메뉴 건너뛰기




Volumn 85, Issue 2, 2011, Pages 925-931

A dimeric Rep protein initiates replication of a linear archaeal virus genome: Implications for the Rep mechanism and viral replication

Author keywords

[No Author keywords available]

Indexed keywords

HELICASE; SIRV1 ENZYME; UNCLASSIFIED DRUG;

EID: 78650652308     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01467-10     Document Type: Article
Times cited : (34)

References (37)
  • 1
    • 0029565858 scopus 로고
    • Vaccinia virus DNA replication: A short review
    • Beaud, G. 1995. Vaccinia virus DNA replication: a short review. Biochimie 77:774-779.
    • (1995) Biochimie , vol.77 , pp. 774-779
    • Beaud, G.1
  • 2
    • 0035933282 scopus 로고    scopus 로고
    • Holliday junction resolving enzymes of archaeal viruses SIRV1 and SIRV2
    • Birkenbihl, R. P., K. Neef, D. Prangishvili, and B. Kemper. 2001. Holliday junction resolving enzymes of archaeal viruses SIRV1 and SIRV2. J. Mol. Biol. 309:1067-1076.
    • (2001) J. Mol. Biol. , vol.309 , pp. 1067-1076
    • Birkenbihl, R.P.1    Neef, K.2    Prangishvili, D.3    Kemper, B.4
  • 3
    • 0035264536 scopus 로고    scopus 로고
    • The genome of the archaeal virus SIRV1 has features in common with genomes of eukaryal viruses
    • Blum, H., W. Zillig, S. Mallok, H. Domdey, and D. Prangishvili. 2001. The genome of the archaeal virus SIRV1 has features in common with genomes of eukaryal viruses. Virology 281:6-9.
    • (2001) Virology , vol.281 , pp. 6-9
    • Blum, H.1    Zillig, W.2    Mallok, S.3    Domdey, H.4    Prangishvili, D.5
  • 6
    • 0002256769 scopus 로고    scopus 로고
    • Parvovirus DNA replication
    • M. L. DePamphilis (ed.), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY
    • Cotmore, S. F., and P. Tattersall. 1996. Parvovirus DNA replication, p. 799-813. In M. L. DePamphilis (ed.), DNA replication in eukaryotic cells, vol. 31. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
    • (1996) DNA Replication in Eukaryotic Cells , vol.31 , pp. 799-813
    • Cotmore, S.F.1    Tattersall, P.2
  • 7
    • 33747052534 scopus 로고    scopus 로고
    • DNA cleavage by the A22R resolvase of vaccinia virus
    • Culyba, M. J., J. E. Harrison, Y. Hwang, and F. D. Bushman. 2006. DNA cleavage by the A22R resolvase of vaccinia virus. Virology 352:466-476.
    • (2006) Virology , vol.352 , pp. 466-476
    • Culyba, M.J.1    Harrison, J.E.2    Hwang, Y.3    Bushman, F.D.4
  • 8
    • 0034785376 scopus 로고    scopus 로고
    • Vaccinia virus telomeres: Interaction with the viral I1, I6, and K4 proteins
    • DeMasi, J., S. Du, D. Lennon, and P. Traktman. 2001. Vaccinia virus telomeres: interaction with the viral I1, I6, and K4 proteins. J. Virol. 75:10090-10105.
    • (2001) J. Virol. , vol.75 , pp. 10090-10105
    • Demasi, J.1    Du, S.2    Lennon, D.3    Traktman, P.4
  • 10
    • 0029796546 scopus 로고    scopus 로고
    • Vaccinia virus DNA replication: Two hundred base pairs of telomeric sequence confer optimal replication efficiency on minichromosome templates
    • Du, S., and P. Traktman. 1996. Vaccinia virus DNA replication: two hundred base pairs of telomeric sequence confer optimal replication efficiency on minichromosome templates. Proc. Natl. Acad. Sci. U. S. A. 93:9693-9698.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 9693-9698
    • Du, S.1    Traktman, P.2
  • 12
    • 0034255274 scopus 로고    scopus 로고
    • Bacterial-type DNA Holliday junction resolvases in eukaryotic viruses
    • Garcia, A. D., L. Aravind, E. Koonin, and B. Moss. 2000. Bacterial-type DNA Holliday junction resolvases in eukaryotic viruses. Proc. Natl. Acad. Sci. U. S. A. 97:8926-8931.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 8926-8931
    • Garcia, A.D.1    Aravind, L.2    Koonin, E.3    Moss, B.4
  • 13
    • 0036671409 scopus 로고    scopus 로고
    • Structural unity among viral origin binding proteins: Crystal structure of the n uclease domain of adeno-associated virus Rep
    • Hickman, A. B., D. R. Ronning, R. M. Kotin, and F. Dyda. 2002. Structural unity among viral origin binding proteins: crystal structure of the n uclease domain of adeno-associated virus Rep. Mol. Cell 10:327-337.
    • (2002) Mol. Cell , vol.10 , pp. 327-337
    • Hickman, A.B.1    Ronning, D.R.2    Kotin, R.M.3    Dyda, F.4
  • 14
    • 0026748738 scopus 로고
    • Conserved sequence motifs in the initiator proteins for rolling circle DNA replication encoded by diverse replicons from eubacteria, eucaryotes and archaebacteria
    • Ilyina, T. V., and E. V. Koonin. 1992. Conserved sequence motifs in the initiator proteins for rolling circle DNA replication encoded by diverse replicons from eubacteria, eucaryotes and archaebacteria. Nucleic Acids Res. 20:3279-3285.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3279-3285
    • Ilyina, T.V.1    Koonin, E.V.2
  • 15
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and K. Henrick. 2007. Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372:774-797.
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 16
    • 22544441094 scopus 로고    scopus 로고
    • ProFunc: A server for predicting protein function from 3D structure
    • Laskowski, R. A., J. D. Watson, and J. M. Thornton. 2005. ProFunc: a server for predicting protein function from 3D structure. Nucleic Acids Res. 33:W89-W93.
    • (2005) Nucleic Acids Res. , vol.33
    • Laskowski, R.A.1    Watson, J.D.2    Thornton, J.M.3
  • 17
    • 0029042501 scopus 로고
    • In vitro cleavage and joining at the viral origin of repli- cation by the replication initiator protein of tomato yellow leaf curl virus
    • Laufs, J., W. Traut, F. Heyraud, V. Matzeit, S. G. Rogers, J. Schell, and B. Gronenborn. 1995. In vitro cleavage and joining at the viral origin of repli- cation by the replication initiator protein of tomato yellow leaf curl virus. Proc. Natl. Acad. Sci. U. S. A. 92:3879-3883.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 3879-3883
    • Laufs, J.1    Traut, W.2    Heyraud, F.3    Matzeit, V.4    Rogers, S.G.5    Schell, J.6    Gronenborn, B.7
  • 18
    • 58949085244 scopus 로고    scopus 로고
    • An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol
    • Liu, H., and J. H. Naismith. 2008. An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol. BMC Biotechnol. 8:91.
    • (2008) BMC Biotechnol. , vol.8 , pp. 91
    • Liu, H.1    Naismith, J.H.2
  • 19
    • 67650979184 scopus 로고    scopus 로고
    • Conversion of linear DNA with hairpin telomeres into a circular molecule in the course of phage N15 lytic replication
    • Mardanov, A. V., and N. V. Ravin. 2009. Conversion of linear DNA with hairpin telomeres into a circular molecule in the course of phage N15 lytic replication. J. Mol. Biol. 391:261-268.
    • (2009) J. Mol. Biol. , vol.391 , pp. 261-268
    • Mardanov, A.V.1    Ravin, N.V.2
  • 20
    • 0028024632 scopus 로고
    • Active site of the replication protein of the rolling circle plasmid pC194
    • Noirot-Gros, M. F., V. Bidnenko, and S. D. Ehrlich. 1994. Active site of the replication protein of the rolling circle plasmid pC194. EMBO J. 13:4412-4420.
    • (1994) EMBO J. , vol.13 , pp. 4412-4420
    • Noirot-Gros, M.F.1    Bidnenko, V.2    Ehrlich, S.D.3
  • 21
    • 0029908732 scopus 로고    scopus 로고
    • Change of a catalytic reaction carried out by a DNA replication protein
    • Noirot-Gros, M. F., and S. D. Ehrlich. 1996. Change of a catalytic reaction carried out by a DNA replication protein. Science 274:777-780.
    • (1996) Science , vol.274 , pp. 777-780
    • Noirot-Gros, M.F.1    Ehrlich, S.D.2
  • 22
    • 0035957520 scopus 로고    scopus 로고
    • The two active-site tyrosine residues of the A protein play non-equivalent roles during initiation of rolling circle replication of bacteriophage p2
    • Odegrip, R., and E. Haggard-Ljungquist. 2001. The two active-site tyrosine residues of the A protein play non-equivalent roles during initiation of rolling circle replication of bacteriophage p2. J. Mol. Biol. 308:147-163.
    • (2001) J. Mol. Biol. , vol.308 , pp. 147-163
    • Odegrip, R.1    Haggard-Ljungquist, E.2
  • 24
    • 0035694680 scopus 로고    scopus 로고
    • Sequences and replication of genomes of the archaeal rudiviruses SIRV1 and SIRV2: Relationships to the archaeal lipothrixvirus SIFV and some eukaryal viruses
    • Peng, X., H. Blum, Q. She, S. Mallok, K. Brugger, R. A. Garrett, W. Zillig, and D. Prangishvili. 2001. Sequences and replication of genomes of the archaeal rudiviruses SIRV1 and SIRV2: relationships to the archaeal lipothrixvirus SIFV and some eukaryal viruses. Virology 291:226-234.
    • (2001) Virology , vol.291 , pp. 226-234
    • Peng, X.1    Blum, H.2    She, Q.3    Mallok, S.4    Brugger, K.5    Garrett, R.A.6    Zillig, W.7    Prangishvili, D.8
  • 25
    • 0021352583 scopus 로고
    • Investigation of vaccinia virus DNA replication employing a conditional lethal mutant defective in DNA
    • Pogo, B. G., E. M. Berkowitz, and S. Dales. 1984. Investigation of vaccinia virus DNA replication employing a conditional lethal mutant defective in DNA. Virology 132:436-444.
    • (1984) Virology , vol.132 , pp. 436-444
    • Pogo, B.G.1    Berkowitz, E.M.2    Dales, S.3
  • 26
    • 0019419353 scopus 로고
    • Initiation and termination of vaccinia virus DNA replication
    • Pogo, B. G., M. O'Shea, and P. Freimuth. 1981. Initiation and termination of vaccinia virus DNA replication. Virology 108:241-248.
    • (1981) Virology , vol.108 , pp. 241-248
    • Pogo, B.G.1    O'shea, M.2    Freimuth, P.3
  • 27
    • 0345583680 scopus 로고    scopus 로고
    • A novel virus family, the Rudiviridae: Structure, virushost interactions and genome variability of the sulfolobus viruses SIRV1 and SIRV2
    • Prangishvili, D., H. P. Arnold, D. Gotz, U. Ziese, I. Holz, J. K. Kristjansson, and W. Zillig. 1999. A novel virus family, the Rudiviridae: structure, virushost interactions and genome variability of the sulfolobus viruses SIRV1 and SIRV2. Genetics 152:1387-1396.
    • (1999) Genetics , vol.152 , pp. 1387-1396
    • Prangishvili, D.1    Arnold, H.P.2    Gotz, D.3    Ziese, U.4    Holz, I.5    Kristjansson, J.K.6    Zillig, W.7
  • 28
    • 33645087247 scopus 로고    scopus 로고
    • Evolutionary genomics of archaeal viruses: Unique viral genomes in the third domain of life
    • Prangishvili, D., R. A. Garrett, and E. V. Koonin. 2006. Evolutionary genomics of archaeal viruses: unique viral genomes in the third domain of life. Virus Res. 117:52-67.
    • (2006) Virus Res. , vol.117 , pp. 52-67
    • Prangishvili, D.1    Garrett, R.A.2    Koonin, E.V.3
  • 29
    • 24944532259 scopus 로고    scopus 로고
    • Cytoplasmic organization of POXvirus DNA replication
    • Schramm, B., and J. K. Locker. 2005. Cytoplasmic organization of POXvirus DNA replication. Traffic 6:839-846.
    • (2005) Traffic , vol.6 , pp. 839-846
    • Schramm, B.1    Locker, J.K.2
  • 30
    • 33745288811 scopus 로고    scopus 로고
    • Demonstration of nicking/joining activity at the origin of DNA replication associated with the rep and rep' proteins of porcine circovirus type 1
    • Steinfeldt, T., T. Finsterbusch, and A. Mankertz. 2006. Demonstration of nicking/joining activity at the origin of DNA replication associated with the rep and rep' proteins of porcine circovirus type 1. J. Virol. 80:6225-6234.
    • (2006) J. Virol. , vol.80 , pp. 6225-6234
    • Steinfeldt, T.1    Finsterbusch, T.2    Mankertz, A.3
  • 31
    • 0032708385 scopus 로고    scopus 로고
    • A single rep protein initiates replication of multiple genome components of faba bean necrotic yellows virus, a single-stranded DNA virus of plants
    • Timchenko, T., F. de Kouchkovsky, L. Katul, C. David, H. J. Vetten, and B. Gronenborn. 1999. A single rep protein initiates replication of multiple genome components of faba bean necrotic yellows virus, a single-stranded DNA virus of plants. J. Virol. 73:10173-10182.
    • (1999) J. Virol. , vol.73 , pp. 10173-10182
    • Timchenko, T.1    De Kouchkovsky, F.2    Katul, L.3    David, C.4    Vetten, H.J.5    Gronenborn, B.6
  • 32
    • 33947536545 scopus 로고    scopus 로고
    • Sequence and recombination analyses of the geminivirus replication initiator protein
    • Vadivukarasi, T., K. R. Girish, and R. Usha. 2007. Sequence and recombination analyses of the geminivirus replication initiator protein. J. Biosci. 32:17-29.
    • (2007) J. Biosci. , vol.32 , pp. 17-29
    • Vadivukarasi, T.1    Girish, K.R.2    Usha, R.3
  • 33
    • 0023057871 scopus 로고
    • Two juxtaposed tyrosyl-OH groups participate in phi X174 gene A protein catalysed cleavage and ligation of DNA
    • van Mansfeld, A. D., H. A. van Teeffelen, P. D. Baas, and H. S. Jansz. 1986. Two juxtaposed tyrosyl-OH groups participate in phi X174 gene A protein catalysed cleavage and ligation of DNA. Nucleic Acids Res. 14:4229-4238.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 4229-4238
    • Van Mansfeld, A.D.1    Van Teeffelen, H.A.2    Baas, P.D.3    Jansz, H.S.4
  • 34
    • 33847235317 scopus 로고    scopus 로고
    • Solution structure, divalent metal and DNA binding of the endonuclease domain from the replication initiation protein from porcine circovirus 2
    • Vega-Rocha, S., I. J. Byeon, B. Gronenborn, A. M. Gronenborn, and R. Campos-Olivas. 2007. Solution structure, divalent metal and DNA binding of the endonuclease domain from the replication initiation protein from porcine circovirus 2. J. Mol. Biol. 367:473-487.
    • (2007) J. Mol. Biol. , vol.367 , pp. 473-487
    • Vega-Rocha, S.1    Byeon, I.J.2    Gronenborn, B.3    Gronenborn, A.M.4    Campos-Olivas, R.5
  • 35
    • 34249700716 scopus 로고    scopus 로고
    • Solution structure of the endonuclease domain from the master replication initiator protein of the nanovirus faba bean necrotic yellows virus and comparison with the corresponding geminivirus and circovirus structures
    • Vega-Rocha, S., B. Gronenborn, A. M. Gronenborn, and R. Campos-Olivas. 2007. Solution structure of the endonuclease domain from the master replication initiator protein of the nanovirus faba bean necrotic yellows virus and comparison with the corresponding geminivirus and circovirus structures. Biochemistry 46:6201-6212.
    • (2007) Biochemistry , vol.46 , pp. 6201-6212
    • Vega-Rocha, S.1    Gronenborn, B.2    Gronenborn, A.M.3    Campos-Olivas, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.