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Volumn 32, Issue 8, 2004, Pages 2623-2631

The hepatitis C virus Core protein is a potent nucleic acid chaperone that directs dimerization of the viral (+) strand RNA in vitro

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; COMPLEMENTARY DNA; COMPLEMENTARY RNA; CORE PROTEIN; DOUBLE STRANDED DNA; PALINDROMIC DNA; VIRUS PROTEIN; VIRUS RNA; NUCLEOCAPSID PROTEIN, HEPATITIS C VIRUS; VIRUS DNA;

EID: 3042576370     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkh579     Document Type: Article
Times cited : (103)

References (44)
  • 1
    • 0035811625 scopus 로고    scopus 로고
    • Hepatitis C virus infection
    • Lauer,G.M. and Walker,B.D. (2001) Hepatitis C virus infection. N. Engl. J. Med., 345, 41-52.
    • (2001) N. Engl. J. Med. , vol.345 , pp. 41-52
    • Lauer, G.M.1    Walker, B.D.2
  • 2
    • 0037300877 scopus 로고    scopus 로고
    • Structural biology of hepatitis C virus
    • vii
    • Penin,F. (2003) Structural biology of hepatitis C virus. Clin. Liver Dis., 7, 1-21, vii.
    • (2003) Clin. Liver Dis. , vol.7 , pp. 1-21
    • Penin, F.1
  • 3
    • 0035928765 scopus 로고    scopus 로고
    • Hepatitis C virus core protein: Intriguing properties and functional relevance
    • Ray,R.B. and Ray,R. (2001) Hepatitis C virus core protein: intriguing properties and functional relevance. FEMS Microbiol. Lett., 202, 149-156.
    • (2001) FEMS Microbiol. Lett. , vol.202 , pp. 149-156
    • Ray, R.B.1    Ray, R.2
  • 4
    • 0034053296 scopus 로고    scopus 로고
    • Properties of the hepatitis C virus core protein: A structural protein that modulates cellular processes
    • McLauchlan,J. (2000) Properties of the hepatitis C virus core protein: a structural protein that modulates cellular processes. J. Viral Hepat., 7, 2-14.
    • (2000) J. Viral Hepat. , vol.7 , pp. 2-14
    • McLauchlan, J.1
  • 5
    • 0035130118 scopus 로고    scopus 로고
    • Self-assembly of nucleocapsid-like particles from recombinant hepatitis C virus core protein
    • Kunkel,M., Lorinezi,M., Rijnbrand,R., Lemon,S.M. and Watowich,S.J. (2001) Self-assembly of nucleocapsid-like particles from recombinant hepatitis C virus core protein. J. Virol., 75, 2119-2129.
    • (2001) J. Virol. , vol.75 , pp. 2119-2129
    • Kunkel, M.1    Lorinezi, M.2    Rijnbrand, R.3    Lemon, S.M.4    Watowich, S.J.5
  • 6
    • 0032731641 scopus 로고    scopus 로고
    • Interaction of hepatitis C virus core protein with viral sense RNA and suppression of its translation
    • Shimoike,T., Mimori,S., Tani,H., Matsuura,Y. and Miyamura,T. (1999) Interaction of hepatitis C virus core protein with viral sense RNA and suppression of its translation. J. Virol., 73, 9718-9725.
    • (1999) J. Virol. , vol.73 , pp. 9718-9725
    • Shimoike, T.1    Mimori, S.2    Tani, H.3    Matsuura, Y.4    Miyamura, T.5
  • 7
    • 0031977996 scopus 로고    scopus 로고
    • Hepatitis C virus structural proteins assemble into viruslike particles in insect cells
    • Baumert,T.F., Ito,S., Wong,D.T. and Liang,T.J. (1998) Hepatitis C virus structural proteins assemble into viruslike particles in insect cells. J. Virol., 72, 3827-3836.
    • (1998) J. Virol. , vol.72 , pp. 3827-3836
    • Baumert, T.F.1    Ito, S.2    Wong, D.T.3    Liang, T.J.4
  • 8
    • 0031679786 scopus 로고    scopus 로고
    • Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: Significance for viral replication
    • Rein,A., Henderson,L.E. and Levin,J.G. (1998) Nucleic-acid-chaperone activity of retroviral nucleocapsid proteins: significance for viral replication. Trends Biochem. Sci., 23, 297-301.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 297-301
    • Rein, A.1    Henderson, L.E.2    Levin, J.G.3
  • 9
    • 0034565966 scopus 로고    scopus 로고
    • Nucleocapsid protein of human immunodeficiency virus as a model protein with chaperoning functions and as a target for antiviral drugs
    • Darlix,J.L., Cristofari,G., Rau,M., Pechoux,C., Berthoux,L. and Roques,B. (2000) Nucleocapsid protein of human immunodeficiency virus as a model protein with chaperoning functions and as a target for antiviral drugs. Adv. Pharmacol., 48, 345-372.
    • (2000) Adv. Pharmacol. , vol.48 , pp. 345-372
    • Darlix, J.L.1    Cristofari, G.2    Rau, M.3    Pechoux, C.4    Berthoux, L.5    Roques, B.6
  • 10
    • 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
  • 13
    • 0025991559 scopus 로고
    • Gene mapping of the putative structural region of the hepatitis C virus genome by in vitro processing analysis
    • Hijikata,M., Kato,N., Ootsuyama,Y., Nakagawa,M. and Shimotohno,K. (1991) Gene mapping of the putative structural region of the hepatitis C virus genome by in vitro processing analysis. Proc. Natl Acad. Sci. USA, 88, 5547-5551.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5547-5551
    • Hijikata, M.1    Kato, N.2    Ootsuyama, Y.3    Nakagawa, M.4    Shimotohno, K.5
  • 14
    • 0028239937 scopus 로고
    • In vitro asymmetric binding of the pleiotropic regulatory protein, FruR, to the ace operator controlling glyoxylate shunt enzyme synthesis
    • Cortay,J.C., Negre,D., Scarabel,M., Ramseier,T.M., Vartak,N.B., Reizer,J., Saier,M.H.,Jr and Cozzone,A.J. (1994) In vitro asymmetric binding of the pleiotropic regulatory protein, FruR, to the ace operator controlling glyoxylate shunt enzyme synthesis. J. Biol. Chem., 269, 14885-14891.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14885-14891
    • Cortay, J.C.1    Negre, D.2    Scarabel, M.3    Ramseier, T.M.4    Vartak, N.B.5    Reizer, J.6    Saier Jr., M.H.7    Cozzone, A.J.8
  • 15
    • 0025021014 scopus 로고
    • A study of the dimer formation of Rous sarcoma virus RNA and of its effect on viral protein synthesis in vitro
    • Bieth,E., Gabus,C. and Darlix,J.L. (1990) A study of the dimer formation of Rous sarcoma virus RNA and of its effect on viral protein synthesis in vitro. Nucleic Acids Res., 18, 119-127.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 119-127
    • Bieth, E.1    Gabus, C.2    Darlix, J.L.3
  • 16
    • 0026100895 scopus 로고
    • Interaction of HIV-1 reverse transcriptase with a synthetic form of its replication primer, tRNA(Lys,3)
    • Barat,C., Le Grice,S.F. and Darlix,J.L. (1991) Interaction of HIV-1 reverse transcriptase with a synthetic form of its replication primer, tRNA(Lys,3). Nucleic Acids Res., 19, 751-757.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 751-757
    • Barat, C.1    Le Grice, S.F.2    Darlix, J.L.3
  • 17
    • 0034705568 scopus 로고    scopus 로고
    • The GAG-like protein of the yeast Ty1 retrotransposon contains a nucleic acid chaperone domain analogous to retroviral nucleocapsid proteins
    • Cristofari,G., Ficheux,D. and Darlix,J.L. (2000) The GAG-like protein of the yeast Ty1 retrotransposon contains a nucleic acid chaperone domain analogous to retroviral nucleocapsid proteins. J. Biol. Chem., 275, 19210-19217.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19210-19217
    • Cristofari, G.1    Ficheux, D.2    Darlix, J.L.3
  • 18
    • 0242413008 scopus 로고    scopus 로고
    • Unusual multiple recoding events leading to alternative forms of hepatitis C virus core protein from genotype 1b
    • Boulant,S., Becchi,M., Penin,F. and Lavergne,J.P. (2003) Unusual multiple recoding events leading to alternative forms of hepatitis C virus core protein from genotype 1b. J. Biol. Chem., 278, 45785-45792.
    • (2003) J. Biol. Chem. , vol.278 , pp. 45785-45792
    • Boulant, S.1    Becchi, M.2    Penin, F.3    Lavergne, J.P.4
  • 20
    • 0028129970 scopus 로고
    • DNA strand exchange and selective DNA annealing promoted by the human immunodeficiency virus type 1 nucleocapsid protein
    • Tsuchihashi,Z. and Brown,P.O. (1994) DNA strand exchange and selective DNA annealing promoted by the human immunodeficiency virus type 1 nucleocapsid protein. J. Virol., 68, 5863-5870.
    • (1994) J. Virol. , vol.68 , pp. 5863-5870
    • Tsuchihashi, Z.1    Brown, P.O.2
  • 21
    • 0029044016 scopus 로고
    • Analysis of the nucleic acid annealing activities of nucleocapsid protein from HIV-1
    • Lapadat-Tapolsky,M., Pernelle,C., Borie,C. and Darlix,J.L. (1995) Analysis of the nucleic acid annealing activities of nucleocapsid protein from HIV-1. Nucleic Acids Res., 23, 2434-2441.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 2434-2441
    • Lapadat-Tapolsky, M.1    Pernelle, C.2    Borie, C.3    Darlix, J.L.4
  • 22
    • 0035163939 scopus 로고    scopus 로고
    • Nucleic acid chaperone activity of the ORF1 protein from the mouse LINE-1 retrotransposon
    • Martin,S.L. and Bushman,F.D. (2001) Nucleic acid chaperone activity of the ORF1 protein from the mouse LINE-1 retrotransposon. Mol. Cell. Biol., 21, 467-475.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 467-475
    • Martin, S.L.1    Bushman, F.D.2
  • 23
    • 0025598002 scopus 로고
    • Cis elements and trans-acting factors involved in the RNA dimerization of the human immunodeficiency virus HIV-1
    • Darlix,J.L., Gabus,C., Nugeyre,M.T., Clavel,F. and Barre-Sinoussi,F. (1990) Cis elements and trans-acting factors involved in the RNA dimerization of the human immunodeficiency virus HIV-1. J. Mol. Biol., 216, 689-699.
    • (1990) J. Mol. Biol. , vol.216 , pp. 689-699
    • Darlix, J.L.1    Gabus, C.2    Nugeyre, M.T.3    Clavel, F.4    Barre-Sinoussi, F.5
  • 24
    • 0037102438 scopus 로고    scopus 로고
    • A 5′-3′ long-range interaction in Ty1 RNA controls its reverse transcription and retrotransposition
    • Cristofari,G., Bampi,C., Wilhelm,M., Wilhelm,F.X. and Darlix,J.L. (2002) A 5′-3′ long-range interaction in Ty1 RNA controls its reverse transcription and retrotransposition. EMBO J., 21, 4368-4379.
    • (2002) EMBO J. , vol.21 , pp. 4368-4379
    • Cristofari, G.1    Bampi, C.2    Wilhelm, M.3    Wilhelm, F.X.4    Darlix, J.L.5
  • 25
    • 0036712305 scopus 로고    scopus 로고
    • RNA chaperone StpA loosens interactions of the tertiary structure in the td group I intron in vivo
    • Waldsich,C., Grossberger,R. and Schroeder,R. (2002) RNA chaperone StpA loosens interactions of the tertiary structure in the td group I intron in vivo. Genes Dev., 16, 2300-2312.
    • (2002) Genes Dev. , vol.16 , pp. 2300-2312
    • Waldsich, C.1    Grossberger, R.2    Schroeder, R.3
  • 26
    • 0028057811 scopus 로고
    • RNA annealing activities in HeLa nuclei
    • Portman,D.S. and Dreyfuss,G. (1994) RNA annealing activities in HeLa nuclei. EMBO J., 13, 213-221.
    • (1994) EMBO J. , vol.13 , pp. 213-221
    • Portman, D.S.1    Dreyfuss, G.2
  • 27
    • 0037332361 scopus 로고    scopus 로고
    • 3′ nontranslated RNA signals required for replication of hepatitis C virus RNA
    • Yi,M. and Lemon,S.M. (2003) 3′ nontranslated RNA signals required for replication of hepatitis C virus RNA. J. Virol., 77, 3557-3568.
    • (2003) J. Virol. , vol.77 , pp. 3557-3568
    • Yi, M.1    Lemon, S.M.2
  • 28
    • 0030019828 scopus 로고    scopus 로고
    • Kissing-loop model of HIV-1 genome dimerization: HIV-1 RNAs can assume alternative dimeric forms and all sequences upstream or downstream of hairpin 248-271 are dispensable for dimer formation
    • Laughrea,M. and Jette,L. (1996) Kissing-loop model of HIV-1 genome dimerization: HIV-1 RNAs can assume alternative dimeric forms and all sequences upstream or downstream of hairpin 248-271 are dispensable for dimer formation. Biochemistry, 35, 1589-1598.
    • (1996) Biochemistry , vol.35 , pp. 1589-1598
    • Laughrea, M.1    Jette, L.2
  • 29
    • 0029868164 scopus 로고    scopus 로고
    • A kissing complex together with a stable dimer is involved in the HIV-1Lai RNA dimerization process in vitro
    • Muriaux,D., Fosse,P. and Paoletti,J. (1996) A kissing complex together with a stable dimer is involved in the HIV-1Lai RNA dimerization process in vitro. Biochemistry, 35, 5075-5082.
    • (1996) Biochemistry , vol.35 , pp. 5075-5082
    • Muriaux, D.1    Fosse, P.2    Paoletti, J.3
  • 30
    • 0030480326 scopus 로고    scopus 로고
    • NCp7 activates HIV-1Lai RNA dimerization by converting a transient loop-loop complex into a stable dimer
    • Muriaux,D., De Rocquigny,H., Roques,B.P. and Paoletti,J. (1996) NCp7 activates HIV-1Lai RNA dimerization by converting a transient loop-loop complex into a stable dimer. J. Biol. Chem., 271, 33686-33692.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33686-33692
    • Muriaux, D.1    De Rocquigny, H.2    Roques, B.P.3    Paoletti, J.4
  • 31
    • 0028239204 scopus 로고
    • Identification of the primary site of the human immunodeficiency virus type 1 RNA dimerization in vitro
    • Skripkin,E., Paillart,J.C., Marquet,R., Ehresmann,B. and Ehresmann,C. (1994) Identification of the primary site of the human immunodeficiency virus type 1 RNA dimerization in vitro. Proc. Natl Acad. Sci. USA, 91, 4945-4949.
    • (1994) Proc. Natl. Acad. Sci. USA, , vol.91 , pp. 4945-4949
    • Skripkin, E.1    Paillart, J.C.2    Marquet, R.3    Ehresmann, B.4    Ehresmann, C.5
  • 32
    • 0027996464 scopus 로고
    • Mutational analysis of the bipartite dimer linkage structure of human immunodeficiency virus type 1 genomic RNA
    • Paillart,J.C., Marquet,R., Skripkin,E., Ehresmann,B. and Ehresmann,C. (1994) Mutational analysis of the bipartite dimer linkage structure of human immunodeficiency virus type 1 genomic RNA. J. Biol. Chem., 269, 27486-27493.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27486-27493
    • Paillart, J.C.1    Marquet, R.2    Skripkin, E.3    Ehresmann, B.4    Ehresmann, C.5
  • 33
    • 0028027708 scopus 로고
    • A 19-nucleotide sequence upstream of the ′ major splice donor is part of the dimerization domain of human immunodeficiency virus 1 genomic RNA
    • Laughrea,M. and Jette,L. (1994) A 19-nucleotide sequence upstream of the ′ major splice donor is part of the dimerization domain of human immunodeficiency virus 1 genomic RNA. Biochemistry, 33, 13464-13474.
    • (1994) Biochemistry , vol.33 , pp. 13464-13474
    • Laughrea, M.1    Jette, L.2
  • 34
    • 0032816079 scopus 로고    scopus 로고
    • A recombinant hepatitis C virus RNA-dependent RNA polymerase capable of copying the full-length viral RNA
    • Oh,J.W., Ito,T. and Lai,M.M. (1999) A recombinant hepatitis C virus RNA-dependent RNA polymerase capable of copying the full-length viral RNA. J. Virol., 73, 7694-7702.
    • (1999) J. Virol. , vol.73 , pp. 7694-7702
    • Oh, J.W.1    Ito, T.2    Lai, M.M.3
  • 35
    • 0034625351 scopus 로고    scopus 로고
    • Template requirement and initiation site selection by hepatitis C virus polymerase on a minimal viral RNA template
    • Oh,J.W., Sheu,G.T. and Lai,M.M. (2000) Template requirement and initiation site selection by hepatitis C virus polymerase on a minimal viral RNA template. J. Biol. Chem., 275, 17710-17717.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17710-17717
    • Oh, J.W.1    Sheu, G.T.2    Lai, M.M.3
  • 36
    • 0034977831 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 4G-poly(A) binding protein interaction is required for poly(A) tail-mediated stimulation of picornavirus internal ribosome entry segment-driven translation but not for X-mediated stimulation of hepatitis C virus translation
    • Michel,Y.M., Borman,A.M., Paulous,S. and Kean,K.M. (2001) Eukaryotic initiation factor 4G-poly(A) binding protein interaction is required for poly(A) tail-mediated stimulation of picornavirus internal ribosome entry segment-driven translation but not for X-mediated stimulation of hepatitis C virus translation. Mol. Cell. Biol., 21, 4097-4109.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 4097-4109
    • Michel, Y.M.1    Borman, A.M.2    Paulous, S.3    Kean, K.M.4
  • 37
    • 0031658923 scopus 로고    scopus 로고
    • The 3′-untranslated region of hepatitis C virus RNA enhances translation from an internal ribosomal entry site
    • Ito,T., Tahara,S.M. and Lai,M.M. (1998) The 3′-untranslated region of hepatitis C virus RNA enhances translation from an internal ribosomal entry site. J. Virol., 72, 8789-8796.
    • (1998) J. Virol. , vol.72 , pp. 8789-8796
    • Ito, T.1    Tahara, S.M.2    Lai, M.M.3
  • 38
    • 0030939498 scopus 로고    scopus 로고
    • RNA-RNA interaction is required for the formation of specific bicoid mRNA 3′ UTR-STAUFEN ribonucleoprotein particles
    • Ferrandon,D., Koch,I., Westhof,E. and Nusslein-Volhard,C. (1997) RNA-RNA interaction is required for the formation of specific bicoid mRNA 3′ UTR-STAUFEN ribonucleoprotein particles. EMBO J., 16, 1751-1758.
    • (1997) EMBO J. , vol.16 , pp. 1751-1758
    • Ferrandon, D.1    Koch, I.2    Westhof, E.3    Nusslein-Volhard, C.4
  • 39
    • 0036196640 scopus 로고    scopus 로고
    • A natural intergenotypic recombinant of hepatitis C virus identified in St. Petersburg
    • Kalinina,O., Norder,H., Mukomolov,S. and Magnius,L.O. (2002) A natural intergenotypic recombinant of hepatitis C virus identified in St. Petersburg. J. Virol., 76, 4034-4043.
    • (2002) J. Virol. , vol.76 , pp. 4034-4043
    • Kalinina, O.1    Norder, H.2    Mukomolov, S.3    Magnius, L.O.4
  • 41
    • 0036500976 scopus 로고    scopus 로고
    • The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding
    • Pang,P.S., Jankowsky,E., Planet,P.J. and Pyle,A.M. (2002) The hepatitis C viral NS3 protein is a processive DNA helicase with cofactor enhanced RNA unwinding. EMBO J., 21, 1168-1176.
    • (2002) EMBO J. , vol.21 , pp. 1168-1176
    • Pang, P.S.1    Jankowsky, E.2    Planet, P.J.3    Pyle, A.M.4
  • 42
    • 0035808566 scopus 로고    scopus 로고
    • Active disruption of an RNA-protein interaction by a DExH/D RNA helicase
    • Jankowsky,E., Gross,C.H., Shuman,S. and Pyle,A.M. (2001) Active disruption of an RNA-protein interaction by a DExH/D RNA helicase. Science, 291, 121-125.
    • (2001) Science , vol.291 , pp. 121-125
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 43
    • 0029938477 scopus 로고    scopus 로고
    • Identification of a highly conserved sequence element at the 3′ terminus of hepatitis C virus genome RNA
    • Kolykhalov,A.A., Feinstone,S.M. and Rice,C.M. (1996) Identification of a highly conserved sequence element at the 3′ terminus of hepatitis C virus genome RNA. J. Virol., 70, 3363-3371.
    • (1996) J. Virol. , vol.70 , pp. 3363-3371
    • Kolykhalov, A.A.1    Feinstone, S.M.2    Rice, C.M.3
  • 44
    • 0030812847 scopus 로고    scopus 로고
    • Determination of the secondary structure of and cellular protein binding to the 3′-untranslated region of the hepatitis C virus RNA genome
    • Ito,T. and Lai,M.M. (1997) Determination of the secondary structure of and cellular protein binding to the 3′-untranslated region of the hepatitis C virus RNA genome. J. Virol., 71, 8698-8706.
    • (1997) J. Virol. , vol.71 , pp. 8698-8706
    • Ito, T.1    Lai, M.M.2


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