.
    • (2006) Virology , vol.349 , Issue.1 , pp. 197-211
    • Bhattacharya, R.1    Basak, S.2    Chattopadhyay, D.J.3
  • 8
    • 0019474851 scopus 로고
    • Interaction of VSV leader RNA and nucleocapsid protein may control VSV genome replication
    • Blumberg B.M., Leppert M., Kolakofsky D. Interaction of VSV leader RNA and nucleocapsid protein may control VSV genome replication. Cell 1981, 23(3):837-845.
    • (1981) Cell , vol.23 , Issue.3 , pp. 837-845
    • Blumberg, B.M.1    Leppert, M.2    Kolakofsky, D.3
  • 9
    • 0020714002 scopus 로고
    • N protein of vesicular stomatitis virus selectively encapsidates leader RNA in-vitro
    • Blumberg B.M., Giorgi C., Kolakofsky D. N protein of vesicular stomatitis virus selectively encapsidates leader RNA in-vitro. Cell 1983, 32(2):559-567.
    • (1983) Cell , vol.32 , Issue.2 , pp. 559-567
    • Blumberg, B.M.1    Giorgi, C.2    Kolakofsky, D.3
  • 10
    • 0027260606 scopus 로고
    • The conserved N-terminal region of Sendai virus nucleocapsid protein NP is required for nucleocapsid assembly
    • Buchholz C.J., Spehner D., Drillien R., Neubert W.J., Homann H.E. The conserved N-terminal region of Sendai virus nucleocapsid protein NP is required for nucleocapsid assembly. J. Virol. 1993, 67(10):5803-5812.
    • (1993) J. Virol. , vol.67 , Issue.10 , pp. 5803-5812
    • Buchholz, C.J.1    Spehner, D.2    Drillien, R.3    Neubert, W.J.4    Homann, H.E.5
  • 12
    • 1242328675 scopus 로고    scopus 로고
    • Visualizing the RNA molecule in the bacterially expressed vesicular stomatitis virus nucleoprotein-RNA complex
    • Chen Z., Green T.J., Luo M., Li H. Visualizing the RNA molecule in the bacterially expressed vesicular stomatitis virus nucleoprotein-RNA complex. Structure 2004, 12(2):227-235.
    • (2004) Structure , vol.12 , Issue.2 , pp. 227-235
    • Chen, Z.1    Green, T.J.2    Luo, M.3    Li, H.4
  • 13
    • 37049018431 scopus 로고    scopus 로고
    • 0-P complex formation and encapsidation of viral genome RNA
    • 0-P complex formation and encapsidation of viral genome RNA. J. Virol. 2007, 81(24):13478-13485.
    • (2007) J. Virol. , vol.81 , Issue.24 , pp. 13478-13485
    • Chen, M.1    Ogino, T.2    Banerjee, A.K.3
  • 14
    • 0033587599 scopus 로고    scopus 로고
    • Oligomerization of the influenza virus nucleoprotein: identification of positive and negative sequence elements
    • Elton D., Medcalf E., Bishop K., Digard P. Oligomerization of the influenza virus nucleoprotein: identification of positive and negative sequence elements. Virology 1999, 260(1):190-200.
    • (1999) Virology , vol.260 , Issue.1 , pp. 190-200
    • Elton, D.1    Medcalf, E.2    Bishop, K.3    Digard, P.4
  • 15
    • 76249126382 scopus 로고    scopus 로고
    • Cryo-EM model of the bullet-shaped vesicular stomatitis virus
    • Ge P., Tsao J., Schein S., Green T.J., Luo M., Zhou Z.H. Cryo-EM model of the bullet-shaped vesicular stomatitis virus. Science 2010, 327(5966):689-693.
    • (2010) Science , vol.327 , Issue.5966 , pp. 689-693
    • Ge, P.1    Tsao, J.2    Schein, S.3    Green, T.J.4    Luo, M.5    Zhou, Z.H.6
  • 16
    • 67650872991 scopus 로고    scopus 로고
    • Structure of the vesicular stomatitis virus nucleocapsid in complex with the nucleocapsid-binding domain of the small polymerase cofactor, P
    • Green T.J., Luo M. Structure of the vesicular stomatitis virus nucleocapsid in complex with the nucleocapsid-binding domain of the small polymerase cofactor, P. Proc. Natl. Acad. Sci. U. S. A. 2009, 106(28):11713-11718.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , Issue.28 , pp. 11713-11718
    • Green, T.J.1    Luo, M.2
  • 17
    • 0033809574 scopus 로고    scopus 로고
    • Study of the assembly of vesicular stomatitis virus N protein: role of the P protein
    • Green T.J., Macpherson S., Qiu S., Lebowitz J., Wertz G.W., Luo M. Study of the assembly of vesicular stomatitis virus N protein: role of the P protein. J. Virol. 2000, 74(20):9515-9524.
    • (2000) J. Virol. , vol.74 , Issue.20 , pp. 9515-9524
    • Green, T.J.1    Macpherson, S.2    Qiu, S.3    Lebowitz, J.4    Wertz, G.W.5    Luo, M.6
  • 18
    • 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(5785):357-360.
    • (2006) Science , vol.313 , Issue.5785 , pp. 357-360
    • Green, T.J.1    Zhang, X.2    Wertz, G.W.3    Luo, M.4
  • 19
    • 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., Kolakofsky D. Sendai virus genome synthesis and assembly are coupled: a possible mechanism to promote viral RNA polymerase processivity. J. Gen. Virol. 2001, 82(Pt 12):2895-2903.
    • (2001) J. Gen. Virol. , vol.82 , Issue.PART 12 , pp. 2895-2903
    • Gubbay, O.1    Curran, J.2    Kolakofsky, D.3
  • 20
    • 0032425151 scopus 로고    scopus 로고
    • Characterization of rabies virus nucleocapsids and recombinant nucleocapsid-like structures
    • Iseni F., Barge A., Baudin F., Blondel D., Ruigrok R.W. Characterization of rabies virus nucleocapsids and recombinant nucleocapsid-like structures. J. Gen. Virol. 1998, 79(Pt 12):2909-2919.
    • (1998) J. Gen. Virol. , vol.79 , Issue.PART 12 , pp. 2909-2919
    • Iseni, F.1    Barge, A.2    Baudin, F.3    Blondel, D.4    Ruigrok, R.W.5
  • 21
    • 0042668459 scopus 로고    scopus 로고
    • Newcastle disease virus nucleocapsid protein: self-assembly and length-determination domains
    • Kho C.L., Tan W.S., Tey B.T., Yusoff K. Newcastle disease virus nucleocapsid protein: self-assembly and length-determination domains. J. Gen. Virol. 2003, 84(Pt 8):2163-2168.
    • (2003) J. Gen. Virol. , vol.84 , Issue.PART 8 , pp. 2163-2168
    • Kho, C.L.1    Tan, W.S.2    Tey, B.T.3    Yusoff, K.4
  • 22
    • 0001178028 scopus 로고    scopus 로고
    • Paramyxoviridae: the viruses and their replication
    • Lippincott Williams & Wilkins, Philadelphia, D.M. Knipe, P.M. Howley (Eds.)
    • Lamb R.A., Kolakofsky D. Paramyxoviridae: the viruses and their replication. Fields Virology 2001, Lippincott Williams & Wilkins, Philadelphia. 4th ed. D.M. Knipe, P.M. Howley (Eds.).
    • (2001) Fields Virology
    • Lamb, R.A.1    Kolakofsky, D.2
  • 23
    • 58149493911 scopus 로고    scopus 로고
    • In-vitro initial attachment of HIV-1 integrase to viral ends: control of the DNA specific interaction by the oligomerization state
    • Lesbats P., Metifiot M., Calmels C., Baranova S., Nevinsky G., Andreola M.L., Parissi V. In-vitro initial attachment of HIV-1 integrase to viral ends: control of the DNA specific interaction by the oligomerization state. Nucleic Acids Res. 2008, 36(22):7043-7058.
    • (2008) Nucleic Acids Res. , vol.36 , Issue.22 , pp. 7043-7058
    • Lesbats, P.1    Metifiot, M.2    Calmels, C.3    Baranova, S.4    Nevinsky, G.5    Andreola, M.L.6    Parissi, V.7
  • 24
    • 0031055574 scopus 로고    scopus 로고
    • Protein interaction domains of the measles virus nucleocapsid protein (NP)
    • Liston P., Batal R., DiFlumeri C., Briedis D.J. Protein interaction domains of the measles virus nucleocapsid protein (NP). Arch. Virol. 1997, 142(2):305-321.
    • (1997) Arch. Virol. , vol.142 , Issue.2 , pp. 305-321
    • Liston, P.1    Batal, R.2    DiFlumeri, C.3    Briedis, D.J.4
  • 25
    • 35348924854 scopus 로고    scopus 로고
    • Conserved characteristics of the rhabdovirus nucleoprotein
    • Luo M., Green T.J., Zhang X., Tsao J., Qiu S. Conserved characteristics of the rhabdovirus nucleoprotein. Virus Res. 2007, 129(2):246-251.
    • (2007) Virus Res. , vol.129 , Issue.2 , pp. 246-251
    • Luo, M.1    Green, T.J.2    Zhang, X.3    Tsao, J.4    Qiu, S.5
  • 26
    • 35348886782 scopus 로고    scopus 로고
    • Structural comparisons of the nucleoprotein from three negative strand RNA virus families
    • Luo M., Green T.J., Zhang X., Tsao J., Qiu S. Structural comparisons of the nucleoprotein from three negative strand RNA virus families. Virol. J. 2007, 4:72.
    • (2007) Virol. J. , vol.4 , pp. 72
    • Luo, M.1    Green, T.J.2    Zhang, X.3    Tsao, J.4    Qiu, S.5
  • 27
    • 1542327649 scopus 로고    scopus 로고
    • P-protein of Chandipura virus is an N-protein-specific chaperone that acts at the nucleation stage
    • Majumdar A., Bhattacharya R., Basak S., Shaila M.S., Chattopadhyay D., Roy S. P-protein of Chandipura virus is an N-protein-specific chaperone that acts at the nucleation stage. Biochemistry 2004, 43(10):2863-2870.
    • (2004) Biochemistry , vol.43 , Issue.10 , pp. 2863-2870
    • Majumdar, A.1    Bhattacharya, R.2    Basak, S.3    Shaila, M.S.4    Chattopadhyay, D.5    Roy, S.6
  • 28
    • 0035903162 scopus 로고    scopus 로고
    • Effect of osmolytes and chaperone-like action of P-protein on folding of nucleocapsid protein of Chandipura virus
    • Majumder A., Basak S., Raha T., Chowdhury S.P., Chattopadhyay D., Roy S. Effect of osmolytes and chaperone-like action of P-protein on folding of nucleocapsid protein of Chandipura virus. J. Biol. Chem. 2001, 276(33):30948-30955.
    • (2001) J. Biol. Chem. , vol.276 , Issue.33 , pp. 30948-30955
    • Majumder, A.1    Basak, S.2    Raha, T.3    Chowdhury, S.P.4    Chattopadhyay, D.5    Roy, S.6
  • 29
    • 17644404460 scopus 로고    scopus 로고
    • Complete genome sequences of Chandipura and Isfahan vesiculoviruses
    • Marriott A.C. Complete genome sequences of Chandipura and Isfahan vesiculoviruses. Arch. Virol. 2005, 150(4):671-680.
    • (2005) Arch. Virol. , vol.150 , Issue.4 , pp. 671-680
    • Marriott, A.C.1
  • 30
    • 0023130350 scopus 로고
    • Sequences of Chandipura virus N and NS genes: evidence for high mutability of the NS gene within vesiculoviruses
    • Masters P.S., Banerjee A.K. Sequences of Chandipura virus N and NS genes: evidence for high mutability of the NS gene within vesiculoviruses. Virology 1987, 157(2):298-306.
    • (1987) Virology , vol.157 , Issue.2 , pp. 298-306
    • Masters, P.S.1    Banerjee, A.K.2
  • 31
    • 0023792843 scopus 로고
    • Complex formation with vesicular stomatitis virus phosphoprotein NS prevents binding of nucleocapsid protein N to nonspecific RNA
    • Masters P.S., Banerjee A.K. Complex formation with vesicular stomatitis virus phosphoprotein NS prevents binding of nucleocapsid protein N to nonspecific RNA. J. Virol. 1988, 62(8):2658-2664.
    • (1988) J. Virol. , vol.62 , Issue.8 , pp. 2658-2664
    • Masters, P.S.1    Banerjee, A.K.2
  • 32
    • 0025734250 scopus 로고
    • Assembly and transcription of synthetic vesicular stomatitis virus nucleocapsids
    • Moyer S.A., Smallwood-Kentro S., Haddad A., Prevec L. Assembly and transcription of synthetic vesicular stomatitis virus nucleocapsids. J. Virol. 1991, 65(5):2170-2178.
    • (1991) J. Virol. , vol.65 , Issue.5 , pp. 2170-2178
    • Moyer, S.A.1    Smallwood-Kentro, S.2    Haddad, A.3    Prevec, L.4
  • 33
    • 0031575842 scopus 로고    scopus 로고
    • A highly conserved region of the Sendai virus nucleocapsid protein contributes to the NP-NP binding domain
    • Myers T.M., Pieters A., Moyer S.A. A highly conserved region of the Sendai virus nucleocapsid protein contributes to the NP-NP binding domain. Virology 1997, 229(2):322-335.
    • (1997) Virology , vol.229 , Issue.2 , pp. 322-335
    • Myers, T.M.1    Pieters, A.2    Moyer, S.A.3
  • 34
    • 0033016954 scopus 로고    scopus 로고
    • Identification of nucleocapsid protein residues required for Sendai virus nucleocapsid formation and genome replication
    • Myers T.M., Smallwood S., Moyer S.A. Identification of nucleocapsid protein residues required for Sendai virus nucleocapsid formation and genome replication. J. Gen. Virol. 1999, 80(Pt 6):1383-1391.
    • (1999) J. Gen. Virol. , vol.80 , Issue.PART 6 , pp. 1383-1391
    • Myers, T.M.1    Smallwood, S.2    Moyer, S.A.3
  • 35
    • 0032807746 scopus 로고    scopus 로고
    • Mapping of domains on the human parainfluenza virus type 2 nucleocapsid protein (NP) required for NP-phosphoprotein or NP-NP interaction
    • Nishio M., Tsurudome M., Ito M., Kawano M., Kusagawa S., Komada H., Ito Y. Mapping of domains on the human parainfluenza virus type 2 nucleocapsid protein (NP) required for NP-phosphoprotein or NP-NP interaction. J. Gen. Virol. 1999, 80(Pt 8):2017-2022.
    • (1999) J. Gen. Virol. , vol.80 , Issue.PART 8 , pp. 2017-2022
    • Nishio, M.1    Tsurudome, M.2    Ito, M.3    Kawano, M.4    Kusagawa, S.5    Komada, H.6    Ito, Y.7
  • 36
    • 0028850828 scopus 로고
    • The termini of VSV DI particle RNAs are sufficient to signal RNA encapsidation, replication, and budding to generate infectious particles
    • Pattnaik A.K., Ball L.A., LeGrone A., Wertz G.W. The termini of VSV DI particle RNAs are sufficient to signal RNA encapsidation, replication, and budding to generate infectious particles. Virology 1995, 206(1):760-764.
    • (1995) Virology , vol.206 , Issue.1 , pp. 760-764
    • Pattnaik, A.K.1    Ball, L.A.2    LeGrone, A.3    Wertz, G.W.4
  • 38
    • 75449115142 scopus 로고    scopus 로고
    • Importance of hydrogen bond contacts between the N protein and RNA genome of vesicular stomatitis virus in encapsidation and RNA synthesis
    • Epub 2009 Dec 9.(Feb 84(4)):1741-51
    • Rainsford E.W., Harouoka D., Wertz G.W. Importance of hydrogen bond contacts between the N protein and RNA genome of vesicular stomatitis virus in encapsidation and RNA synthesis. J. Virol. 2010, 84(4):1741-1751. Epub 2009 Dec 9.(Feb 84(4)):1741-51.
    • (2010) J. Virol. , vol.84 , Issue.4 , pp. 1741-1751
    • Rainsford, E.W.1    Harouoka, D.2    Wertz, G.W.3
  • 39
    • 77950939771 scopus 로고    scopus 로고
    • Structural and functional properties of the vesicular stomatitis virus nucleoprotein-RNA complex as revealed by proteolytic digestion
    • Sarkar A., Chattopadhyay S., Cox R., Luo M., Banerjee A.K. Structural and functional properties of the vesicular stomatitis virus nucleoprotein-RNA complex as revealed by proteolytic digestion. Virology 2010, 401(1):61-69.
    • (2010) Virology , vol.401 , Issue.1 , pp. 61-69
    • Sarkar, A.1    Chattopadhyay, S.2    Cox, R.3    Luo, M.4    Banerjee, A.K.5
  • 40
    • 70450209178 scopus 로고    scopus 로고
    • Mutational analysis of human heat-shock transcription factor 1 reveals a regulatory role for oligomerization in DNA-binding specificity
    • Takemori Y., Enoki Y., Yamamoto N., Fukai Y., Adachi K., Sakurai H. Mutational analysis of human heat-shock transcription factor 1 reveals a regulatory role for oligomerization in DNA-binding specificity. Biochem. J. 2009, 424(2):253-261.
    • (2009) Biochem. J. , vol.424 , Issue.2 , pp. 253-261
    • Takemori, Y.1    Enoki, Y.2    Yamamoto, N.3    Fukai, Y.4    Adachi, K.5    Sakurai, H.6
  • 43
    • 0021885051 scopus 로고
    • Mass and molecular composition of vesicular stomatitis virus: a scanning transmission electron microscopy analysis
    • Thomas D., Newcomb W.W., Brown J.C., Wall J.S., Hainfeld J.F., Trus B.L., Steven A.C. Mass and molecular composition of vesicular stomatitis virus: a scanning transmission electron microscopy analysis. J. Virol. 1985, 54(2):598-607.
    • (1985) J. Virol. , vol.54 , Issue.2 , pp. 598-607
    • Thomas, D.1    Newcomb, W.W.2    Brown, J.C.3    Wall, J.S.4    Hainfeld, J.F.5    Trus, B.L.6    Steven, A.C.7
  • 45
    • 37849012529 scopus 로고    scopus 로고
    • Role of intermolecular interactions of vesicular stomatitis virus nucleoprotein in RNA encapsidation
    • Zhang X., Green T.J., Tsao J., Qiu S., Luo M. Role of intermolecular interactions of vesicular stomatitis virus nucleoprotein in RNA encapsidation. J. Virol. 2008, 82(2):674-682.
    • (2008) J. Virol. , vol.82 , Issue.2 , pp. 674-682
    • Zhang, X.1    Green, T.J.2    Tsao, J.3    Qiu, S.4    Luo, M.5


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