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Volumn , Issue , 2009, Pages 365-381

Atomic structure of the herpes simplex virus 1 DNA polymerase

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EID: 84898785449     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/b135974_17     Document Type: Chapter
Times cited : (4)

References (37)
  • 1
    • 3242688965 scopus 로고    scopus 로고
    • The cytomegalovirus DNA polymerase subunit UL44 forms a C clamp-shaped dimer
    • Appleton, B.A., Loregian, A., Filman, D.J., Coen, D.M., and Hogle, J.M. (2004). The cytomegalovirus DNA polymerase subunit UL44 forms a C clamp-shaped dimer. Mol Cell 15, 233-244.
    • (2004) Mol Cell , vol.15 , pp. 233-244
    • Appleton, B.A.1    Loregian, A.2    Filman, D.J.3    Coen, D.M.4    Hogle, J.M.5
  • 2
    • 33646167477 scopus 로고    scopus 로고
    • Crystal structure of the cytomegalovirus DNA polymerase subunit UL44 in complex with the C terminus from the catalytic subunit. Differences in structure and function relative to unliganded UL44
    • Appleton, B.A., Brooks, J., Loregian, A., Filman, D.J., Coen, D.M., and Hogle, J.M. (2006). Crystal structure of the cytomegalovirus DNA polymerase subunit UL44 in complex with the C terminus from the catalytic subunit. Differences in structure and function relative to unliganded UL44. J Biol Chem 281, 5224-5232.
    • (2006) J Biol Chem , vol.281 , pp. 5224-5232
    • Appleton, B.A.1    Brooks, J.2    Loregian, A.3    Filman, D.J.4    Coen, D.M.5    Hogle, J.M.6
  • 3
    • 1542780790 scopus 로고    scopus 로고
    • Herpes simplex virus type-1: A model for genome transactions
    • Boehmer, P.E. and Villani, G. (2003). Herpes simplex virus type-1: A model for genome transactions. Prog Nucleic Acid Res Mol Biol 75, 139-171.
    • (2003) Prog Nucleic Acid Res Mol Biol , vol.75 , pp. 139-171
    • Boehmer, P.E.1    Villani, G.2
  • 4
    • 0032005866 scopus 로고    scopus 로고
    • Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes
    • Brautigam, C. and Steitz, T.A. (1998). Structural and functional insights provided by crystal structures of DNA polymerases and their substrate complexes. Curr Opinion Struct Biol 8, 54-63.
    • (1998) Curr Opinion Struct Biol , vol.8 , pp. 54-63
    • Brautigam, C.1    Steitz, T.A.2
  • 5
    • 0035941229 scopus 로고    scopus 로고
    • Eukaryotic DNA polymerases: Proposal for a revised nomenclature
    • Burgers, P., Koonin, E., Bruford, E. et al. (2001). Eukaryotic DNA polymerases: Proposal for a revised nomenclature. J Biol Chem 276 (47), 43487-43490.
    • (2001) J Biol Chem , vol.276 , Issue.47 , pp. 43487-43490
    • Burgers, P.1    Koonin, E.2    Bruford, E.3
  • 6
    • 0038322040 scopus 로고    scopus 로고
    • The herpes simplex virus type 1DNA polymerase processivity factor increases fidelity without altering pre-steady-state rate constants for polymerization or excision
    • Chaudhuri, M., Song, L., and Parris, D. S. (2003) The Herpes Simplex Virus Type 1DNA Polymerase Processivity Factor Increases Fidelity without Altering Pre-steady-state Rate Constants for Polymerization or Excision. J Biol Chem 278, 8996-9004.
    • (2003) J Biol Chem , vol.278 , pp. 8996-9004
    • Chaudhuri, M.1    Song, L.2    Parris, D.S.3
  • 7
    • 0028826076 scopus 로고
    • Mutations that specifically impair the DNA binding activity of the herpes simplex virus protein UL42
    • Chow, C.S. and Coen, D.M. (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
  • 8
    • 0037394125 scopus 로고    scopus 로고
    • Antiherpesvirus drugs: A promising spectrum of new drugs and drug targets
    • Coen, D.M. and Schaffer, P.A. (2003). Antiherpesvirus drugs: A promising spectrum of new drugs and drug targets. Nat Rev Drug Discov 2, 278-288.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 278-288
    • Coen, D.M.1    Schaffer, P.A.2
  • 9
    • 0024793120 scopus 로고
    • Herpes simplex-1 DNA polymerase. Identification of an intrinsic 5'-3' exonuclease with ribonuclease H activity
    • Crute, J.J. and Lehman, I.R. (1989). Herpes simplex-1 DNA polymerase. Identification of an intrinsic 5'-3' exonuclease with ribonuclease H activity. J Biol Chem 264, 19266-19270.
    • (1989) J Biol Chem , vol.264 , pp. 19266-19270
    • Crute, J.J.1    Lehman, I.R.2
  • 10
    • 2342531101 scopus 로고    scopus 로고
    • Antiviral drugs in current clinical use
    • De Clercq, E. (2004). Antiviral drugs in current clinical use. J Clin Virol 30, 115-133.
    • (2004) J Clin Virol , vol.30 , pp. 115-133
    • De Clercq, E.1
  • 12
    • 0027396861 scopus 로고
    • The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication
    • Digard, P., Bebrin, W.R., Weisshart, K., and Coen, D.M. (1993). The extreme C terminus of herpes simplex virus DNA polymerase is crucial for functional interaction with processivity factor UL42 and for viral replication. J Virol 67, 398-406.
    • (1993) J Virol , vol.67 , pp. 398-406
    • Digard, P.1    Bebrin, W.R.2    Weisshart, K.3    Coen, D.M.4
  • 13
    • 0024554561 scopus 로고
    • The purine path to chemotherapy
    • Elion, G.B. (1989). The purine path to chemotherapy. Science 244, 241-247.
    • (1989) Science , vol.244 , pp. 241-247
    • Elion, G.B.1
  • 14
    • 0035369086 scopus 로고    scopus 로고
    • Structure of the replicating complex of a pol alpha family DNA polymerase
    • Franklin, M., Wang, J., and Steitz, T.A. (2001). Structure of the replicating complex of a pol alpha family DNA polymerase. Cell 105, 657-667.
    • (2001) Cell , vol.105 , pp. 657-667
    • Franklin, M.1    Wang, J.2    Steitz, T.A.3
  • 15
    • 33244478595 scopus 로고    scopus 로고
    • The eureka enzyme: The discovery of DNA polymerase
    • Friedberg, E.C. (2006). The eureka enzyme: The discovery of DNA polymerase. Nat RevMol Cell Biol 7, 143-147.
    • (2006) Nat RevMol Cell Biol , vol.7 , pp. 143-147
    • Friedberg, E.C.1
  • 16
    • 0025866597 scopus 로고
    • Polymerization activity of an alpha-like DNA polymerase requires a conserved 3'-5' exonuclease active site
    • Gibbs, J.S., Weisshart, K., Digard, P., deBruynKops, A., Knipe, D.M., and Coen, D.M.. (1991). Polymerization activity of an alpha-like DNA polymerase requires a conserved 3'-5' exonuclease active site. Mol Cell Biol 11, 4786-4795.
    • (1991) Mol Cell Biol , vol.11 , pp. 4786-4795
    • Gibbs, J.S.1    Weisshart, K.2    Digard, P.3    DeBruynKops, A.4    Knipe, D.M.5    Coen, D.M.6
  • 17
    • 0036527281 scopus 로고    scopus 로고
    • Resistance of herpesviruses to antiviral drugs: Clinical impacts and molecular mechanisms
    • Gilbert, C., Bestman-Smith, J., and Boivin, G. (2002). Resistance of herpesviruses to antiviral drugs: clinical impacts and molecular mechanisms. Drug Res Update 5, 88-114.
    • (2002) Drug Res Update , vol.5 , pp. 88-114
    • Gilbert, C.1    Bestman-Smith, J.2    Boivin, G.3
  • 18
    • 0025253822 scopus 로고
    • The herpes simplex virus type 1 UL42 gene product: A subunit of DNA polymerase that functions to increase processivity
    • Gottlieb, J., Marcy, A.I., Coen, D.M., and Challberg, M.D. (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
  • 19
    • 13044290052 scopus 로고    scopus 로고
    • The enzymological basis for resistance of herpesvirus DNA polymerase mutants to acyclovir: Relationship to the structure of alpha-like DNA polymerases
    • Huang, L., Ishi, K.K., Zuccola, H., Gehring, A.M., Hwang, C.B.C., Hogle, J., and Coen, D.M. (1999). The enzymological basis for resistance of herpesvirus DNA polymerase mutants to acyclovir: relationship to the structure of alpha-like DNA polymerases. Proc Natl Acad Sci USA 96, 447-452.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 447-452
    • Huang, L.1    Ishi, K.K.2    Zuccola, H.3    Gehring, A.M.4    Hwang, C.B.C.5    Hogle, J.6    Coen, D.M.7
  • 20
    • 0032989101 scopus 로고    scopus 로고
    • Effects of exonuclease activity and nucleotide selectivity of the herpes simplex virus DNA polymerase on the fidelity of DNA replication in vivo
    • Hwang, Y.T., Liu, B.Y., Hong, C.Y., Shillitoe, E.J., and Hwang, C.B.C. (1999). Effects of exonuclease activity and nucleotide selectivity of the herpes simplex virus DNA polymerase on the fidelity of DNA replication in vivo. J Virol 73, 5326-5332.
    • (1999) J Virol , vol.73 , pp. 5326-5332
    • Hwang, Y.T.1    Liu, B.Y.2    Hong, C.Y.3    Shillitoe, E.J.4    Hwang, C.B.C.5
  • 21
    • 0018770603 scopus 로고
    • Properties of herpes simplex virus DNA polymerase and characterization of its associated exonuclease activity
    • Knopf, K.W. (1979). Properties of herpes simplex virus DNA polymerase and characterization of its associated exonuclease activity. Eur J Biochem 98, 231-244.
    • (1979) Eur J Biochem , vol.98 , pp. 231-244
    • Knopf, K.W.1
  • 22
    • 34248220998 scopus 로고    scopus 로고
    • Temporal order of evolution of DNA replication systems inferred by comparison of cellular and viral DNA polymerases
    • Koonin, E.V. (2006). Temporal order of evolution of DNA replication systems inferred by comparison of cellular and viral DNA polymerases. Biology Direct 1, 39-57.
    • (2006) Biology Direct , vol.1 , pp. 39-57
    • Koonin, E.V.1
  • 23
    • 0033215473 scopus 로고    scopus 로고
    • Replication of herpes simplex virus DNA
    • Lehman, I.R. and Boehmer, P.E. (1999). Replication of herpes simplex virus DNA. J Bio Chem 274, 28059-28062.
    • (1999) J Bio Chem , vol.274 , pp. 28059-28062
    • Lehman, I.R.1    Boehmer, P.E.2
  • 25
    • 0030795032 scopus 로고    scopus 로고
    • The catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C terminus of the UL8 component of the viral helicase-primase complex
    • Marsden, H.S., McLean, G.W., Barnard, E.C., Francis, G.J., MacEachran, K., Murphy, M., McVey, G., Cross, A., Abbotts, A.P., and Stow, N.D. (1997). The catalytic subunit of the DNA polymerase of herpes simplex virus type 1 interacts specifically with the C terminus of the UL8 component of the viral helicase-primase complex. J Virol 71, 6390-6397.
    • (1997) J Virol , vol.71 , pp. 6390-6397
    • Marsden, H.S.1    McLean, G.W.2    Barnard, E.C.3    Francis, G.J.4    MacEachran, K.5    Murphy, M.6    McVey, G.7    Cross, A.8    Abbotts, A.P.9    Stow, N.D.10
  • 26
    • 0023831378 scopus 로고
    • Identification of the gene encoding the 65-kilodalton DNA binding protein of herpes simplex virus type 1
    • Parris, D.S., Cross, A., Haarr, L., Orr, A., Frame, M.C., Murphy, M., McGeoch, D.J., and Marsden, H.S. (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
  • 27
    • 0024584523 scopus 로고
    • Herpes simplex virus type 1 DNA polymerase. Mechanism of inhibition by acyclovir triphosphate
    • Reardon, J.E. and Spector, T. (1989). Herpes simplex virus type 1 DNA polymerase. Mechanism of inhibition by acyclovir triphosphate. J Biol Chem 264, 7405-7411.
    • (1989) J Biol Chem , vol.264 , pp. 7405-7411
    • Reardon, J.E.1    Spector, T.2
  • 28
    • 0034595517 scopus 로고    scopus 로고
    • Crystal structure of a pol alpha family DNA polymerase from the hyperthermophilic archaeon Thermococcus sp. 9 degrees N-7
    • Rodriguez, A.C., Park, H.W., Mao, C., and Beese, L.S. (2000). Crystal structure of a pol alpha family DNA polymerase from the hyperthermophilic archaeon Thermococcus sp. 9 degrees N-7. J Mol Biol 299, 447-462.
    • (2000) J Mol Biol , vol.299 , pp. 447-462
    • Rodriguez, A.C.1    Park, H.W.2    Mao, C.3    Beese, L.S.4
  • 29
    • 0032692565 scopus 로고    scopus 로고
    • Building a replisome from interacting pieces: Sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex
    • Shamoo, Y. and Steitz, T.A. (1999). Building a replisome from interacting pieces: Sliding clamp complexed to a peptide from DNA polymerase and a polymerase editing complex. Cell 99, 155-166.
    • (1999) Cell , vol.99 , pp. 155-166
    • Shamoo, Y.1    Steitz, T.A.2
  • 30
    • 2442574958 scopus 로고    scopus 로고
    • Contribution of the 3'- To 5'- exonuclease activity of herpes simplex virus type 1 DNA polymerase to the fidelity of DNA synthesis
    • Song, L., Chaudhuri, M., Knopf, C.W., and Parris, D.S. (2004). Contribution of the 3'- To 5'- exonuclease activity of herpes simplex virus type 1 DNA polymerase to the fidelity of DNA synthesis. J Biol Chem 279, 18535-18543.
    • (2004) J Biol Chem , vol.279 , pp. 18535-18543
    • Song, L.1    Chaudhuri, M.2    Knopf, C.W.3    Parris, D.S.4
  • 31
    • 0033581011 scopus 로고    scopus 로고
    • DNA polymerases: Structural diversity and common mechanisms
    • Steitz, T.A. (1999). DNA polymerases: Structural diversity and common mechanisms. J Biol Chem 274, 17395-17398.
    • (1999) J Biol Chem , vol.274 , pp. 17395-17398
    • Steitz, T.A.1
  • 32
    • 0037303608 scopus 로고    scopus 로고
    • Amino acid changes within conserved region III of the herpes simplex virus and human cytomegalovirus DNA polymerases confer resistance to 4-oxo-dihydroquinolines, a novel class of herpesvirus antiviral agents
    • Thomsen, D.R., Oien, N.L., Hopkins, T.A., Knechtel, M.L., Brideau, R.J., Wathen, M.W., and Homa, F.L. (2003). Amino acid changes within conserved region III of the herpes simplex virus and human cytomegalovirus DNA polymerases confer resistance to 4-oxo-dihydroquinolines, a novel class of herpesvirus antiviral agents. J Virol 77, 1868-1876.
    • (2003) J Virol , vol.77 , pp. 1868-1876
    • Thomsen, D.R.1    Oien, N.L.2    Hopkins, T.A.3    Knechtel, M.L.4    Brideau, R.J.5    Wathen, M.W.6    Homa, F.L.7
  • 33
    • 0031587827 scopus 로고    scopus 로고
    • Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69
    • Wang, J., Sattar, A., Wang, C.C., Karam, J.D., Konigsberg, W.H., and Steitz, T. A. (1997). Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69. Cell 89, 1087-1099.
    • (1997) Cell , vol.89 , pp. 1087-1099
    • Wang, J.1    Sattar, A.2    Wang, C.C.3    Karam, J.D.4    Konigsberg, W.H.5    Steitz, T.A.6
  • 34
    • 0036093153 scopus 로고    scopus 로고
    • Non-nucleoside inhibitors of herpesviruses
    • Wathen, M.W. (2002). Non-nucleoside inhibitors of herpesviruses. Rev Med Virol 12, 167-178.
    • (2002) Rev Med Virol , vol.12 , pp. 167-178
    • Wathen, M.W.1
  • 35
    • 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., Chow, C.S., and Coen, D.M. (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
  • 37
    • 0033867542 scopus 로고    scopus 로고
    • The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase
    • Zuccola, H.J., Filman, D.J., Coen, D.M., and Hogle, J.M. (2000). The crystal structure of an unusual processivity factor, herpes simplex virus UL42, bound to the C terminus of its cognate polymerase. Mol Cell 5, 267-278.
    • (2000) Mol Cell , vol.5 , pp. 267-278
    • Zuccola, H.J.1    Filman, D.J.2    Coen, D.M.3    Hogle, J.M.4


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