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Volumn 81, Issue 21, 2007, Pages 12077-12079

Herpes simplex virus mutants with multiple substitutions affecting DNA binding of UL42 are impaired for viral replication and DNA synthesis

Author keywords

[No Author keywords available]

Indexed keywords

DNA POLYMERASE;

EID: 35448968365     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.01133-07     Document Type: Article
Times cited : (14)

References (15)
  • 1
    • 0028826076 scopus 로고
    • Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42
    • Chow, C. S., and D. M. Coen. 1995. Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42. J. Virol. 69:6965-6971.
    • (1995) J. Virol , vol.69 , pp. 6965-6971
    • Chow, C.S.1    Coen, D.M.2
  • 2
    • 0028342556 scopus 로고
    • Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer template
    • Gottlieb, J., and M. D. Challberg. 1994. Interaction of herpes simplex virus type 1 DNA polymerase and the UL42 accessory protein with a model primer template. J. Virol. 68:4937-4945.
    • (1994) J. Virol , vol.68 , pp. 4937-4945
    • Gottlieb, J.1    Challberg, M.D.2
  • 3
    • 0025253822 scopus 로고
    • The herpes simplex virus type 1 UL42 gene product: A subunit of DNA polymerase that functions to increase processivity
    • Gottlieb, J., A. I. Marcy, D. M. Coen, and M. D. Challberg. 1990. The herpes simplex virus type 1 UL42 gene product: a subunit of DNA polymerase that functions to increase processivity. J. Virol. 64:5976-5987.
    • (1990) J. Virol , vol.64 , pp. 5976-5987
    • Gottlieb, J.1    Marcy, A.I.2    Coen, D.M.3    Challberg, M.D.4
  • 4
    • 0033957787 scopus 로고    scopus 로고
    • Sliding clamps: A (tail)ored fit
    • Hingorani, M. M., and M. Donnell. 2000. Sliding clamps: a (tail)ored fit. Curr. Biol. 10:R25-R29.
    • (2000) Curr. Biol , vol.10
    • Hingorani, M.M.1    Donnell, M.2
  • 5
    • 33947420068 scopus 로고    scopus 로고
    • Mutations that decrease DNA binding of the processivity factor of the herpes simplex DNA polymerase reduce viral yield, alter the kinetics of viral DNA replication, and decrease fidelity of DNA replication
    • Jiang, C., Y. T. Hwang, J. C. W. Randell, D. M. Coen, and C. B. C. Hwang. 2007. Mutations that decrease DNA binding of the processivity factor of the herpes simplex DNA polymerase reduce viral yield, alter the kinetics of viral DNA replication, and decrease fidelity of DNA replication. J. Virol. 81:3495-3502.
    • (2007) J. Virol , vol.81 , pp. 3495-3502
    • Jiang, C.1    Hwang, Y.T.2    Randell, J.C.W.3    Coen, D.M.4    Hwang, C.B.C.5
  • 6
    • 0025957442 scopus 로고
    • Isolation of a herpes simplex virus type 1 mutant deleted for the essential UL42 gene and characterization of its null phenotype
    • Johnson, P. A., M. G. Best, T. Friedmann, and D. S. Parris. 1991. Isolation of a herpes simplex virus type 1 mutant deleted for the essential UL42 gene and characterization of its null phenotype. J. Virol. 65:700-710.
    • (1991) J. Virol , vol.65 , pp. 700-710
    • Johnson, P.A.1    Best, M.G.2    Friedmann, T.3    Parris, D.S.4
  • 7
    • 0023871104 scopus 로고
    • A temperature-sensitive mutation in a herpes simplex virus type 1 gene required for viral DNA synthesis maps to coordinates 0.609 through 0.614 in UL
    • Marchetti, M. E., C. A. Smith, and P. A. Schaffer. 1988. A temperature-sensitive mutation in a herpes simplex virus type 1 gene required for viral DNA synthesis maps to coordinates 0.609 through 0.614 in UL. J. Virol. 62:715-721.
    • (1988) J. Virol , vol.62 , pp. 715-721
    • Marchetti, M.E.1    Smith, C.A.2    Schaffer, P.A.3
  • 8
    • 0032005707 scopus 로고    scopus 로고
    • Interaction between the herpes simplex virus type 1 origin-binding and DNA polymerase accessory proteins
    • Monahan, S. J., L. A. Grinstead, W. Olivieri, and D. S. Parris. 1998. Interaction between the herpes simplex virus type 1 origin-binding and DNA polymerase accessory proteins. Virology 241:122-130.
    • (1998) Virology , vol.241 , pp. 122-130
    • Monahan, S.J.1    Grinstead, L.A.2    Olivieri, W.3    Parris, D.S.4
  • 9
    • 0023831378 scopus 로고
    • Identification of the gene encoding the 65-kilodalton DNA-binding protein of herpes simplex virus type 1
    • Parris, D. S., A. Cross, L. Haarr, A. Orr, M. C. Frame, M. Murphy, D. J. McGeoch, and H. S. Marsden. 1988. Identification of the gene encoding the 65-kilodalton DNA-binding protein of herpes simplex virus type 1. J. Virol. 62:818-825.
    • (1988) J. Virol , vol.62 , pp. 818-825
    • Parris, D.S.1    Cross, A.2    Haarr, L.3    Orr, A.4    Frame, M.C.5    Murphy, M.6    McGeoch, D.J.7    Marsden, H.S.8
  • 10
    • 0017773789 scopus 로고
    • Identification of the herpes simplex virus DNA polymerase gene
    • Purifoy, D. J. M., R. B. Lewis, and K. L. Powell. 1977. Identification of the herpes simplex virus DNA polymerase gene. Nature 269:621-623.
    • (1977) Nature , vol.269 , pp. 621-623
    • Purifoy, D.J.M.1    Lewis, R.B.2    Powell, K.L.3
  • 11
    • 0347627532 scopus 로고    scopus 로고
    • The herpes simplex virus processivity factor, UL42, binds DNA as a monomer
    • Randell, J. C., and D. M. Coen. 2004. The herpes simplex virus processivity factor, UL42, binds DNA as a monomer. J. Mol. Biol. 335:409-413.
    • (2004) J. Mol. Biol , vol.335 , pp. 409-413
    • Randell, J.C.1    Coen, D.M.2
  • 12
    • 24644512131 scopus 로고    scopus 로고
    • Effects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesis
    • Randell, J. C., G. Komazin, C. Jiang, C. B. Hwang, and D. M. Coen. 2005. Effects of substitutions of arginine residues on the basic surface of herpes simplex virus UL42 support a role for DNA binding in processive DNA synthesis. J. Virol. 79:12025-12034.
    • (2005) J. Virol , vol.79 , pp. 12025-12034
    • Randell, J.C.1    Komazin, G.2    Jiang, C.3    Hwang, C.B.4    Coen, D.M.5
  • 13
    • 2442653990 scopus 로고    scopus 로고
    • Taylor, T. J., and D. M. Knipe. 2004. Proteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8. J. Virol. 78:5856-5866.
    • Taylor, T. J., and D. M. Knipe. 2004. Proteomics of herpes simplex virus replication compartments: association of cellular DNA replication, repair, recombination, and chromatin remodeling proteins with ICP8. J. Virol. 78:5856-5866.
  • 14
    • 0242576925 scopus 로고    scopus 로고
    • Functional interaction between the herpes simplex virus type 1 polymerase processivity factor and origin-binding proteins: Enhancement of UL9 helicase activity
    • Trego, K. S., and D. S. Parris. 2003. Functional interaction between the herpes simplex virus type 1 polymerase processivity factor and origin-binding proteins: enhancement of UL9 helicase activity. J. Virol. 77:12646-12659.
    • (2003) J. Virol , vol.77 , pp. 12646-12659
    • Trego, K.S.1    Parris, D.S.2
  • 15
    • 0032888971 scopus 로고    scopus 로고
    • Herpes simplex virus processivity factor UL42 imparts increased DNA-binding specificity to the viral DNA polymerase and decreased dissociation from primer-template without reducing the elongation rate
    • Weisshart, K., C. S. Chow, and D. M. Coen. 1999. Herpes simplex virus processivity factor UL42 imparts increased DNA-binding specificity to the viral DNA polymerase and decreased dissociation from primer-template without reducing the elongation rate. J. Virol. 73:55-66.
    • (1999) J. Virol , vol.73 , pp. 55-66
    • Weisshart, K.1    Chow, C.S.2    Coen, D.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.