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Volumn 342, Issue 4, 2006, Pages 1188-1196

Biochemical characterization of Periplaneta fuliginosa densovirus non-structural protein NS1

Author keywords

ATPase; Far Western; Helicase; NS1; Oligomerization; Periplaneta fuliginosa densovirus; South Western; Yeast two hybrid

Indexed keywords

DNA FRAGMENT; DOUBLE STRANDED DNA; HELICASE; MAGNESIUM ION; MALTOSE BINDING PROTEIN; MANGANESE; NONSTRUCTURAL PROTEIN 1; RECOMBINANT PROTEIN; SINGLE STRANDED DNA; UNCLASSIFIED DRUG; VIRUS DNA; VIRUS PROTEIN;

EID: 33644913102     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2006.02.053     Document Type: Article
Times cited : (22)

References (46)
  • 1
    • 0000023308 scopus 로고
    • Densonucleosis viruses constitute an increasingly diversified subfamily among the parvoviruses
    • P. Tijssen, and M. Bergoin Densonucleosis viruses constitute an increasingly diversified subfamily among the parvoviruses Semin. Virol. 6 1995 347 355
    • (1995) Semin. Virol. , vol.6 , pp. 347-355
    • Tijssen, P.1    Bergoin, M.2
  • 2
    • 0026802505 scopus 로고
    • Complete nucleotide sequence of the cloned infectious genome of Junonia coenia densovirus reveals an organization unique among parvoviruses
    • B. Dumas, M. Jourdan, A.M. Pascaud, and M. Bergoin Complete nucleotide sequence of the cloned infectious genome of Junonia coenia densovirus reveals an organization unique among parvoviruses Virology 191 1992 202 222
    • (1992) Virology , vol.191 , pp. 202-222
    • Dumas, B.1    Jourdan, M.2    Pascaud, A.M.3    Bergoin, M.4
  • 4
    • 0025998886 scopus 로고
    • Nucleotide sequence and genomic organization of Aedes densonucleosis virus
    • B.N. Afanasiev, E.E. Galyov, L.P. Buchatsky, and Y.V. Kozlov Nucleotide sequence and genomic organization of Aedes densonucleosis virus Virology 185 1991 323 336
    • (1991) Virology , vol.185 , pp. 323-336
    • Afanasiev, B.N.1    Galyov, E.E.2    Buchatsky, L.P.3    Kozlov, Y.V.4
  • 5
    • 0028350191 scopus 로고
    • Complete nucleotide sequence and genomic organization of the Aedes albopictus parvovirus (AaPV) pathogenic for Aedes aegypti larvae
    • Y. Boublik, F.X. Jousset, and M. Bergoin Complete nucleotide sequence and genomic organization of the Aedes albopictus parvovirus (AaPV) pathogenic for Aedes aegypti larvae Virology 200 1994 752 763
    • (1994) Virology , vol.200 , pp. 752-763
    • Boublik, Y.1    Jousset, F.X.2    Bergoin, M.3
  • 6
    • 0034634322 scopus 로고    scopus 로고
    • Infectious hypodermal and hematopoietic necrosis virus of shrimp is related to mosquito Brevidensoviruses
    • H. Shike, A.K. Dhar, J.C. Burns, C. Shimizu, F.X. Jousset, K.R. Klimpel, and M. Bergoin Infectious hypodermal and hematopoietic necrosis virus of shrimp is related to mosquito Brevidensoviruses Virology 277 2000 167 177
    • (2000) Virology , vol.277 , pp. 167-177
    • Shike, H.1    Dhar, A.K.2    Burns, J.C.3    Shimizu, C.4    Jousset, F.X.5    Klimpel, K.R.6    Bergoin, M.7
  • 7
    • 0036060436 scopus 로고    scopus 로고
    • Genome organization of Casphalia extranea densovirus, a new Iteravirus
    • G. Fédière, Y. Li, Z. Zádori, J. Szelei, and P. Tijssen Genome organization of Casphalia extranea densovirus, a new Iteravirus Virology 292 2002 299 308
    • (2002) Virology , vol.292 , pp. 299-308
    • Fédière, G.1    Li, Y.2    Zádori, Z.3    Szelei, J.4    Tijssen, P.5
  • 8
    • 0034782919 scopus 로고    scopus 로고
    • Genome organization of the densovirus from Bombyx mori (BmDNV-1) and enzyme activity of its capsid
    • Y. Li, Z. Zádori, H. Bando, R. Dubuc, G. Fédière, J. Szelei, and P. Tijssen Genome organization of the densovirus from Bombyx mori (BmDNV-1) and enzyme activity of its capsid J. Gen. Virol. 82 2001 2821 2825
    • (2001) J. Gen. Virol. , vol.82 , pp. 2821-2825
    • Li, Y.1    Zádori, Z.2    Bando, H.3    Dubuc, R.4    Fédière, G.5    Szelei, J.6    Tijssen, P.7
  • 9
    • 12944258616 scopus 로고    scopus 로고
    • Changes to virus taxonomy 2004
    • M.A. Mayo Changes to virus taxonomy 2004 Arch. Virol. 150 2004 189 198
    • (2004) Arch. Virol. , vol.150 , pp. 189-198
    • Mayo, M.A.1
  • 10
    • 0034466121 scopus 로고    scopus 로고
    • Complete sequence and organization of Periplaneta fuliginosa densovirus genome
    • H.T. Guo, J.M. Zhang, and Y.Y. Hu Complete sequence and organization of Periplaneta fuliginosa densovirus genome Acta Virol. 44 2000 315 322
    • (2000) Acta Virol. , vol.44 , pp. 315-322
    • Guo, H.T.1    Zhang, J.M.2    Hu, Y.Y.3
  • 11
    • 0020684648 scopus 로고
    • Nucleotide sequence and organization of the adeno-associated virus 2 genome
    • A. Srivastava, E. Lusby, and K. Berns Nucleotide sequence and organization of the adeno-associated virus 2 genome J. Virol. 45 1983 555 564
    • (1983) J. Virol. , vol.45 , pp. 555-564
    • Srivastava, A.1    Lusby, E.2    Berns, K.3
  • 12
    • 0025034511 scopus 로고
    • Terminal structure of a densovirus implies a hairpin transfer replication which is similar to the model for AAV
    • H. Bando, H. Choi, Y. Ito, and S. Kawase Terminal structure of a densovirus implies a hairpin transfer replication which is similar to the model for AAV Virology 179 1990 57 63
    • (1990) Virology , vol.179 , pp. 57-63
    • Bando, H.1    Choi, H.2    Ito, Y.3    Kawase, S.4
  • 13
    • 0022470376 scopus 로고
    • Nucleotide sequence and genome organization of human parvovirus B19 isolated from the serum of a child during aplastic crisis
    • R.O. Shade, M. Blundell, S.F. Cotmore, P. Tattersall, and C.R. Astell Nucleotide sequence and genome organization of human parvovirus B19 isolated from the serum of a child during aplastic crisis J. Virol. 58 1986 921 936
    • (1986) J. Virol. , vol.58 , pp. 921-936
    • Shade, R.O.1    Blundell, M.2    Cotmore, S.F.3    Tattersall, P.4    Astell, C.R.5
  • 14
    • 0032729127 scopus 로고    scopus 로고
    • Genome organization and mRNA structure of Periplaneta fuliginosa densovirus imply alternative splicing involvement in viral gene expression
    • J. Yamagishi, Y. Hu, J. Zheng, and H. Bando Genome organization and mRNA structure of Periplaneta fuliginosa densovirus imply alternative splicing involvement in viral gene expression Arch. Virol. 144 1999 2111 2124
    • (1999) Arch. Virol. , vol.144 , pp. 2111-2124
    • Yamagishi, J.1    Hu, Y.2    Zheng, J.3    Bando, H.4
  • 15
    • 0025282292 scopus 로고
    • Cloning of minute virus of mice cDNAs and preliminary analysis of individual viral proteins expressed in murine cells
    • K.E. Clemens, D.R. Cerutis, L.R. Burger, Q. Yang, and D.J. Pintel Cloning of minute virus of mice cDNAs and preliminary analysis of individual viral proteins expressed in murine cells J. Virol. 64 1990 3967 3973
    • (1990) J. Virol. , vol.64 , pp. 3967-3973
    • Clemens, K.E.1    Cerutis, D.R.2    Burger, L.R.3    Yang, Q.4    Pintel, D.J.5
  • 16
    • 0026802053 scopus 로고
    • In vitro excision and replication of 5′ telomeres of minute virus of mice DNA from cloned palindromic concatemer junctions
    • S.F. Cotmore, J.P.F. Nuesch, and P. Tattersall In vitro excision and replication of 5′ telomeres of minute virus of mice DNA from cloned palindromic concatemer junctions Virology 190 1992 365 377
    • (1992) Virology , vol.190 , pp. 365-377
    • Cotmore, S.F.1    Nuesch, J.P.F.2    Tattersall, P.3
  • 17
    • 0028143560 scopus 로고
    • Sequence requirements for stable binding and function of Rep68 on the adeno-associated virus type 2 inverted terminal repeats
    • J.A. Chiorini, S.M. Wiener, R.A. Owens, S.R. Kyostio, R.M. Kotin, and B. Safer Sequence requirements for stable binding and function of Rep68 on the adeno-associated virus type 2 inverted terminal repeats J. Virol. 68 1994 7448 7457
    • (1994) J. Virol. , vol.68 , pp. 7448-7457
    • Chiorini, J.A.1    Wiener, S.M.2    Owens, R.A.3    Kyostio, S.R.4    Kotin, R.M.5    Safer, B.6
  • 18
    • 0026501098 scopus 로고
    • In vivo resolution of circular plasmids containing concatemer junction fragments from minute virus of mice DNA and their subsequent replication as linear molecules
    • S.F. Cotmore, and P. Tattersall In vivo resolution of circular plasmids containing concatemer junction fragments from minute virus of mice DNA and their subsequent replication as linear molecules J. Virol. 66 1992 420 431
    • (1992) J. Virol. , vol.66 , pp. 420-431
    • Cotmore, S.F.1    Tattersall, P.2
  • 20
    • 0025362618 scopus 로고
    • The AAV origin binding protein Rep68 is an ATP-dependent site-specific endonuclease with DNA helicase activity
    • D.S. Im, and N. Muzyczka The AAV origin binding protein Rep68 is an ATP-dependent site-specific endonuclease with DNA helicase activity Cell 61 1990 447 457
    • (1990) Cell , vol.61 , pp. 447-457
    • Im, D.S.1    Muzyczka, N.2
  • 21
    • 0027476207 scopus 로고
    • Identification of a DNA-binding domain in the amino terminus of adeno-associated virus Rep protein
    • R.A. Owens, M.D. Weitzman, S.R. Kyostio, and B.J. Carter Identification of a DNA-binding domain in the amino terminus of adeno-associated virus Rep protein J. Virol. 67 1993 997 1005
    • (1993) J. Virol. , vol.67 , pp. 997-1005
    • Owens, R.A.1    Weitzman, M.D.2    Kyostio, S.R.3    Carter, B.J.4
  • 22
    • 0030896669 scopus 로고    scopus 로고
    • Mutational analysis of the adeno-associated virus Rep68 protein: Identification of critical residues necessary for site-specific endonuclease activity
    • S.L. Walker, R.S. Wonderling, and R.A. Owens Mutational analysis of the adeno-associated virus Rep68 protein: identification of critical residues necessary for site-specific endonuclease activity J. Virol. 71 1997 2722 2730
    • (1997) J. Virol. , vol.71 , pp. 2722-2730
    • Walker, S.L.1    Wonderling, R.S.2    Owens, R.A.3
  • 23
    • 0028136544 scopus 로고
    • Mutations in the NTP-binding motif of minute virus of mice (MVM) NS1 protein uncouple ATPase and DNA helicase functions
    • H.K. Jindal, C.B. Yong, G.M. Wilson, P. Tam, and C.R. Astell Mutations in the NTP-binding motif of minute virus of mice (MVM) NS1 protein uncouple ATPase and DNA helicase functions J. Biol. Chem. 269 1994 3283 3289
    • (1994) J. Biol. Chem. , vol.269 , pp. 3283-3289
    • Jindal, H.K.1    Yong, C.B.2    Wilson, G.M.3    Tam, P.4    Astell, C.R.5
  • 24
    • 0026748738 scopus 로고
    • Conserved sequence motifs in the initiator proteins for rolling circle DNA replication encoded by diverse replicons from eubacteria, eucaryotes, and archaebacteria
    • T.V. Ilyina, and E.V. Koonin Conserved sequence motifs in the initiator proteins for rolling circle DNA replication encoded by diverse replicons from eubacteria, eucaryotes, and archaebacteria Nucleic Acids Res. 20 1992 3279 3285
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3279-3285
    • Ilyina, T.V.1    Koonin, E.V.2
  • 26
    • 0028124463 scopus 로고
    • The two-hybrid system: An assay for protein-protein interactions
    • S. Fields, and R. Sternglanz The two-hybrid system: an assay for protein-protein interactions Trends Genet. 10 1994 286 292
    • (1994) Trends Genet. , vol.10 , pp. 286-292
    • Fields, S.1    Sternglanz, R.2
  • 27
    • 0023680201 scopus 로고
    • Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein
    • C. Guana, P. Lib, P.D. Riggsa, and H. Inouyeb Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein Gene 67 1988 21 30
    • (1988) Gene , vol.67 , pp. 21-30
    • Guana, C.1    Lib, P.2    Riggsa, P.D.3    Inouyeb, H.4
  • 28
    • 0028107265 scopus 로고
    • Biologically active Rep proteins of adeno-associated virus type 2 produced as fusion proteins in Escherichia coli
    • J.A. Chiorini, M.D. Weitzman, R.A. Owens, E. Urcelay, B. Safer, and R.M. Kotin Biologically active Rep proteins of adeno-associated virus type 2 produced as fusion proteins in Escherichia coli J. Virol. 68 1994 797 804
    • (1994) J. Virol. , vol.68 , pp. 797-804
    • Chiorini, J.A.1    Weitzman, M.D.2    Owens, R.A.3    Urcelay, E.4    Safer, B.5    Kotin, R.M.6
  • 30
    • 0030978731 scopus 로고    scopus 로고
    • Maize streak virus coat protein binds single- and double-stranded DNA in vitro
    • H. Liu, M.I. Boulton, and J.W. Davies Maize streak virus coat protein binds single- and double-stranded DNA in vitro J. Gen. Virol. 78 1997 1265 1270
    • (1997) J. Gen. Virol. , vol.78 , pp. 1265-1270
    • Liu, H.1    Boulton, M.I.2    Davies, J.W.3
  • 31
    • 0028290387 scopus 로고
    • Identification of linear DNA sequences that specifically bind the adeno-associated virus Rep protein
    • D.M. McCarty, D.J. Pereira, I. Zolotukhin, X. Zhou, J.H. Ryan, and N. Muzyczka Identification of linear DNA sequences that specifically bind the adeno-associated virus Rep protein J. Virol. 68 1994 4988 4997
    • (1994) J. Virol. , vol.68 , pp. 4988-4997
    • McCarty, D.M.1    Pereira, D.J.2    Zolotukhin, I.3    Zhou, X.4    Ryan, J.H.5    Muzyczka, N.6
  • 33
    • 0032954382 scopus 로고    scopus 로고
    • Biochemical characterization of adeno-associated virus Rep68 DNA helicase and ATPase activities
    • X. Zhou, I. Zolotukhin, D.S. Im, and N. Muzyczka Biochemical characterization of adeno-associated virus Rep68 DNA helicase and ATPase activities J. Virol. 73 1999 1580 1590
    • (1999) J. Virol. , vol.73 , pp. 1580-1590
    • Zhou, X.1    Zolotukhin, I.2    Im, D.S.3    Muzyczka, N.4
  • 34
    • 0029007446 scopus 로고
    • Bovine papillomavirus type 1 E1 ATPase activity does not depend on binding to DNA nor to viral E2 protein
    • S. Santucci, C.B. Andrea, and P. Clertant Bovine papillomavirus type 1 E1 ATPase activity does not depend on binding to DNA nor to viral E2 protein J. Gen. Virol. 76 1995 1129 1140
    • (1995) J. Gen. Virol. , vol.76 , pp. 1129-1140
    • Santucci, S.1    Andrea, C.B.2    Clertant, P.3
  • 35
    • 0029784485 scopus 로고    scopus 로고
    • A steady-state and pre-steady-state kinetic analysis of the NTPase activity associated with the hepatitis C virus NS3 helicase domain
    • F. Preugschat, D.R. Averett, B.E. Clarke, and D.J.T. Porter A steady-state and pre-steady-state kinetic analysis of the NTPase activity associated with the hepatitis C virus NS3 helicase domain J. Biol. Chem. 271 1996 24449 24457
    • (1996) J. Biol. Chem. , vol.271 , pp. 24449-24457
    • Preugschat, F.1    Averett, D.R.2    Clarke, B.E.3    Porter, D.J.T.4
  • 36
    • 0021071027 scopus 로고
    • The gene 4 protein of bacteriophage T7. Characterization of helicase activity
    • S.W. Matson, S. Tabor, and C.C. Richardson The gene 4 protein of bacteriophage T7. Characterization of helicase activity J. Biol. Chem. 258 1983 14017 14024
    • (1983) J. Biol. Chem. , vol.258 , pp. 14017-14024
    • Matson, S.W.1    Tabor, S.2    Richardson, C.C.3
  • 37
    • 0022977660 scopus 로고
    • The Escherichia coli DnaB replication protein is a DNA helicase
    • J.H. LeBowitz, and R. McMacken The Escherichia coli DnaB replication protein is a DNA helicase J. Biol. Chem. 261 1986 4738 4748
    • (1986) J. Biol. Chem. , vol.261 , pp. 4738-4748
    • Lebowitz, J.H.1    McMacken, R.2
  • 38
    • 2442706340 scopus 로고    scopus 로고
    • Unraveling DNA helicases: Motif, structure, mechanism, and function
    • N. Tutejia, and R. Tutejia Unraveling DNA helicases: Motif, structure, mechanism, and function Eur. J. Biochem. 271 2004 1849 1863
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1849-1863
    • Tutejia, N.1    Tutejia, R.2
  • 40
    • 0027405966 scopus 로고
    • Asymmetric resolution of a parvovirus palindrome in vitro
    • S.F. Cotmore, J.P. Nuesch, and P. Tattersall Asymmetric resolution of a parvovirus palindrome in vitro J. Virol. 67 1993 1579 1589
    • (1993) J. Virol. , vol.67 , pp. 1579-1589
    • Cotmore, S.F.1    Nuesch, J.P.2    Tattersall, P.3
  • 41
    • 0023856253 scopus 로고
    • The NS-1 polypeptide of minute virus of mice is covalently attached to the 59 termini of duplex replicative form DNA and progeny single strands
    • S.F. Cotmore, and P. Tattersall The NS-1 polypeptide of minute virus of mice is covalently attached to the 59 termini of duplex replicative form DNA and progeny single strands J. Virol. 62 1988 851 860
    • (1988) J. Virol. , vol.62 , pp. 851-860
    • Cotmore, S.F.1    Tattersall, P.2
  • 42
    • 0024469826 scopus 로고
    • Both excision and replication of cloned autonomous parvovirus DNA require the NS1 (rep) protein
    • S.L. Rhode III Both excision and replication of cloned autonomous parvovirus DNA require the NS1 (rep) protein J. Virol. 63 1989 4249 4256
    • (1989) J. Virol. , vol.63 , pp. 4249-4256
    • Rhode III, S.L.1
  • 43
    • 0027518667 scopus 로고
    • Helicase-catalyzed DNA unwinding
    • T.M. Lohman Helicase-catalyzed DNA unwinding J. Biol. Chem. 268 1993 2269 2272
    • (1993) J. Biol. Chem. , vol.268 , pp. 2269-2272
    • Lohman, T.M.1
  • 44
    • 0030947409 scopus 로고    scopus 로고
    • The Rep78 gene product of adeno-associated virus (AAV) self-associates to form a hexameric complex in the presence of AAV ori sequences
    • R.H. Smith, A.J. Spano, and R.M. Kotin The Rep78 gene product of adeno-associated virus (AAV) self-associates to form a hexameric complex in the presence of AAV ori sequences J. Virol. 71 1997 4461 4471
    • (1997) J. Virol. , vol.71 , pp. 4461-4471
    • Smith, R.H.1    Spano, A.J.2    Kotin, R.M.3
  • 45
    • 0026773870 scopus 로고
    • The GC box and TATA transcription control elements in the P38 promoter of the minute virus of mice are necessary and sufficient for transactivation by the nonstructural protein NS1
    • J.K. Ahn, Z.W. Pitluk, and D.C. Ward The GC box and TATA transcription control elements in the P38 promoter of the minute virus of mice are necessary and sufficient for transactivation by the nonstructural protein NS1 J. Virol. 66 1992 3776 3783
    • (1992) J. Virol. , vol.66 , pp. 3776-3783
    • Ahn, J.K.1    Pitluk, Z.W.2    Ward, D.C.3
  • 46
    • 0032889252 scopus 로고    scopus 로고
    • A novel heterogeneous nuclear ribonucleoprotein-like protein interacts with NS1 of the minute virus of mice
    • C.E. Harris, R.A. Boden, and C.R. Astell A novel heterogeneous nuclear ribonucleoprotein-like protein interacts with NS1 of the minute virus of mice J. Virol. 73 1999 72 80
    • (1999) J. Virol. , vol.73 , pp. 72-80
    • Harris, C.E.1    Boden, R.A.2    Astell, C.R.3


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