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Volumn 54, Issue 2, 2015, Pages 240-249

Polymerase and exonuclease activities in herpes simplex virus type 1 DNA polymerase are not highly coordinated

Author keywords

[No Author keywords available]

Indexed keywords

BINDING SITES; DNA; NUCLEOTIDES; OLIGONUCLEOTIDES; VIRUSES;

EID: 84922330345     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500840v     Document Type: Article
Times cited : (12)

References (46)
  • 1
    • 0021688781 scopus 로고
    • Novel interaction of aphidicolin with herpes simplex virus DNA polymerase and polymerase-associated exonuclease
    • Frank, K. B., Derse, D. D., Bastow, K. F., and Cheng, Y. C. (1984) Novel interaction of aphidicolin with herpes simplex virus DNA polymerase and polymerase-associated exonuclease J. Biol. Chem. 259, 13282-13286
    • (1984) J. Biol. Chem. , vol.259 , pp. 13282-13286
    • Frank, K.B.1    Derse, D.D.2    Bastow, K.F.3    Cheng, Y.C.4
  • 3
    • 0031008223 scopus 로고    scopus 로고
    • Herpes simplex virus DNA replication
    • Boehmer, P. E. and Lehman, I. R. (1997) Herpes simplex virus DNA replication Annu. Rev. Biochem. 66, 347-384
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 347-384
    • Boehmer, P.E.1    Lehman, I.R.2
  • 5
    • 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. Biol. Chem. 274, 28059-28062
    • (1999) J. Biol. Chem. , vol.274 , pp. 28059-28062
    • Lehman, I.R.1    Boehmer, P.E.2
  • 6
    • 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
  • 7
    • 0038322040 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 DNA 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 1 DNA 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
  • 8
    • 0023091627 scopus 로고
    • Cyclin/PCNA is the auxiliary protein of DNA polymerase-delta
    • Bravo, R., Frank, R., Blundell, P. A., and Macdonald-Bravo, H. (1987) Cyclin/PCNA is the auxiliary protein of DNA polymerase-delta Nature 326, 515-517
    • (1987) Nature , vol.326 , pp. 515-517
    • Bravo, R.1    Frank, R.2    Blundell, P.A.3    Macdonald-Bravo, H.4
  • 9
    • 0025809742 scopus 로고
    • Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme
    • Stukenberg, P. T., Studwell-Vaughan, P. S., and ODonnell, M. (1991) Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme J. Biol. Chem. 266, 11328-11334
    • (1991) J. Biol. Chem. , vol.266 , pp. 11328-11334
    • Stukenberg, P.T.1    Studwell-Vaughan, P.S.2    Odonnell, M.3
  • 10
    • 0023665337 scopus 로고
    • Escherichia coli thioredoxin stabilizes complexes of bacteriophage T7 DNA polymerase and primed templates
    • Huber, H. E., Tabor, S., and Richardson, C. C. (1987) Escherichia coli thioredoxin stabilizes complexes of bacteriophage T7 DNA polymerase and primed templates J. Biol. Chem. 262, 16224-16232
    • (1987) J. Biol. Chem. , vol.262 , pp. 16224-16232
    • Huber, H.E.1    Tabor, S.2    Richardson, C.C.3
  • 11
    • 0023665251 scopus 로고
    • Escherichia coli thioredoxin confers processivity on the DNA polymerase activity of the gene 5 protein of bacteriophage T7
    • Tabor, S., Huber, H. E., and Richardson, C. C. (1987) Escherichia coli thioredoxin confers processivity on the DNA polymerase activity of the gene 5 protein of bacteriophage T7 J. Biol. Chem. 262, 16212-16223
    • (1987) J. Biol. Chem. , vol.262 , pp. 16212-16223
    • Tabor, S.1    Huber, H.E.2    Richardson, C.C.3
  • 12
    • 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
  • 13
    • 0027997561 scopus 로고
    • Detecting the ability of viral, bacterial and eukaryotic replication proteins to track along DNA
    • Tinker, R. L., Kassavetis, G. A., and Geiduschek, E. P. (1994) Detecting the ability of viral, bacterial and eukaryotic replication proteins to track along DNA EMBO J. 13, 5330-5337
    • (1994) EMBO J. , vol.13 , pp. 5330-5337
    • Tinker, R.L.1    Kassavetis, G.A.2    Geiduschek, E.P.3
  • 14
    • 0026717535 scopus 로고
    • Three-dimensional structure of the beta subunit of E. Coli DNA polymerase III holoenzyme: A sliding DNA clamp
    • Kong, X. P., Onrust, R., ODonnell, M., and Kuriyan, J. (1992) Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp Cell 69, 425-437
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.P.1    Onrust, R.2    Odonnell, M.3    Kuriyan, J.4
  • 15
    • 0028618183 scopus 로고
    • Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA
    • Krishna, T. S., Kong, X. P., Gary, S., Burgers, P. M., and Kuriyan, J. (1994) Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA Cell 79, 1233-1243
    • (1994) Cell , vol.79 , pp. 1233-1243
    • Krishna, T.S.1    Kong, X.P.2    Gary, S.3    Burgers, P.M.4    Kuriyan, J.5
  • 16
    • 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
  • 17
    • 0347627532 scopus 로고    scopus 로고
    • The herpes simplex virus processivity factor, UL42, binds DNA as a monomer
    • Randell, J. C. and Coen, D. M. (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
  • 18
    • 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
  • 19
    • 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
  • 20
    • 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
  • 21
    • 67650908759 scopus 로고    scopus 로고
    • Mutations that increase DNA binding by the processivity factor of herpes simplex virus affect virus production and DNA replication fidelity
    • Jiang, C., Komazin-Meredith, G., Tian, W., Coen, D. M., and Hwang, C. B. (2009) Mutations that increase DNA binding by the processivity factor of herpes simplex virus affect virus production and DNA replication fidelity J. Virol. 83, 7573-7580
    • (2009) J. Virol. , vol.83 , pp. 7573-7580
    • Jiang, C.1    Komazin-Meredith, G.2    Tian, W.3    Coen, D.M.4    Hwang, C.B.5
  • 23
    • 0037058824 scopus 로고    scopus 로고
    • Key role of template sequence for primer synthesis by the herpes simplex virus 1 helicase-primase
    • Ramirez-Aguilar, K. A., Low-Nam, N. A., and Kuchta, R. D. (2002) Key role of template sequence for primer synthesis by the herpes simplex virus 1 helicase-primase Biochemistry 41, 14569-14579
    • (2002) Biochemistry , vol.41 , pp. 14569-14579
    • Ramirez-Aguilar, K.A.1    Low-Nam, N.A.2    Kuchta, R.D.3
  • 25
    • 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 Challberg, M. D. (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
  • 26
    • 0024549097 scopus 로고
    • DNA substrate structural requirements for the exonuclease and polymerase activities of procaryotic and phage DNA polymerases
    • Cowart, M., Gibson, K. J., Allen, D. J., and Benkovic, S. J. (1989) DNA substrate structural requirements for the exonuclease and polymerase activities of procaryotic and phage DNA polymerases Biochemistry 28, 1975-1983
    • (1989) Biochemistry , vol.28 , pp. 1975-1983
    • Cowart, M.1    Gibson, K.J.2    Allen, D.J.3    Benkovic, S.J.4
  • 27
    • 0027337930 scopus 로고
    • DNA polymerase epsilon: Aphidicolin inhibition and the relationship between polymerase and exonuclease activity
    • Cheng, C. H. and Kuchta, R. D. (1993) DNA polymerase epsilon: aphidicolin inhibition and the relationship between polymerase and exonuclease activity Biochemistry 32, 8568-8574
    • (1993) Biochemistry , vol.32 , pp. 8568-8574
    • Cheng, C.H.1    Kuchta, R.D.2
  • 28
    • 0025950771 scopus 로고
    • Mechanism of DNA polymerase alpha inhibition by aphidicolin
    • Sheaff, R., Ilsley, D., and Kuchta, R. (1991) Mechanism of DNA polymerase alpha inhibition by aphidicolin Biochemistry 30, 8590-8597
    • (1991) Biochemistry , vol.30 , pp. 8590-8597
    • Sheaff, R.1    Ilsley, D.2    Kuchta, R.3
  • 30
    • 0030025084 scopus 로고    scopus 로고
    • Exonucleolytic proofreading during replication of repetitive DNA
    • Kroutil, L. C., Register, K., Bebenek, K., and Kunkel, T. A. (1996) Exonucleolytic proofreading during replication of repetitive DNA Biochemistry 35, 1046-1053
    • (1996) Biochemistry , vol.35 , pp. 1046-1053
    • Kroutil, L.C.1    Register, K.2    Bebenek, K.3    Kunkel, T.A.4
  • 31
    • 0029017879 scopus 로고
    • Purification and properties of wild-type and exonuclease-deficient DNA polymerase II from Escherichia coli
    • Cai, H., Yu, H., McEntee, K., Kunkel, T. A., and Goodman, M. F. (1995) Purification and properties of wild-type and exonuclease-deficient DNA polymerase II from Escherichia coli J. Biol. Chem. 270, 15327-15335
    • (1995) J. Biol. Chem. , vol.270 , pp. 15327-15335
    • Cai, H.1    Yu, H.2    McEntee, K.3    Kunkel, T.A.4    Goodman, M.F.5
  • 32
    • 0027482444 scopus 로고
    • Base selection, proofreading, and mismatch repair during DNA replication in Escherichia coli
    • Schaaper, R. M. (1993) Base selection, proofreading, and mismatch repair during DNA replication in Escherichia coli J. Biol. Chem. 268, 23762-23765
    • (1993) J. Biol. Chem. , vol.268 , pp. 23762-23765
    • Schaaper, R.M.1
  • 33
    • 0026643492 scopus 로고
    • Processive proofreading is intrinsic to T4 DNA polymerase
    • Reddy, M. K., Weitzel, S. E., and von Hippel, P. H. (1992) Processive proofreading is intrinsic to T4 DNA polymerase J. Biol. Chem. 267, 14157-14166
    • (1992) J. Biol. Chem. , vol.267 , pp. 14157-14166
    • Reddy, M.K.1    Weitzel, S.E.2    Von Hippel, P.H.3
  • 34
    • 0025963376 scopus 로고
    • Kinetic partitioning between the exonuclease and polymerase sites in DNA error correction
    • Donlin, M. J., Patel, S. S., and Johnson, K. A. (1991) Kinetic partitioning between the exonuclease and polymerase sites in DNA error correction Biochemistry 30, 538-546
    • (1991) Biochemistry , vol.30 , pp. 538-546
    • Donlin, M.J.1    Patel, S.S.2    Johnson, K.A.3
  • 36
    • 0035851098 scopus 로고    scopus 로고
    • Exonuclease proofreading by human mitochondrial DNA polymerase
    • Johnson, A. A. and Johnson, K. A. (2001) Exonuclease proofreading by human mitochondrial DNA polymerase J. Biol. Chem. 276, 38097-38107
    • (2001) J. Biol. Chem. , vol.276 , pp. 38097-38107
    • Johnson, A.A.1    Johnson, K.A.2
  • 38
    • 0031550641 scopus 로고    scopus 로고
    • Assembly of herpes simplex virus replication proteins at two distinct intranuclear sites
    • Uprichard, S. L. and Knipe, D. M. (1997) Assembly of herpes simplex virus replication proteins at two distinct intranuclear sites Virology 229, 113-125
    • (1997) Virology , vol.229 , pp. 113-125
    • Uprichard, S.L.1    Knipe, D.M.2
  • 39
    • 0023677817 scopus 로고
    • Tyrosyl-tRNA synthetase acts as an asymmetric dimer in charging tRNA. A rationale for half-of-the-sites activity
    • Ward, W. H. and Fersht, A. R. (1988) Tyrosyl-tRNA synthetase acts as an asymmetric dimer in charging tRNA. A rationale for half-of-the-sites activity Biochemistry 27, 5525-5530
    • (1988) Biochemistry , vol.27 , pp. 5525-5530
    • Ward, W.H.1    Fersht, A.R.2
  • 40
    • 0026019625 scopus 로고
    • Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: A two metal ion mechanism
    • Beese, L. S. and Steitz, T. A. (1991) Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism EMBO J. 10, 25-33
    • (1991) EMBO J. , vol.10 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 41
    • 0029666424 scopus 로고    scopus 로고
    • 2-terminal fragment of T4 DNA polymerase and its complexes with single-stranded DNA and with divalent metal ions
    • 2-terminal fragment of T4 DNA polymerase and its complexes with single-stranded DNA and with divalent metal ions Biochemistry 35, 8110-8119
    • (1996) Biochemistry , vol.35 , pp. 8110-8119
    • Wang, J.1    Yu, P.2    Lin, T.C.3    Konigsberg, W.H.4    Steitz, T.A.5
  • 42
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
    • Doublie, S., Tabor, S., Long, A. M., Richardson, C. C., and Ellenberger, T. (1998) Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution Nature 391, 251-258
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 43
    • 0035369086 scopus 로고    scopus 로고
    • Structure of the replicating complex of a pol alpha family DNA polymerase
    • Franklin, M. C., 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.C.1    Wang, J.2    Steitz, T.A.3
  • 44
    • 84861584310 scopus 로고    scopus 로고
    • Contribution of partial charge interactions and base stacking to the efficiency of primer extension at and beyond abasic sites in DNA
    • Xia, S., Vashishtha, A., Bulkley, D., Eom, S. H., Wang, J., and Konigsberg, W. H. (2012) Contribution of partial charge interactions and base stacking to the efficiency of primer extension at and beyond abasic sites in DNA Biochemistry 51, 4922-4931
    • (2012) Biochemistry , vol.51 , pp. 4922-4931
    • Xia, S.1    Vashishtha, A.2    Bulkley, D.3    Eom, S.H.4    Wang, J.5    Konigsberg, W.H.6
  • 45
    • 0024397102 scopus 로고
    • Inactivation of DNA polymerase i (Klenow fragment) by adenosine 2′,3′-epoxide 5′-triphosphate: Evidence for the formation of a tight-binding inhibitor
    • Catalano, C. E. and Benkovic, S. J. (1989) Inactivation of DNA polymerase I (Klenow fragment) by adenosine 2′,3′-epoxide 5′-triphosphate: evidence for the formation of a tight-binding inhibitor Biochemistry 28, 4374-4382
    • (1989) Biochemistry , vol.28 , pp. 4374-4382
    • Catalano, C.E.1    Benkovic, S.J.2
  • 46
    • 84860390395 scopus 로고    scopus 로고
    • A crystallographic study of the role of sequence context in thymine glycol bypass by a replicative DNA polymerase serendipitously sheds light on the exonuclease complex
    • Aller, P., Duclos, S., Wallace, S. S., and Doublie, S. (2011) A crystallographic study of the role of sequence context in thymine glycol bypass by a replicative DNA polymerase serendipitously sheds light on the exonuclease complex J. Mol. Biol. 412, 22-34
    • (2011) J. Mol. Biol. , vol.412 , pp. 22-34
    • Aller, P.1    Duclos, S.2    Wallace, S.S.3    Doublie, S.4


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