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Volumn 47, Issue 34, 2008, Pages 8977-8984

Interaction of herpes primase with the sugar of a NTP

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL REACTIONS; FLOW INTERACTIONS; FLUORINE; HYDROGEN; MONOMERS; NONMETALS; NUCLEIC ACIDS; ORGANIC ACIDS; POLYMERIZATION; POLYMERS; SUGAR (SUCROSE);

EID: 50149098782     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi8008467     Document Type: Article
Times cited : (6)

References (36)
  • 1
    • 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
  • 2
    • 0037377759 scopus 로고    scopus 로고
    • Recruitment of polymerase to herpes simplex virus type 1 replication foci in cells expressing mutant primase (UL52) proteins
    • Carrington-Lawrence, S. D., and Weller, S. K. (2003) Recruitment of polymerase to herpes simplex virus type 1 replication foci in cells expressing mutant primase (UL52) proteins. J. Virol. 77, 4237-4247.
    • (2003) J. Virol , vol.77 , pp. 4237-4247
    • Carrington-Lawrence, S.D.1    Weller, S.K.2
  • 4
    • 0025292145 scopus 로고
    • Herpes simplex virus helicase-primase: The UL8 protein is not required for DNA-dependent ATPase and DNA helicase activities
    • Calder, J. M., and Stow, N. D. (1990) Herpes simplex virus helicase-primase: the UL8 protein is not required for DNA-dependent ATPase and DNA helicase activities. Nucleic Acids Res. 18, 3573-3578.
    • (1990) Nucleic Acids Res , vol.18 , pp. 3573-3578
    • Calder, J.M.1    Stow, N.D.2
  • 5
    • 0026073154 scopus 로고
    • Association of DNA helicase and primase activities with a subassembly of the herpes simplex virus 1 helicase-primase composed of the UL5 and UL52 gene products
    • Dodson, M. S., and Lehman, I. R. (1991) Association of DNA helicase and primase activities with a subassembly of the herpes simplex virus 1 helicase-primase composed of the UL5 and UL52 gene products. Proc. Natl. Acad. Sci. U.S.A. 88, 1105-1109.
    • (1991) Proc. Natl. Acad. Sci. U.S.A , vol.88 , pp. 1105-1109
    • Dodson, M.S.1    Lehman, I.R.2
  • 6
    • 0026632424 scopus 로고
    • The UL8 subunit of the herpes simplex virus helicase-primase complex is required for efficient primer utilization
    • Sherman, G., Gottlieb, J., and Challberg, M. D. (1992) The UL8 subunit of the herpes simplex virus helicase-primase complex is required for efficient primer utilization. J. Virol. 66, 4884-48892.
    • (1992) J. Virol , vol.66 , pp. 4884-48892
    • Sherman, G.1    Gottlieb, J.2    Challberg, M.D.3
  • 7
    • 0030930191 scopus 로고    scopus 로고
    • The UL8 subunit of the heterotrimeric herpes simplex virus type 1 helicase-primase is required for the unwinding of single stand DNA-binding protein (ICP8)-coated DNA substrates
    • Falkenberg, M., Bushnell, D. A., Elias, P., and Lehman, I. R. (1997) The UL8 subunit of the heterotrimeric herpes simplex virus type 1 helicase-primase is required for the unwinding of single stand DNA-binding protein (ICP8)-coated DNA substrates. J. Biol. Chem. 272, 22766-22770.
    • (1997) J. Biol. Chem , vol.272 , pp. 22766-22770
    • Falkenberg, M.1    Bushnell, D.A.2    Elias, P.3    Lehman, I.R.4
  • 8
    • 0007398685 scopus 로고    scopus 로고
    • Herpes simplex virus type-1 single-strand DNA-binding protein (ICP8) enhances the ability of the viral DNA helicase-primase to unwind cisplatin-modified DNA
    • Gac, N. T. L., Villani, G., and Boehmer, P. E. (1998) Herpes simplex virus type-1 single-strand DNA-binding protein (ICP8) enhances the ability of the viral DNA helicase-primase to unwind cisplatin-modified DNA. J. Biol. Chem. 273, 13801-13807.
    • (1998) J. Biol. Chem , vol.273 , pp. 13801-13807
    • Gac, N.T.L.1    Villani, G.2    Boehmer, P.E.3
  • 9
    • 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
    • Mardsen, 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
    • Mardsen, 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
  • 10
    • 0027991973 scopus 로고
    • The herpes simplex virus type 1 origin-binding protein interacts specifically with the viral UL8 protein
    • McLean, G. W., Abbotts, A. P., Parry, M. E., Marsden, H. S., and Stow, N. D. (1994) The herpes simplex virus type 1 origin-binding protein interacts specifically with the viral UL8 protein. J. Gen. Virol. 75, 2699-2706.
    • (1994) J. Gen. Virol , vol.75 , pp. 2699-2706
    • McLean, G.W.1    Abbotts, A.P.2    Parry, M.E.3    Marsden, H.S.4    Stow, N.D.5
  • 11
    • 0028075341 scopus 로고
    • The UL8 component of the herpes simplex virus helicase-primase complex stimulates primer synthesis by a subassembly of the UL5 and UL52 components
    • Tenney, D. J., Hurlburt, W. W., Micheletti, P. A., Bifano, M., and Hamatake, R. K. (1994) The UL8 component of the herpes simplex virus helicase-primase complex stimulates primer synthesis by a subassembly of the UL5 and UL52 components. J. Biol. Chem. 269, 5030-5035.
    • (1994) J. Biol. Chem , vol.269 , pp. 5030-5035
    • Tenney, D.J.1    Hurlburt, W.W.2    Micheletti, P.A.3    Bifano, M.4    Hamatake, R.K.5
  • 12
    • 0037058824 scopus 로고    scopus 로고
    • 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, 4569-4579.
    • 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, 4569-4579.
  • 13
    • 0022852279 scopus 로고
    • Studies of the DNA helicase-RNA primase unit from bacteriophage T4. A trinucleotide sequence on the DNA template starts RNA primer synthesis
    • Cha, T. A., and Alberts, B. M. (1986) Studies of the DNA helicase-RNA primase unit from bacteriophage T4. A trinucleotide sequence on the DNA template starts RNA primer synthesis. J. Biol. Chem. 261, 7001-7010.
    • (1986) J. Biol. Chem , vol.261 , pp. 7001-7010
    • Cha, T.A.1    Alberts, B.M.2
  • 14
    • 0024806757 scopus 로고
    • Structural features of the priming signal recognized by primase: Mutational analysis of the phage G4 origin of complementary DNA strand synthesis
    • Hiasa, H., Sakai, H., Tanaka, K., Honda, Y., Komano, T., and Godson, G. N. (1989) Structural features of the priming signal recognized by primase: mutational analysis of the phage G4 origin of complementary DNA strand synthesis. Gene 84, 9-16.
    • (1989) Gene , vol.84 , pp. 9-16
    • Hiasa, H.1    Sakai, H.2    Tanaka, K.3    Honda, Y.4    Komano, T.5    Godson, G.N.6
  • 15
    • 0026356394 scopus 로고
    • Requirements for primer synthesis by bacteriophage T7 63-kDa gene 4 protein. Roles of template sequence and T7 56-kDa gene 4 protein
    • Mendelman, L. V., and Richardson, C. C. (1991) Requirements for primer synthesis by bacteriophage T7 63-kDa gene 4 protein. Roles of template sequence and T7 56-kDa gene 4 protein. J. Biol. Chem. 266, 23240-23250.
    • (1991) J. Biol. Chem , vol.266 , pp. 23240-23250
    • Mendelman, L.V.1    Richardson, C.C.2
  • 16
    • 0025782760 scopus 로고
    • Specificity of recognition sequence for Eschericia coli primase
    • Yoda, K., and Okazaki, T. (1991) Specificity of recognition sequence for Eschericia coli primase. Mol. Gen. Genet. 227, 1-8.
    • (1991) Mol. Gen. Genet , vol.227 , pp. 1-8
    • Yoda, K.1    Okazaki, T.2
  • 17
    • 0027513148 scopus 로고
    • The mechanism of calf thymus DNA primase: Slow initiation, rapid polymerization and intelligent termination
    • Sheaff, R., and Kuchta, R. D. (1993) The mechanism of calf thymus DNA primase: slow initiation, rapid polymerization and intelligent termination. Biochemistry 32, 3027-3037.
    • (1993) Biochemistry , vol.32 , pp. 3027-3037
    • Sheaff, R.1    Kuchta, R.D.2
  • 19
    • 3142762309 scopus 로고    scopus 로고
    • Herpes simplex virus I DNA primase: A polymerase with extraordinarily low fidelity
    • Ramirez-Aguilar, K. A., and Kuchta, R. D. (2004) Herpes simplex virus I DNA primase: a polymerase with extraordinarily low fidelity. Biochemistry 43, 9084-9091.
    • (2004) Biochemistry , vol.43 , pp. 9084-9091
    • Ramirez-Aguilar, K.A.1    Kuchta, R.D.2
  • 20
    • 28244441232 scopus 로고    scopus 로고
    • Herpes simplex virus I primase employs watson-crick hydrogen bonding to identify cognate NTPs
    • Ramirez-Aguilar, K. A., Moore, C. L., and Kuchta, R. D. (2005) Herpes simplex virus I primase employs watson-crick hydrogen bonding to identify cognate NTPs. Biochemistry 44, 15585-15593.
    • (2005) Biochemistry , vol.44 , pp. 15585-15593
    • Ramirez-Aguilar, K.A.1    Moore, C.L.2    Kuchta, R.D.3
  • 21
    • 33846300306 scopus 로고    scopus 로고
    • Human DNA polymerase alpha uses a combination of positive and negative selectivity to polymerize purine dNTPs with high fidelity
    • Beckman, J., Kincaid, K., Hocek, M., Spratt, T., Engels, J., Cosstick, R., and Kuchta, R. D. (2007) Human DNA polymerase alpha uses a combination of positive and negative selectivity to polymerize purine dNTPs with high fidelity. Biochemistry 46, 448-460.
    • (2007) Biochemistry , vol.46 , pp. 448-460
    • Beckman, J.1    Kincaid, K.2    Hocek, M.3    Spratt, T.4    Engels, J.5    Cosstick, R.6    Kuchta, R.D.7
  • 22
    • 0028928572 scopus 로고
    • Acyclic guanosine analogs inhibit DNA polymerases alpha, delta and epsilon with very different potencies and have unique mechanisms of action
    • Ilsley, D. I., Lee, S. H., Miller, W., and Kuchta, R. D. (1995) Acyclic guanosine analogs inhibit DNA polymerases alpha, delta and epsilon with very different potencies and have unique mechanisms of action. Biochemistry 34, 2504-2510.
    • (1995) Biochemistry , vol.34 , pp. 2504-2510
    • Ilsley, D.I.1    Lee, S.H.2    Miller, W.3    Kuchta, R.D.4
  • 23
    • 0025970299 scopus 로고
    • Inhibition of DNA primase by 9-beta-D-arabinofuranosyladenosine triphosphate
    • Kuchta, R. D., and Willhelm, L. (1991) Inhibition of DNA primase by 9-beta-D-arabinofuranosyladenosine triphosphate. Biochemistry 30, 797-803.
    • (1991) Biochemistry , vol.30 , pp. 797-803
    • Kuchta, R.D.1    Willhelm, L.2
  • 24
    • 0026637347 scopus 로고
    • Inhibition of DNA primase and polymerase alpha by arabinofuranosylnucleoside triphosphates and related compounds
    • Kuchta, R. D., Ilsley, D., Kravig, K. D., Schubert, S., and Harris, B. (1992) Inhibition of DNA primase and polymerase alpha by arabinofuranosylnucleoside triphosphates and related compounds. Biochemistry 31, 4720-4728.
    • (1992) Biochemistry , vol.31 , pp. 4720-4728
    • Kuchta, R.D.1    Ilsley, D.2    Kravig, K.D.3    Schubert, S.4    Harris, B.5
  • 25
    • 0042318450 scopus 로고    scopus 로고
    • Facile polymerization of dNTPs bearing unatural base analogues by DNA polymerase alpha and klenow fragment (DNA polymerase I)
    • Chiaramonte, M., Moore, C. L., Kincaid, K., and Kuchta, R. D. (2003) Facile polymerization of dNTPs bearing unatural base analogues by DNA polymerase alpha and klenow fragment (DNA polymerase I). Biochemistry 42, 10472-10481.
    • (2003) Biochemistry , vol.42 , pp. 10472-10481
    • Chiaramonte, M.1    Moore, C.L.2    Kincaid, K.3    Kuchta, R.D.4
  • 26
    • 1042265191 scopus 로고    scopus 로고
    • Mechanism of primer synthesis by the herpes simplex virus 1 helicase-primase
    • Ramirez-Aguilar, K., and Kuchta, R. D. (2004) Mechanism of primer synthesis by the herpes simplex virus 1 helicase-primase. Biochemistry 43, 1103-1112.
    • (2004) Biochemistry , vol.43 , pp. 1103-1112
    • Ramirez-Aguilar, K.1    Kuchta, R.D.2
  • 27
    • 0026464542 scopus 로고
    • Kinetic characterization of the polymerase and exonuclease activities of the gene 43 protein of bacteriophage T4
    • Capson, T., Peliska, J. A., Kaboord, B. F., West, M. F., Lively, C., Dahlberg, M., and Benkovic, S. J. (1992) Kinetic characterization of the polymerase and exonuclease activities of the gene 43 protein of bacteriophage T4. Biochemistry 31, 10984-10994.
    • (1992) Biochemistry , vol.31 , pp. 10984-10994
    • Capson, T.1    Peliska, J.A.2    Kaboord, B.F.3    West, M.F.4    Lively, C.5    Dahlberg, M.6    Benkovic, S.J.7
  • 28
    • 14644432415 scopus 로고    scopus 로고
    • Base selectivity is impaired by mutants that perturb hydrogen bonding networks in the RB69 DNA polymerase active site
    • Yang, G., Wang, J., and Konigsberg, W. (2005) Base selectivity is impaired by mutants that perturb hydrogen bonding networks in the RB69 DNA polymerase active site. Biochemistry 44, 3338-3346.
    • (2005) Biochemistry , vol.44 , pp. 3338-3346
    • Yang, G.1    Wang, J.2    Konigsberg, W.3
  • 29
    • 33747462891 scopus 로고    scopus 로고
    • A new paradigm for DNA polymerase specificity
    • Tsai, Y.-C., and Johnson, K. A. (2006) A new paradigm for DNA polymerase specificity. Biochemistry 45, 9675-9687.
    • (2006) Biochemistry , vol.45 , pp. 9675-9687
    • Tsai, Y.-C.1    Johnson, K.A.2
  • 30
    • 0025051277 scopus 로고
    • DNA primase: Processivity and the primase to polymerase alpha activity switch
    • Kuchta, R. D., Reid, B., and Chang, L. M. S. (1990) DNA primase: processivity and the primase to polymerase alpha activity switch. J. Biol. Chem. 265, 16158-16165.
    • (1990) J. Biol. Chem , vol.265 , pp. 16158-16165
    • Kuchta, R.D.1    Reid, B.2    Chang, L.M.S.3
  • 31
    • 0037180395 scopus 로고    scopus 로고
    • Synthesis of nucleotide analogues that potently and selectively inhibit human primase
    • Moore, C. L., Chiaramonte, M., Higgins, T., and Kuchta, R. D. (2002) Synthesis of nucleotide analogues that potently and selectively inhibit human primase. Biochemistry 41, 14066-14075.
    • (2002) Biochemistry , vol.41 , pp. 14066-14075
    • Moore, C.L.1    Chiaramonte, M.2    Higgins, T.3    Kuchta, R.D.4
  • 32
    • 8844232440 scopus 로고    scopus 로고
    • Polymerization of the triphosphates of AraC 2′,2′-difluorodeoxycytidine and ThioAraC by human DNA polymerase alpha and DNA primase
    • Richardson, K. A., Vega, T. P., Moore, C. L., Rohloff, J. C., Tomkinson, B., Bendele, R. A., Richardson, F. C., and Kuchta, R. D. (2004) Polymerization of the triphosphates of AraC 2′,2′-difluorodeoxycytidine and ThioAraC by human DNA polymerase alpha and DNA primase. Biochem. Pharmacol. 68, 2337-2346.
    • (2004) Biochem. Pharmacol , vol.68 , pp. 2337-2346
    • Richardson, K.A.1    Vega, T.P.2    Moore, C.L.3    Rohloff, J.C.4    Tomkinson, B.5    Bendele, R.A.6    Richardson, F.C.7    Kuchta, R.D.8
  • 33
    • 0028038222 scopus 로고
    • Misincorporation of nucleotides by calf thymus DNA primase and elongation of primers containing multiple non-cognate nucleotides by DNA polymerase alpha
    • Sheaff, R., and Kuchta, R. D. (1994) Misincorporation of nucleotides by calf thymus DNA primase and elongation of primers containing multiple non-cognate nucleotides by DNA polymerase alpha. J. Biol. Chem. 269, 19225-19231.
    • (1994) J. Biol. Chem , vol.269 , pp. 19225-19231
    • Sheaff, R.1    Kuchta, R.D.2
  • 34
    • 22444435033 scopus 로고    scopus 로고
    • Origin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: Structural insights and new members
    • Lakshminarayan, M. I., Koonin, E. V., Leipe, D. D., and Aravind, L. (2005) Origin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: structural insights and new members. Nucleic Acids Res. 33, 3875-3896w.
    • (2005) Nucleic Acids Res , vol.33
    • Lakshminarayan, M.I.1    Koonin, E.V.2    Leipe, D.D.3    Aravind, L.4
  • 35
    • 0028998313 scopus 로고
    • Identification of the Primase active site of the herpes simplex virus type I helicase-primase
    • Dracheva, S., Koonin, E. V., and Crute, J. J. (1995) Identification of the Primase active site of the herpes simplex virus type I helicase-primase. J. Biol. Chem. 270, 14148-14153.
    • (1995) J. Biol. Chem , vol.270 , pp. 14148-14153
    • Dracheva, S.1    Koonin, E.V.2    Crute, J.J.3
  • 36
    • 0033564245 scopus 로고    scopus 로고
    • Arg304 of human DNA primase is a key contributor to catalysis and NTP binding: Primase and the family X polymerases share significant sequence homology
    • Kirk, B. W., and Kuchta, R. D. (1999) Arg304 of human DNA primase is a key contributor to catalysis and NTP binding: primase and the family X polymerases share significant sequence homology. Biochemistry 38, 7727-7737.
    • (1999) Biochemistry , vol.38 , pp. 7727-7737
    • Kirk, B.W.1    Kuchta, R.D.2


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