메뉴 건너뛰기




Volumn 74, Issue 5, 2000, Pages 2067-2072

Interaction of the cauliflower mosaic virus coat protein with the pregenomic RNA leader

Author keywords

[No Author keywords available]

Indexed keywords

COAT PROTEIN; RNA; VIRUS DNA; VIRUS PROTEIN; ZINC FINGER PROTEIN;

EID: 0033962105     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.74.5.2067-2072.2000     Document Type: Article
Times cited : (38)

References (49)
  • 1
    • 0025266663 scopus 로고
    • Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging result in production of noninfectious virus
    • Aldovini, A., and R. A. Young. 1990. Mutations of RNA and protein sequences involved in human immunodeficiency virus type 1 packaging result in production of noninfectious virus. J. Virol. 64:1920-1926.
    • (1990) J. Virol. , vol.64 , pp. 1920-1926
    • Aldovini, A.1    Young, R.A.2
  • 2
    • 0031903417 scopus 로고    scopus 로고
    • Binding of the human immunodeficiency virus type 1 Gag protein to the viral RNA encapsidation signal in the yeast three-hybrid system
    • Bacharach, E., and S. P. Goff. 1998. Binding of the human immunodeficiency virus type 1 Gag protein to the viral RNA encapsidation signal in the yeast three-hybrid system. J. Virol. 72:6944-6949.
    • (1998) J. Virol. , vol.72 , pp. 6944-6949
    • Bacharach, E.1    Goff, S.P.2
  • 3
    • 0027336170 scopus 로고
    • Analysis of the interactions of HIV1 replication primer tRNA(Lys, 3) with nucleocapsid protein and reverse transcriptase
    • Barat, C., O. Schatz, S. Le Grice, and J. L. Darlix. 1993. Analysis of the interactions of HIV1 replication primer tRNA(Lys, 3) with nucleocapsid protein and reverse transcriptase. J. Mol. Biol. 231:185-190.
    • (1993) J. Mol. Biol. , vol.231 , pp. 185-190
    • Barat, C.1    Schatz, O.2    Le Grice, S.3    Darlix, J.L.4
  • 4
    • 0000884978 scopus 로고
    • Using the two-hybrid system to detect protein-protein interactions
    • D. A. Hartley (ed.), Oxford University Press, Oxford, United Kingdom
    • Bartel, P. L., C.-T. Chien, R. Sternglanz, and S. Fields. 1993. Using the two-hybrid system to detect protein-protein interactions, p. 153-179. In D. A. Hartley (ed.), Cellular interactions in development: a practical approach. Oxford University Press, Oxford, United Kingdom.
    • (1993) Cellular Interactions in Development: a Practical Approach , pp. 153-179
    • Bartel, P.L.1    Chien, C.-T.2    Sternglanz, R.3    Fields, S.4
  • 5
    • 0026706346 scopus 로고
    • Hepadnaviral assembly is initiated by polymerase binding to the encapsidation signal in the viral RNA genome
    • Bartenschlager, R., and H. Schaller. 1992. Hepadnaviral assembly is initiated by polymerase binding to the encapsidation signal in the viral RNA genome. EMBO J. 9:3413-3420.
    • (1992) EMBO J. , vol.9 , pp. 3413-3420
    • Bartenschlager, R.1    Schaller, H.2
  • 6
    • 0029134623 scopus 로고
    • Retroviral nucleocapsid domains mediate the specific recognition of genomic viral RNAs by chimeric gag polyproteins during RNA packaging in vivo
    • Berkowitz, R. D., A. Ohagen, S. Hoglund, and S. P. Goff. 1995. Retroviral nucleocapsid domains mediate the specific recognition of genomic viral RNAs by chimeric Gag polyproteins during RNA packaging in vivo. J. Virol. 69:6445-6456.
    • (1995) J. Virol. , vol.69 , pp. 6445-6456
    • Berkowitz, R.D.1    Ohagen, A.2    Hoglund, S.3    Goff, S.P.4
  • 8
    • 0024593741 scopus 로고
    • Biosynthesis of the reverse transcriptase of hepatitis B viruses involves de novo translational initiation not ribosomal frameshifting
    • Chang, L.-J., P. Pryciak, D. V. Ganem, and H. E. Varmus. 1989. Biosynthesis of the reverse transcriptase of hepatitis B viruses involves de novo translational initiation not ribosomal frameshifting. Nature 337:364-367.
    • (1989) Nature , vol.337 , pp. 364-367
    • Chang, L.-J.1    Pryciak, P.2    Ganem, D.V.3    Varmus, H.E.4
  • 9
    • 0031770525 scopus 로고    scopus 로고
    • The cauliflower mosaic virus capsid protein: Assembly and nucleic acid binding in vitro
    • Chapdelaine, Y., and T. Hohn. 1998. The cauliflower mosaic virus capsid protein: assembly and nucleic acid binding in vitro. Virus Genes 17:139-150.
    • (1998) Virus Genes , vol.17 , pp. 139-150
    • Chapdelaine, Y.1    Hohn, T.2
  • 10
    • 0023055867 scopus 로고
    • Amino acid sequence homology in gag region of reverse transcribing elements and the coat protein gene of cauliflower mosaic virus
    • Covey, S. N. 1986. Amino acid sequence homology in gag region of reverse transcribing elements and the coat protein gene of cauliflower mosaic virus. Nucleic Acids Res. 14:623-633.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 623-633
    • Covey, S.N.1
  • 11
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein hound to the SL3 psi-RNA recognition element
    • De Guzman, R. N., Z. R. Wu, C. C. Stalling, L. Pappalardo, P. N. Borer, and M. F. Summers. 1998. Structure of the HIV-1 nucleocapsid protein hound to the SL3 psi-RNA recognition element. Science 279:384-388.
    • (1998) Science , vol.279 , pp. 384-388
    • De Guzman, R.N.1    Wu, Z.R.2    Stalling, C.C.3    Pappalardo, L.4    Borer, P.N.5    Summers, M.F.6
  • 12
    • 0025155072 scopus 로고
    • Point mutations in the proximal Cys-His box of Rous sarcoma virus nucleocapsid protein
    • Dupraz, P., S. Oertle, C. Meric, P. Damay, and P. F. Spahr. 1990. Point mutations in the proximal Cys-His box of Rous sarcoma virus nucleocapsid protein. J. Virol. 64:4978-4987.
    • (1990) J. Virol. , vol.64 , pp. 4978-4987
    • Dupraz, P.1    Oertle, S.2    Meric, C.3    Damay, P.4    Spahr, P.F.5
  • 13
    • 84989696276 scopus 로고
    • Cauliflower mosaic virus as a gene expression vector for plants
    • Fütterer, J., J.-M. Bonneville, and T. Hohn. 1990. Cauliflower mosaic virus as a gene expression vector for plants. Physiol. Plant. 79:154-157.
    • (1990) Physiol. Plant. , vol.79 , pp. 154-157
    • Fütterer, J.1    Bonneville, J.-M.2    Hohn, T.3
  • 15
    • 0002565136 scopus 로고
    • Involvement of nucleocapsids in reverse transcription - A general phenomenon?
    • Fütterer, J., and T. Hohn. 1987. Involvement of nucleocapsids in reverse transcription - a general phenomenon? Trends Biochem. Sci. 12:92-95.
    • (1987) Trends Biochem. Sci. , vol.12 , pp. 92-95
    • Fütterer, J.1    Hohn, T.2
  • 16
    • 0027318243 scopus 로고
    • Nonlinear ribosome migration on cauliflower mosaic virus 35S RNA
    • Fütterer, J., Z. Kiss-László, and T. Hohn. 1993. Nonlinear ribosome migration on cauliflower mosaic virus 35S RNA. Cell 73:789-802.
    • (1993) Cell , vol.73 , pp. 789-802
    • Fütterer, J.1    Kiss-László, Z.2    Hohn, T.3
  • 17
    • 0019046844 scopus 로고
    • Nucleotide sequence of cauliflower mosaic virus DNA
    • Franck, A., H. Guilley, G. Jonard, K. E. Richards, and L, Hirth. 1980. Nucleotide sequence of cauliflower mosaic virus DNA. Cell 21:285-294.
    • (1980) Cell , vol.21 , pp. 285-294
    • Franck, A.1    Guilley, H.2    Jonard, G.3    Richards, K.E.4    Hirth, L.5
  • 18
    • 0031711593 scopus 로고    scopus 로고
    • HIV-1: Fifteen proteins and an RNA
    • Frankel, A. D., and J. A. Young. 1998. HIV-1: fifteen proteins and an RNA. Annu. Rev. Biochem. 67:1-25.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 1-25
    • Frankel, A.D.1    Young, J.A.2
  • 19
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz, D., A. St. Jean, R. A. Woods, and R. H. Schiestl. 1992. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20:1425-1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425-1425
    • Gietz, D.1    Jean, A.S.2    Woods, R.A.3    Schiestl, R.H.4
  • 20
    • 0024110320 scopus 로고
    • Point mutants of Moloney murine leukemia virus that fail to package viral RNA: Evidence for specific RNA recognition by a "zinc finger-like" protein sequence
    • Gorelick, R. J., L. E. Henderson, J. P. Hanser, and A. Rein. 1988 Point mutants of Moloney murine leukemia virus that fail to package viral RNA: evidence for specific RNA recognition by a "zinc finger-like" protein sequence. Proc. Natl. Acad. Sci. USA 85:8420-8424.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 8420-8424
    • Gorelick, R.J.1    Henderson, L.E.2    Hanser, J.P.3    Rein, A.4
  • 21
    • 0025893875 scopus 로고
    • An analysis of the sequence of an infectious clone of rice tungro bacilliform virus, a plant pararetrovirus
    • Hay, J. M., M. C. Jones, M. L. Blackebrough, I. Dasgupta, J. W. Davies, and R. Hull. 1991. An analysis of the sequence of an infectious clone of rice tungro bacilliform virus, a plant pararetrovirus. Nucleic Acids Res. 19:2615-2621.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 2615-2621
    • Hay, J.M.1    Jones, M.C.2    Blackebrough, M.L.3    Dasgupta, I.4    Davies, J.W.5    Hull, R.6
  • 22
    • 0031576992 scopus 로고    scopus 로고
    • Alternative structures of the cauliflower mosaic virus 35 S RNA leader: Implications for viral expression and replication
    • Hemmings-Mieszczak, M., G. Steger, and T. Hohn. 1997. Alternative structures of the cauliflower mosaic virus 35 S RNA leader: implications for viral expression and replication. J. Mol. Biol. 267:1075-1088.
    • (1997) J. Mol. Biol. , vol.267 , pp. 1075-1088
    • Hemmings-Mieszczak, M.1    Steger, G.2    Hohn, T.3
  • 23
    • 0031984932 scopus 로고    scopus 로고
    • Regulation of CaMV 35 S RNA translation is mediated by a stable hairpin in the leader
    • Hemmings-Mieszczak, M., G. Sieger, and T. Hohn. 1998. Regulation of CaMV 35 S RNA translation is mediated by a stable hairpin in the leader. RNA 4:101-111.
    • (1998) RNA , vol.4 , pp. 101-111
    • Hemmings-Mieszczak, M.1    Sieger, G.2    Hohn, T.3
  • 24
    • 0029864077 scopus 로고    scopus 로고
    • Interaction between cauliflower mosaic virus inclusion body protein and capsid protein: Implications for viral assembly
    • Himmelbach, A., Y. Chapdelaine, and T. Hohn. 1996. Interaction between cauliflower mosaic virus inclusion body protein and capsid protein: implications for viral assembly. Virology 217:147-157.
    • (1996) Virology , vol.217 , pp. 147-157
    • Himmelbach, A.1    Chapdelaine, Y.2    Hohn, T.3
  • 25
    • 0029552874 scopus 로고
    • Retroelements: Propagation and adaptation
    • Hull, R., and S. N. Covey. 1995. Retroelements: propagation and adaptation. Virus Genes 11:105-118.
    • (1995) Virus Genes , vol.11 , pp. 105-118
    • Hull, R.1    Covey, S.N.2
  • 26
    • 0029851089 scopus 로고    scopus 로고
    • Solid-phase synthesis, metal binding and folding properties of caulimovirus-related 'zinc finger'
    • Ji, H., R. Zhang, L. Lai, and M. Shao. 1996. Solid-phase synthesis, metal binding and folding properties of caulimovirus-related 'zinc finger'. Int. J. Pept. Protein Res. 48:461-464.
    • (1996) Int. J. Pept. Protein Res. , vol.48 , pp. 461-464
    • Ji, H.1    Zhang, R.2    Lai, L.3    Shao, M.4
  • 28
    • 0029020455 scopus 로고
    • Splicing of cauliflower mosaic virus 35S RNA is essential for viral infectivity
    • Kiss-László, Z., S. Blanc, and T. Hohn. 1995. Splicing of cauliflower mosaic virus 35S RNA is essential for viral infectivity. EMBO J. 14:3552-3562.
    • (1995) EMBO J. , vol.14 , pp. 3552-3562
    • Kiss-László, Z.1    Blanc, S.2    Hohn, T.3
  • 29
    • 0027452550 scopus 로고
    • Regulating the fate of mRNA: The control of cellular iron metabolism
    • Klausner, R. D., T. A. Rouault, and J. B. Harford. 1993. Regulating the fate of mRNA: the control of cellular iron metabolism. Cell 72:19-28.
    • (1993) Cell , vol.72 , pp. 19-28
    • Klausner, R.D.1    Rouault, T.A.2    Harford, J.B.3
  • 30
    • 0032582693 scopus 로고    scopus 로고
    • The open reading frame III of cauliflower mosaic virus forms a tetramer through a N-terminal coiled-coil
    • Leclerc, D., L. Burri, A. V. Kajava, J.-L. Mougeot, D. Hess, A. Lustig, G. Kleeman, and T. Hohn. 1998. The open reading frame III of cauliflower mosaic virus forms a tetramer through a N-terminal coiled-coil. J. Biol. Chem. 273:29015-29021.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29015-29021
    • Leclerc, D.1    Burri, L.2    Kajava, A.V.3    Mougeot, J.-L.4    Hess, D.5    Lustig, A.6    Kleeman, G.7    Hohn, T.8
  • 31
    • 0032889564 scopus 로고    scopus 로고
    • Nuclear targeting of the cauliflower mosaic virus coat protein
    • Leclerc, D., Y. Chapdelaine, and T. Hohn. 1999. Nuclear targeting of the cauliflower mosaic virus coat protein. J. Virol. 73:553-560.
    • (1999) J. Virol. , vol.73 , pp. 553-560
    • Leclerc, D.1    Chapdelaine, Y.2    Hohn, T.3
  • 32
    • 0033023880 scopus 로고    scopus 로고
    • Foamy viruses are unconventional retroviruses
    • Linial, M. L. 1999. Foamy viruses are unconventional retroviruses. J. Virol. 73:1747-1755.
    • (1999) J. Virol. , vol.73 , pp. 1747-1755
    • Linial, M.L.1
  • 33
    • 0023124353 scopus 로고
    • Cauliflower mosaic virus coat protein is phosphorylated in vitro by a virion associated protein kinase
    • Martinez-Izquierdo, J., and T. Hohn. 1987. Cauliflower mosaic virus coat protein is phosphorylated in vitro by a virion associated protein kinase. Proc. Natl. Acad. Sci. USA 84:1824-1828.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1824-1828
    • Martinez-Izquierdo, J.1    Hohn, T.2
  • 34
    • 0024507854 scopus 로고
    • Characterization of moloney murine leukemia virus mutants with single-amino-acid substitutions in the Cys-His box of the nucleocapsid protein
    • Meric, C., and S. P. Goff. 1989. Characterization of Moloney murine leukemia virus mutants with single-amino-acid substitutions in the Cys-His box of the nucleocapsid protein. J. Virol. 63:1558-1568.
    • (1989) J. Virol. , vol.63 , pp. 1558-1568
    • Meric, C.1    Goff, S.P.2
  • 35
    • 0023755462 scopus 로고
    • The gag gene products of human immunodeficiency virus type 1: Alignment within the gag open reading frame, identification of posttranslational modifications, and evidence for alternative gag precursors
    • Mervis, R. J., N. Ahmad, E. P. Lillehoj, M. G. Raum, F. H. Salazar, H. W. Chan, and S. Venkatesan. 1988. The gag gene products of human immunodeficiency virus type 1: alignment within the gag open reading frame, identification of posttranslational modifications, and evidence for alternative gag precursors. J. Virol. 62:3593-4002.
    • (1988) J. Virol. , vol.62 , pp. 3593-4002
    • Mervis, R.J.1    Ahmad, N.2    Lillehoj, E.P.3    Raum, M.G.4    Salazar, F.H.5    Chan, H.W.6    Venkatesan, S.7
  • 36
    • 0028841843 scopus 로고    scopus 로고
    • Comparison of packaging strategy in retroviruses and pararetroviruses
    • Mesnard, J.-M., and C. Carriere. 1996. Comparison of packaging strategy in retroviruses and pararetroviruses. Virology 213:1-6.
    • (1996) Virology , vol.213 , pp. 1-6
    • Mesnard, J.-M.1    Carriere, C.2
  • 38
    • 0344980122 scopus 로고    scopus 로고
    • A short open reading frame terminating in front of a stable hairpin is conserved feature in pregenomic RNA leaders of plant pararetroviruses
    • Pooggin, M. M., J. Fütterer, K. G. Skryabin, and T. Hohn. 1999. A short open reading frame terminating in front of a stable hairpin is conserved feature in pregenomic RNA leaders of plant pararetroviruses. J. Gen. Virol. 80:2217-2228.
    • (1999) J. Gen. Virol. , vol.80 , pp. 2217-2228
    • Pooggin, M.M.1    Fütterer, J.2    Skryabin, K.G.3    Hohn, T.4
  • 39
    • 0031969162 scopus 로고    scopus 로고
    • Forced evolution reveals the importance of short open reading frame A and secondary structure in the cauliflower mosaic virus 35S RNA leader
    • Pooggin, M. M., T. Hohn, and J. Futterer. 1998. Forced evolution reveals the importance of short open reading frame A and secondary structure in the cauliflower mosaic virus 35S RNA leader. J. Virol. 72:4157-4169.
    • (1998) J. Virol. , vol.72 , pp. 4157-4169
    • Pooggin, M.M.1    Hohn, T.2    Futterer, J.3
  • 40
    • 0027950659 scopus 로고
    • Pararetroviruses and retroviruses: A comparative review of viral structure and gene expression strategies
    • Rothnie, H. M., Y. Chapdelaine, and T. Hohn. 1994. Pararetroviruses and retroviruses: a comparative review of viral structure and gene expression strategies. Adv. Virus Res. 44:1-67.
    • (1994) Adv. Virus Res. , vol.44 , pp. 1-67
    • Rothnie, H.M.1    Chapdelaine, Y.2    Hohn, T.3
  • 41
    • 0024968115 scopus 로고
    • Synthesis and encapsidation of duck hepatitis B virus reverse transcriptase do not require formation of core-polymerase fusion proteins
    • Schlicht, H.-J., J. Salfeld, and H. Schaller. 1989. Synthesis and encapsidation of duck hepatitis B virus reverse transcriptase do not require formation of core-polymerase fusion proteins. Cell 56:85-92.
    • (1989) Cell , vol.56 , pp. 85-92
    • Schlicht, H.-J.1    Salfeld, J.2    Schaller, H.3
  • 43
    • 0029882332 scopus 로고    scopus 로고
    • An in vitro assay of β-galactosidase from yeast
    • Schneider, S., M. Buchert, and B. H. Howard. 1996. An in vitro assay of β-galactosidase from yeast. BioTechniques 20:960-962.
    • (1996) BioTechniques , vol.20 , pp. 960-962
    • Schneider, S.1    Buchert, M.2    Howard, B.H.3
  • 44
    • 0027407916 scopus 로고
    • The putative zinc finger of a caulimovirus is essential for infectivity but does not influence gene expression
    • Scholthof, H. B., F. C. Wu, J. M. Kiernan, and R. J. Shepherd. 1993 The putative zinc finger of a caulimovirus is essential for infectivity but does not influence gene expression. J. Gen. Virol. 74:775-780.
    • (1993) J. Gen. Virol. , vol.74 , pp. 775-780
    • Scholthof, H.B.1    Wu, F.C.2    Kiernan, J.M.3    Shepherd, R.J.4
  • 45
    • 0030782150 scopus 로고    scopus 로고
    • Distinct functions and requirements for the Cys-His boxes of the human immunodeficiency virus type 1 nucleocapsid protein during RNA encapsidation and replication
    • Schwartz, M. D., D. Fiore, and A. T. Panganiban. 1997. Distinct functions and requirements for the Cys-His boxes of the human immunodeficiency virus type 1 nucleocapsid protein during RNA encapsidation and replication. J. Virol. 71:9295-9305.
    • (1997) J. Virol. , vol.71 , pp. 9295-9305
    • Schwartz, M.D.1    Fiore, D.2    Panganiban, A.T.3
  • 47
    • 0001118596 scopus 로고    scopus 로고
    • Synthesis, assembly, and processing of viral proteins
    • J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • Swanstrom, R., and J. W. Wills. 1997. Synthesis, assembly, and processing of viral proteins, p. 263-334. In J. M. Coffin, S. H. Hughes, and H. E. Varmus (ed.), Retroviruses. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.W.2
  • 48
    • 0027161850 scopus 로고
    • Coat protein of cauliflower mosaic virus binds to ssDNA
    • Thompson, S. R., and U. Melcher. 1993. Coat protein of cauliflower mosaic virus binds to ssDNA. J. Gen. Virol. 74:1141-1148.
    • (1993) J. Gen. Virol. , vol.74 , pp. 1141-1148
    • Thompson, S.R.1    Melcher, U.2
  • 49
    • 0024744264 scopus 로고
    • Cauliflower mosaic virus produces an aspartic proteinase to cleave its polyproteins
    • Torruella, M., K. Gordon, and T. Hohn. 1989. Cauliflower mosaic virus produces an aspartic proteinase to cleave its polyproteins. EMBO J. 8:2819-2825.
    • (1989) EMBO J. , vol.8 , pp. 2819-2825
    • Torruella, M.1    Gordon, K.2    Hohn, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.