메뉴 건너뛰기




Volumn 1804, Issue 5, 2010, Pages 1180-1189

Mechanism and evolution of DNA primases

Author keywords

Counting; dNTP; Fidelity; Inhibition; Initiation; Mechanism; Misincorporation; NTP; Polymerase; Primase

Indexed keywords

DEOXYRIBONUCLEOSIDE TRIPHOSPHATE; DNA POLYMERASE; DNA PRIMASE; HELICASE;

EID: 77949570959     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.06.011     Document Type: Review
Times cited : (114)

References (94)
  • 2
    • 0025640874 scopus 로고
    • Accuracy of DNA primase
    • Zhang S.-S., and Grosse F. Accuracy of DNA primase. J. Mol. Biol. 216 (1990) 475-479
    • (1990) J. Mol. Biol. , vol.216 , pp. 475-479
    • Zhang, S.-S.1    Grosse, F.2
  • 3
    • 0004820396 scopus 로고
    • Analysis of nucleotide pools in animal cells
    • Hauschka P.V. Analysis of nucleotide pools in animal cells. Methods Cell Biol. 3 (1973) 362-462
    • (1973) Methods Cell Biol. , vol.3 , pp. 362-462
    • Hauschka, P.V.1
  • 4
    • 36248984797 scopus 로고    scopus 로고
    • The heterodimeric primase from the euryarchaeon Pyrococcus abyssi: a multifunctional enzyme for initiation and repair?
    • LeBreton M., Henneke G., Norais C., Flament D., Myllykallio H., Querellou J., and Raffin J.P. The heterodimeric primase from the euryarchaeon Pyrococcus abyssi: a multifunctional enzyme for initiation and repair?. J. Mol. Biol. 374 (2007) 1172-1185
    • (2007) J. Mol. Biol. , vol.374 , pp. 1172-1185
    • LeBreton, M.1    Henneke, G.2    Norais, C.3    Flament, D.4    Myllykallio, H.5    Querellou, J.6    Raffin, J.P.7
  • 5
    • 9244224132 scopus 로고    scopus 로고
    • The heterodimeric primase of the hyperthermophilic archaeon Sulfolobus solfataricus possesses DNA and RNA primase, polymerase, and 3′-terminal nucleotidyl transferase activities
    • Lao-Sireix S.-H., and Bell S.D. The heterodimeric primase of the hyperthermophilic archaeon Sulfolobus solfataricus possesses DNA and RNA primase, polymerase, and 3′-terminal nucleotidyl transferase activities. J. Mol. Biol. 344 (2004) 1251-1263
    • (2004) J. Mol. Biol. , vol.344 , pp. 1251-1263
    • Lao-Sireix, S.-H.1    Bell, S.D.2
  • 6
    • 0029128798 scopus 로고
    • Telomerase and DNA end replication: no longer a lagging strand problem
    • Lingner J., Cooper J.P., and Cech T.R. Telomerase and DNA end replication: no longer a lagging strand problem,. Science 269 (1995) 1533-1534
    • (1995) Science , vol.269 , pp. 1533-1534
    • Lingner, J.1    Cooper, J.P.2    Cech, T.R.3
  • 7
    • 0027256834 scopus 로고
    • The adenovirus terminal protein influences binding of replication proteins and changes the origin structure
    • Pronk R., and van del Vliet P.C. The adenovirus terminal protein influences binding of replication proteins and changes the origin structure. Nucleic Ac. Res. 21 (1993) 2293-2300
    • (1993) Nucleic Ac. Res. , vol.21 , pp. 2293-2300
    • Pronk, R.1    van del Vliet, P.C.2
  • 8
    • 33747639275 scopus 로고    scopus 로고
    • Conserved sequence box II directs transcription termination and primer formation in mitochondria
    • Pham X.H., Farge G., Shi Y., Gaspari M., Gustafsson C.M., and Falkenberg M. Conserved sequence box II directs transcription termination and primer formation in mitochondria. J. Biol. Chem. 281 (2006) 24057-24062
    • (2006) J. Biol. Chem. , vol.281 , pp. 24057-24062
    • Pham, X.H.1    Farge, G.2    Shi, Y.3    Gaspari, M.4    Gustafsson, C.M.5    Falkenberg, M.6
  • 10
    • 0030812830 scopus 로고    scopus 로고
    • Primer tRNAs for reverse transcription
    • Mak J., and Kleiman L. Primer tRNAs for reverse transcription. J. Virol. 71 (1997) 8087-8095
    • (1997) J. Virol. , vol.71 , pp. 8087-8095
    • Mak, J.1    Kleiman, L.2
  • 12
    • 0032530488 scopus 로고    scopus 로고
    • Toprim - a conserved catalytic domain in type IA and II topoisomerases, DnaG-type Primases, OLD family nucleases and RecR proteins
    • Aravind L., Leipe D.D., and Koonin E.V. Toprim - a conserved catalytic domain in type IA and II topoisomerases, DnaG-type Primases, OLD family nucleases and RecR proteins. Nucleic Acids Res. 26 (1998) 4205-4213
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4205-4213
    • Aravind, L.1    Leipe, D.D.2    Koonin, E.V.3
  • 13
    • 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. Origin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: structural insights and new members. Nucleic Acids Res. 33 (2005) 3875-3896w
    • (2005) Nucleic Acids Res. , vol.33
    • Lakshminarayan, M.I.1    Koonin, E.V.2    Leipe, D.D.3    Aravind, L.4
  • 14
    • 0033613231 scopus 로고    scopus 로고
    • Interactions of DNA with human DNA primase monitored with photoactivatable cross-linking agents: implications for the role of the p58 subunit
    • Arezi B., Kirk B.W., Copeland W.C., and Kuchta R.D. Interactions of DNA with human DNA primase monitored with photoactivatable cross-linking agents: implications for the role of the p58 subunit. Biochemistry 38 (1999) 12899-12907
    • (1999) Biochemistry , vol.38 , pp. 12899-12907
    • Arezi, B.1    Kirk, B.W.2    Copeland, W.C.3    Kuchta, R.D.4
  • 15
    • 1042265191 scopus 로고    scopus 로고
    • Mechanism of primer synthesis by the herpes simplex virus 1 helicase-primase
    • Ramirez-Aguilar K., and Kuchta R.D. Mechanism of primer synthesis by the herpes simplex virus 1 helicase-primase,. Biochemistry 43 (2004) 1103-1112
    • (2004) Biochemistry , vol.43 , pp. 1103-1112
    • Ramirez-Aguilar, K.1    Kuchta, R.D.2
  • 16
    • 0027513148 scopus 로고
    • The mechanism of calf thymus DNA primase: slow initiation, rapid polymerization and intelligent termination
    • Sheaff R., and Kuchta R.D. The mechanism of calf thymus DNA primase: slow initiation, rapid polymerization and intelligent termination. Biochemistry 32 (1993) 3027-3037
    • (1993) Biochemistry , vol.32 , pp. 3027-3037
    • Sheaff, R.1    Kuchta, R.D.2
  • 17
    • 0028820262 scopus 로고
    • Primer synthesis kinetics by Escherichia coli primase on single-stranded DNA templates
    • Swart J.R., and Griep M.A. Primer synthesis kinetics by Escherichia coli primase on single-stranded DNA templates. Biochemistry 34 (1995) 16097-16106
    • (1995) Biochemistry , vol.34 , pp. 16097-16106
    • Swart, J.R.1    Griep, M.A.2
  • 18
    • 66049164017 scopus 로고    scopus 로고
    • Structure and function of primase RepB′ encoded by broad-host-range plasmid RSF1010 that replicates exclusively in leading-strand mode
    • S. Geibel, S. Banchenko, M. Engel, Lanka, W. Saenger, Structure and function of primase RepB′ encoded by broad-host-range plasmid RSF1010 that replicates exclusively in leading-strand mode, Proc. Natl. Acad. Sci. USA 106 (2009) 7810-7815.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7810-7815
    • Geibel, S.1    Banchenko, S.2    Engel, M.3    Lanka4    Saenger, W.5
  • 19
    • 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. Herpes simplex virus helicase-primase: the UL8 protein is not required for DNA-dependent ATPase and DNA helicase activities. Nucleic Acids Res. 18 (1990) 3573-3578
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3573-3578
    • Calder, J.M.1    Stow, N.D.2
  • 20
    • 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. 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. 88 (1991) 1105-1109
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 1105-1109
    • Dodson, M.S.1    Lehman, I.R.2
  • 21
    • 0033520101 scopus 로고    scopus 로고
    • Human DNA primase: anion inhibition, manganese stimulation, and their effects on in vitro start site selection
    • Kirk B.W., and Kuchta R.D. Human DNA primase: anion inhibition, manganese stimulation, and their effects on in vitro start site selection. Biochemistry 38 (1999) 10126-10134
    • (1999) Biochemistry , vol.38 , pp. 10126-10134
    • Kirk, B.W.1    Kuchta, R.D.2
  • 22
    • 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. The UL8 subunit of the herpes simplex virus helicase-primase complex is required for efficient primer utilization. J. Virol. 66 (1992) 4884-48892
    • (1992) J. Virol. , vol.66 , pp. 4884-48892
    • Sherman, G.1    Gottlieb, J.2    Challberg, M.D.3
  • 23
    • 0037117724 scopus 로고    scopus 로고
    • The p58 subunit of human DNA primase is important for primer initiation
    • Zerbe L., and Kuchta R.D. The p58 subunit of human DNA primase is important for primer initiation. Elongat. Count., Biochem. 41 (2002) 4891-4900
    • (2002) Elongat. Count., Biochem. , vol.41 , pp. 4891-4900
    • Zerbe, L.1    Kuchta, R.D.2
  • 24
    • 0027379095 scopus 로고
    • Enzymatic characterization of the individual mammalian primase subunits reveals a biphasic mechanism for initiation of DNA replication
    • Copeland W.C., and Wang T.S.F. Enzymatic characterization of the individual mammalian primase subunits reveals a biphasic mechanism for initiation of DNA replication. J. Biol. Chem. 268 (1993) 26179-26189
    • (1993) J. Biol. Chem. , vol.268 , pp. 26179-26189
    • Copeland, W.C.1    Wang, T.S.F.2
  • 25
    • 34548492954 scopus 로고    scopus 로고
    • An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis
    • Klinge S., Hirst J., Maman J.D., Krude T., and Pellegrini L. An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis. Nat. Struct. Mol. Biol. 14 (2007) 875-877
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 875-877
    • Klinge, S.1    Hirst, J.2    Maman, J.D.3    Krude, T.4    Pellegrini, L.5
  • 26
    • 36348995555 scopus 로고    scopus 로고
    • An iron-sulfur cluster in the C-terminal domain of the p58 subunit of human DNA primase
    • Weiner B.E., Huang H., Dattilo B.M., Nilges M.J., Fanning E.C., and Chazin W.J. An iron-sulfur cluster in the C-terminal domain of the p58 subunit of human DNA primase. J. Biol. Chem. 282 (2007) 33444-33451
    • (2007) J. Biol. Chem. , vol.282 , pp. 33444-33451
    • Weiner, B.E.1    Huang, H.2    Dattilo, B.M.3    Nilges, M.J.4    Fanning, E.C.5    Chazin, W.J.6
  • 27
    • 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. 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 (1999) 7727-7737
    • (1999) Biochemistry , vol.38 , pp. 7727-7737
    • Kirk, B.W.1    Kuchta, R.D.2
  • 28
    • 0035169689 scopus 로고    scopus 로고
    • Crystal structure of a DNA-dependent RNA polymerase (DNA primase)
    • Augustin M.A., Huber R., and Kaiser J.T. Crystal structure of a DNA-dependent RNA polymerase (DNA primase). Nat. Struct. Mol. Biol. 8 (2001) 57-61
    • (2001) Nat. Struct. Mol. Biol. , vol.8 , pp. 57-61
    • Augustin, M.A.1    Huber, R.2    Kaiser, J.T.3
  • 29
    • 38849106170 scopus 로고    scopus 로고
    • Identification of a DNA primase template tracking site redefines the geometry of primer synthesis
    • Corn J.E., Pelton J.G., and Berger J.M. Identification of a DNA primase template tracking site redefines the geometry of primer synthesis. Nat. Struct. Mol. Biol. 15 (2006) 163-169
    • (2006) Nat. Struct. Mol. Biol. , vol.15 , pp. 163-169
    • Corn, J.E.1    Pelton, J.G.2    Berger, J.M.3
  • 30
    • 0346025633 scopus 로고    scopus 로고
    • Crystal structure of the Pyrococcus horikoshii DNA primase-UTP complex: implications for the mechanism of primer synthesis
    • Ito N., Nureki O., Shirouzu M., Yokoyama S., and Hanaoka F. Crystal structure of the Pyrococcus horikoshii DNA primase-UTP complex: implications for the mechanism of primer synthesis. Genes Cells 8 (2003) 913-923
    • (2003) Genes Cells , vol.8 , pp. 913-923
    • Ito, N.1    Nureki, O.2    Shirouzu, M.3    Yokoyama, S.4    Hanaoka, F.5
  • 31
    • 0038054465 scopus 로고    scopus 로고
    • Modular architecture of the bacteriophage T7 primase couples RNA primer synthesis to DNA synthesis
    • Kato M., Ito T., Wagner G., Richardson C.C., and Ellenberger T. Modular architecture of the bacteriophage T7 primase couples RNA primer synthesis to DNA synthesis. Mol. Cell 11 (2003) 1349-1360
    • (2003) Mol. Cell , vol.11 , pp. 1349-1360
    • Kato, M.1    Ito, T.2    Wagner, G.3    Richardson, C.C.4    Ellenberger, T.5
  • 32
    • 0034737468 scopus 로고    scopus 로고
    • Structure of the RNA polymerase domain of E. coli primase
    • Keck J.L., Roche D.D., Lynch A.S., and Berger J.M. Structure of the RNA polymerase domain of E. coli primase. Science 287 (2000) 2482-2486
    • (2000) Science , vol.287 , pp. 2482-2486
    • Keck, J.L.1    Roche, D.D.2    Lynch, A.S.3    Berger, J.M.4
  • 34
    • 0028106396 scopus 로고
    • Requirement for a zinc motif for template recognition by the bacteriophage T7 primase
    • Mendelman L.V., Beauchamp B.B., and Richardson C.C. Requirement for a zinc motif for template recognition by the bacteriophage T7 primase. EMBO J. 13 (1994) 3909-3916
    • (1994) EMBO J. , vol.13 , pp. 3909-3916
    • Mendelman, L.V.1    Beauchamp, B.B.2    Richardson, C.C.3
  • 35
    • 0033583318 scopus 로고    scopus 로고
    • 2+ finger motif of UL52 severely affects the biochemical activities of the HSV-1 helicase-primase subcomplex
    • 2+ finger motif of UL52 severely affects the biochemical activities of the HSV-1 helicase-primase subcomplex. J. Biol. Chem. 274 (1999) 8068-8076
    • (1999) J. Biol. Chem. , vol.274 , pp. 8068-8076
    • Biswas, N.1    Weller, S.K.2
  • 36
    • 0030018018 scopus 로고    scopus 로고
    • The role of zinc and the reactivity of cysteines in E. coli primase
    • Griep M.A., and Lokey E.R. The role of zinc and the reactivity of cysteines in E. coli primase. Biochemistry 35 (1996) 8260-8267
    • (1996) Biochemistry , vol.35 , pp. 8260-8267
    • Griep, M.A.1    Lokey, E.R.2
  • 37
    • 0033570097 scopus 로고    scopus 로고
    • The linker region between the helicase and primase domains of the bacteriophage T7 gene 4 protein is critical for hexamer formation
    • Guo S., Tabor S., and Richardson C.C. The linker region between the helicase and primase domains of the bacteriophage T7 gene 4 protein is critical for hexamer formation. J. Biol. Chem. 274 (1999) 30303-30309
    • (1999) J. Biol. Chem. , vol.274 , pp. 30303-30309
    • Guo, S.1    Tabor, S.2    Richardson, C.C.3
  • 38
    • 33646759589 scopus 로고    scopus 로고
    • Primer initiation and extension by T7 DNA primase
    • Qimron U., Lee S.-J., Hamdan S.M., and Richardson C.C. Primer initiation and extension by T7 DNA primase. EMBO J. 25 (2006) 2198-2208
    • (2006) EMBO J. , vol.25 , pp. 2198-2208
    • Qimron, U.1    Lee, S.-J.2    Hamdan, S.M.3    Richardson, C.C.4
  • 39
    • 0023645225 scopus 로고
    • Bacteriophage T4 DNA primase-helicase. Characterization of oligomer synthesis by T4 61 protein alone and in conjunction with T4 41 protein
    • Hinton D.M., and Nossal N.G. Bacteriophage T4 DNA primase-helicase. Characterization of oligomer synthesis by T4 61 protein alone and in conjunction with T4 41 protein. J. Biol. Chem. 262 (1987) 10873-10878
    • (1987) J. Biol. Chem. , vol.262 , pp. 10873-10878
    • Hinton, D.M.1    Nossal, N.G.2
  • 40
    • 21844446871 scopus 로고    scopus 로고
    • The oligomeric T4 primase is the functional form during replication
    • Yang J., Xi J., Zhuang Z., and Benkovic S.J. The oligomeric T4 primase is the functional form during replication,. J. Biol. Chem. 280 (2005) 25416-25423
    • (2005) J. Biol. Chem. , vol.280 , pp. 25416-25423
    • Yang, J.1    Xi, J.2    Zhuang, Z.3    Benkovic, S.J.4
  • 41
    • 0029741204 scopus 로고    scopus 로고
    • The ATP-activated hexameric helicase of bacteriophage T4 (gp41) forms a stable primosome with a single subunit of T4-coded primase (gp61)
    • Dong F., and von Hippel P.H. The ATP-activated hexameric helicase of bacteriophage T4 (gp41) forms a stable primosome with a single subunit of T4-coded primase (gp61). J. Biol. Chem. 271 (1996) 19625-19631
    • (1996) J. Biol. Chem. , vol.271 , pp. 19625-19631
    • Dong, F.1    von Hippel, P.H.2
  • 42
    • 0035909835 scopus 로고    scopus 로고
    • A zinc ribbon protein in DNA replication: primer synthesis and macromolecular interactions by the bacteriophage T4 primase
    • Valentine A.M., Ishmael F.T., Shier B.K., and Benkovic S.J. A zinc ribbon protein in DNA replication: primer synthesis and macromolecular interactions by the bacteriophage T4 primase. Biochemistry 40 (2001) 15074-15085
    • (2001) Biochemistry , vol.40 , pp. 15074-15085
    • Valentine, A.M.1    Ishmael, F.T.2    Shier, B.K.3    Benkovic, S.J.4
  • 43
    • 0347993077 scopus 로고    scopus 로고
    • Mechanisms and stoichiometry of interaction of DnaG primase with DnaB helicase of E. coli in RNA primer synthesis
    • Mitkova A.V., Khopde S.J., and Biswas S.B. Mechanisms and stoichiometry of interaction of DnaG primase with DnaB helicase of E. coli in RNA primer synthesis. J. Biol. Chem. 278 (2003) 52253-52261
    • (2003) J. Biol. Chem. , vol.278 , pp. 52253-52261
    • Mitkova, A.V.1    Khopde, S.J.2    Biswas, S.B.3
  • 44
    • 0034141871 scopus 로고    scopus 로고
    • DnaB Helicase stimulates primer synthesis activity on short oligonucleotide templates
    • Johnson S.K., Bhattacharyya S., and Griep M.A. DnaB Helicase stimulates primer synthesis activity on short oligonucleotide templates. Biochemistry 39 (2000) 736-744
    • (2000) Biochemistry , vol.39 , pp. 736-744
    • Johnson, S.K.1    Bhattacharyya, S.2    Griep, M.A.3
  • 45
    • 27644594271 scopus 로고    scopus 로고
    • Crosstalk between primase subunits can act to regulate primer synthesis in trans
    • Corn J.E., Pease P.J., Hura G.L., and Berger J.M. Crosstalk between primase subunits can act to regulate primer synthesis in trans. Mol. Cell 20 (2005) 391-401
    • (2005) Mol. Cell , vol.20 , pp. 391-401
    • Corn, J.E.1    Pease, P.J.2    Hura, G.L.3    Berger, J.M.4
  • 46
    • 0031008223 scopus 로고    scopus 로고
    • Herpes simplex virus DNA replication
    • Boehmer P.E., and Lehman I.R. Herpes simplex virus DNA replication. Annu. Rev.Biochem. 66 (1997) 347-384
    • (1997) Annu. Rev.Biochem. , vol.66 , pp. 347-384
    • Boehmer, P.E.1    Lehman, I.R.2
  • 47
    • 0025856010 scopus 로고
    • Herpes simplex virus-1 helicase primase. Physical and catalytic properties
    • Crute J.J., and Lehman I.R. Herpes simplex virus-1 helicase primase. Physical and catalytic properties. J. Biol. Chem. 266 (1991) 4484-4488
    • (1991) J. Biol. Chem. , vol.266 , pp. 4484-4488
    • Crute, J.J.1    Lehman, I.R.2
  • 48
    • 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. Identification of the primase active site of the herpes simplex virus type i helicase-primase. J. Biol. Chem. 270 (1995) 14148-14153
    • (1995) J. Biol. Chem. , vol.270 , pp. 14148-14153
    • Dracheva, S.1    Koonin, E.V.2    Crute, J.J.3
  • 49
    • 0031054522 scopus 로고    scopus 로고
    • Biochemical analyses of mutations in the HSV-1 helicase-primase that alter ATP hydrolysis, DNA unwinding, and coupling between hydrolysis and unwinding
    • Graves-Woodward K.L., Gottlieb J., Challberg M.D., and Weller S.K. Biochemical analyses of mutations in the HSV-1 helicase-primase that alter ATP hydrolysis, DNA unwinding, and coupling between hydrolysis and unwinding. J. Biol. Chem. 272 (1997) 4623-4630
    • (1997) J. Biol. Chem. , vol.272 , pp. 4623-4630
    • Graves-Woodward, K.L.1    Gottlieb, J.2    Challberg, M.D.3    Weller, S.K.4
  • 50
    • 0029666257 scopus 로고    scopus 로고
    • Replacement of Gly815 in helicase motif V alters the single-stranded DNA-dependent ATPase activity of the herpes simplex virus type i helicase-primase
    • Graves-Woodward K.L., and Weller S.K. Replacement of Gly815 in helicase motif V alters the single-stranded DNA-dependent ATPase activity of the herpes simplex virus type i helicase-primase. J. Biol. Chem. (1996) 13629-13635
    • (1996) J. Biol. Chem. , pp. 13629-13635
    • Graves-Woodward, K.L.1    Weller, S.K.2
  • 51
    • 0028278095 scopus 로고
    • Helicase primase complex of herpes simplex virus type1: a mutation in the UL52 subunit abolishes primase activity
    • Klinedinst D.K., and Challberg M.D. Helicase primase complex of herpes simplex virus type1: a mutation in the UL52 subunit abolishes primase activity. J. Virol. 68 (1994) 3693-3701
    • (1994) J. Virol. , vol.68 , pp. 3693-3701
    • Klinedinst, D.K.1    Challberg, M.D.2
  • 52
    • 0035907360 scopus 로고    scopus 로고
    • The UL5 and UL52 subunits of the herpes simplex virus type 1 helicase-primase subcomplex exhibit a complex interdependence for DNA binding
    • Biswas N., and Weller S.K. The UL5 and UL52 subunits of the herpes simplex virus type 1 helicase-primase subcomplex exhibit a complex interdependence for DNA binding. J. Biol. Chem. 276 (2001) 17610-17619
    • (2001) J. Biol. Chem. , vol.276 , pp. 17610-17619
    • Biswas, N.1    Weller, S.K.2
  • 53
    • 44249097571 scopus 로고    scopus 로고
    • Staphylococcus aureus primase has higher initiation specificity, interacts with single-stranded DNA stronger, but is less stimulated by its helicase than E. coli primase
    • Koepsell S.A., Larson M.A., Frey C.A., Hinrichs S.H., and Griep M.A. Staphylococcus aureus primase has higher initiation specificity, interacts with single-stranded DNA stronger, but is less stimulated by its helicase than E. coli primase. Mol. Microbiol. 68 (2008) 1570-1582
    • (2008) Mol. Microbiol. , vol.68 , pp. 1570-1582
    • Koepsell, S.A.1    Larson, M.A.2    Frey, C.A.3    Hinrichs, S.H.4    Griep, M.A.5
  • 54
    • 52649177242 scopus 로고    scopus 로고
    • Hyperthermophilic Aquifex aeolicus initiates primer synthesis on a limited set of trinuclotides comprised of cytosines and guanines
    • Larson M.A., Bressani R., Sayood K., Corn J.E., Berger J.M., Griep M.A., and Hinrichs S.H. Hyperthermophilic Aquifex aeolicus initiates primer synthesis on a limited set of trinuclotides comprised of cytosines and guanines,. Nucleic Acids Res. 36 (2008) 5260-5269
    • (2008) Nucleic Acids Res. , vol.36 , pp. 5260-5269
    • Larson, M.A.1    Bressani, R.2    Sayood, K.3    Corn, J.E.4    Berger, J.M.5    Griep, M.A.6    Hinrichs, S.H.7
  • 55
    • 32444436659 scopus 로고    scopus 로고
    • In the Bacillus stearothermophilus DnaB-DnaG complex, the activities of the two proteins are modulated by distinct but overlapping networks of residues
    • Thirlway J., and Soultanas P. In the Bacillus stearothermophilus DnaB-DnaG complex, the activities of the two proteins are modulated by distinct but overlapping networks of residues,. J. Bacteriol 188 (2006) 1534-1539
    • (2006) J. Bacteriol , vol.188 , pp. 1534-1539
    • Thirlway, J.1    Soultanas, P.2
  • 56
    • 0025214229 scopus 로고
    • Murine DNA polymerase alpha-primase initiates RNA-primed DNA synthesis preferentially upstream of a 3′-CC(C/A)-5′ motif
    • Davey S.K., and Faust E.A. Murine DNA polymerase alpha-primase initiates RNA-primed DNA synthesis preferentially upstream of a 3′-CC(C/A)-5′ motif. J. Biol. Chem. 265 (1990) 3611-3614
    • (1990) J. Biol. Chem. , vol.265 , pp. 3611-3614
    • Davey, S.K.1    Faust, E.A.2
  • 57
    • 0021989747 scopus 로고
    • The primase activity of DNA polymerase alpha from calf thymus
    • Grosse F., and Krauss G. The primase activity of DNA polymerase alpha from calf thymus. J. Biol. Chem. 260 (1988) 1881-1888
    • (1988) J. Biol. Chem. , vol.260 , pp. 1881-1888
    • Grosse, F.1    Krauss, G.2
  • 58
    • 0021340529 scopus 로고
    • Mouse primase initiation sites in the origin region of SV40
    • Tseng B.Y., and Ahlem C.N. Mouse primase initiation sites in the origin region of SV40. Proc. Natl. Acad. Sci. 81 (1984) 2342-2346
    • (1984) Proc. Natl. Acad. Sci. , vol.81 , pp. 2342-2346
    • Tseng, B.Y.1    Ahlem, C.N.2
  • 59
    • 0022362207 scopus 로고
    • DNA primase-DNA polymerase alpha from Simian cells: sequence specificity of initiation sites on Simian virus 40 DNA
    • Yamaguchi M., Hendrickson E.A., and DePamphilis M.L. DNA primase-DNA polymerase alpha from Simian cells: sequence specificity of initiation sites on Simian virus 40 DNA. Mol. Cell. Biol. 5 (1985) 1170-1183
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 1170-1183
    • Yamaguchi, M.1    Hendrickson, E.A.2    DePamphilis, M.L.3
  • 60
    • 0028129436 scopus 로고
    • Mapping initiation sites for SV40 DNA synthesis events in vitro
    • Bullock P.A., Tevosian S., Jones C., and Denis D. Mapping initiation sites for SV40 DNA synthesis events in vitro. Mol. Cell. Biol. 14 (1994) 5043-5055
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5043-5055
    • Bullock, P.A.1    Tevosian, S.2    Jones, C.3    Denis, D.4
  • 61
    • 0020118996 scopus 로고
    • Initiation of SV40 DNA replication in vivo: location and structure of 5′ ends of DNA synthesized in the ori region
    • Hay R.T., and DePamphilis M.L. Initiation of SV40 DNA replication in vivo: location and structure of 5′ ends of DNA synthesized in the ori region. Cell 28 (1982) 767-779
    • (1982) Cell , vol.28 , pp. 767-779
    • Hay, R.T.1    DePamphilis, M.L.2
  • 62
    • 0021717368 scopus 로고
    • Sequence specificity for the initiation of RNA-primed SV40 DNA synthesis in vivo
    • Hay R.T., Hendrickson E.A., and DePamphilis M.L. Sequence specificity for the initiation of RNA-primed SV40 DNA synthesis in vivo. J. Mol. Biol. 175 (1984) 131-157
    • (1984) J. Mol. Biol. , vol.175 , pp. 131-157
    • Hay, R.T.1    Hendrickson, E.A.2    DePamphilis, M.L.3
  • 63
    • 33751385190 scopus 로고
    • RNA priming coupled with DNA synthesis on natural template by calf thymus DNA polymerase alpha-primase
    • Suzuki M., Savoysky E., Izuta S., Tatebe M., Okajima T., and Yoshida S. RNA priming coupled with DNA synthesis on natural template by calf thymus DNA polymerase alpha-primase. Biochemistry 32 (1993) 12782-12792
    • (1993) Biochemistry , vol.32 , pp. 12782-12792
    • Suzuki, M.1    Savoysky, E.2    Izuta, S.3    Tatebe, M.4    Okajima, T.5    Yoshida, S.6
  • 64
    • 0022180425 scopus 로고
    • Initiation of DNA synthesis by the calf thymus DNA polymerase-primase complex
    • Holmes A.M., Cheriathundam E., Bollum F.J., and Chang L.M.S. Initiation of DNA synthesis by the calf thymus DNA polymerase-primase complex. J. Biol. Chem. 260 (1985) 10840-10846
    • (1985) J. Biol. Chem. , vol.260 , pp. 10840-10846
    • Holmes, A.M.1    Cheriathundam, E.2    Bollum, F.J.3    Chang, L.M.S.4
  • 65
    • 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. Key role of template sequence for primer synthesis by the herpes simplex virus 1 helicase-primase. Biochemistry 41 (2002) 4569-4579
    • (2002) Biochemistry , vol.41 , pp. 4569-4579
    • Ramirez-Aguilar, K.A.1    Low-Nam, N.A.2    Kuchta, R.D.3
  • 66
    • 0033544950 scopus 로고    scopus 로고
    • Interaction of bacteriophage T7 gene 4 primase with its template recognition site
    • Frick D.N., and Richardson C.C. Interaction of bacteriophage T7 gene 4 primase with its template recognition site. J. Biol. Chem. 274 (1999) 35889-35898
    • (1999) J. Biol. Chem. , vol.274 , pp. 35889-35898
    • Frick, D.N.1    Richardson, C.C.2
  • 67
    • 0031040805 scopus 로고    scopus 로고
    • Template recognition and ribonucleotide specificity of the DNA primase of bacteriophage T7
    • Kusakabe T., and Richardson C.C. Template recognition and ribonucleotide specificity of the DNA primase of bacteriophage T7. J. Biol. Chem. 272 (1997) 5943-5951
    • (1997) J. Biol. Chem. , vol.272 , pp. 5943-5951
    • Kusakabe, T.1    Richardson, C.C.2
  • 68
    • 0021112424 scopus 로고
    • A DNA primase from mouse cells. Purification and partial characterization
    • Tseng B.Y., and Ahlem C.N. A DNA primase from mouse cells. Purification and partial characterization. J. Biol. Chem. 258 (1983) 9845-9849
    • (1983) J. Biol. Chem. , vol.258 , pp. 9845-9849
    • Tseng, B.Y.1    Ahlem, C.N.2
  • 69
    • 0028331879 scopus 로고
    • Calf thymus DNA polymerase alpha-primase: "communication" and primer: template movement between the two active sites
    • Sheaff R., Kuchta R.D., and Ilsley D. Calf thymus DNA polymerase alpha-primase: "communication" and primer: template movement between the two active sites,. Biochemistry 33 (1994) 2247-2254
    • (1994) Biochemistry , vol.33 , pp. 2247-2254
    • Sheaff, R.1    Kuchta, R.D.2    Ilsley, D.3
  • 71
    • 0025051277 scopus 로고
    • DNA primase: processivity and the primase to polymerase alpha activity switch
    • Kuchta R.D., Reid B., and Chang L.M.S. DNA primase: processivity and the primase to polymerase alpha activity switch. J. Biol. Chem. 265 (1990) 16158-16165
    • (1990) J. Biol. Chem. , vol.265 , pp. 16158-16165
    • Kuchta, R.D.1    Reid, B.2    Chang, L.M.S.3
  • 72
    • 0022970582 scopus 로고
    • Primase and DNA polymerase activities: an analysis of RNA priming and its coupling to DNA synthesis
    • Singh H., Brooke R.G., Pausch M.H., Williams G.T., Trainor C., Dumas L.B., and Yeast D. Primase and DNA polymerase activities: an analysis of RNA priming and its coupling to DNA synthesis. J. Biol. Chem. 261 (1986) 8564-8569
    • (1986) J. Biol. Chem. , vol.261 , pp. 8564-8569
    • Singh, H.1    Brooke, R.G.2    Pausch, M.H.3    Williams, G.T.4    Trainor, C.5    Dumas, L.B.6    Yeast, D.7
  • 73
    • 0030783515 scopus 로고    scopus 로고
    • Increased activity and fidelity of DNA polymerase beta on single-nucleotide gapped DNA
    • Chagovetz A.M., Sweasy J.B., and Preston B.D. Increased activity and fidelity of DNA polymerase beta on single-nucleotide gapped DNA. J. Biol. Chem. 272 (1997) 27501-27504
    • (1997) J. Biol. Chem. , vol.272 , pp. 27501-27504
    • Chagovetz, A.M.1    Sweasy, J.B.2    Preston, B.D.3
  • 74
    • 0029817866 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase beta complexed with DNA: implications for catalytic mechanism
    • Pelletier H., Sawaya M.R., Wolfe W., Wilson S.H., and Kraut J. Crystal structures of human DNA polymerase beta complexed with DNA: implications for catalytic mechanism. Process. Fidel. Biochem. 35 (1996) 12742-12761
    • (1996) Process. Fidel. Biochem. , vol.35 , pp. 12742-12761
    • Pelletier, H.1    Sawaya, M.R.2    Wolfe, W.3    Wilson, S.H.4    Kraut, J.5
  • 75
    • 0027179827 scopus 로고
    • Short gap-filling synthesis by DNA polymerase beta is processive
    • Singhal R.K., and Wilson S.H. Short gap-filling synthesis by DNA polymerase beta is processive. J. Biol. Chem. 268 (1993) 15906-15911
    • (1993) J. Biol. Chem. , vol.268 , pp. 15906-15911
    • Singhal, R.K.1    Wilson, S.H.2
  • 77
    • 0035877578 scopus 로고    scopus 로고
    • A complex of the bacteriophage t7 primase-helicase and DNA polymerase directs primer utilization
    • Kato M., Frick D.N., Lee J., Tabor S., Richardson C.C., and Ellenberger T. A complex of the bacteriophage t7 primase-helicase and DNA polymerase directs primer utilization. J. Biol. Chem. 276 (2001) 21809-21820
    • (2001) J. Biol. Chem. , vol.276 , pp. 21809-21820
    • Kato, M.1    Frick, D.N.2    Lee, J.3    Tabor, S.4    Richardson, C.C.5    Ellenberger, T.6
  • 78
    • 50149098782 scopus 로고    scopus 로고
    • Interaction of herpes primase with the sugar of a NTP
    • Keller K.E., Cavanaugh N.A., and Kuchta R.D. Interaction of herpes primase with the sugar of a NTP. Biochemistry 47 (2008) 8977-8984
    • (2008) Biochemistry , vol.47 , pp. 8977-8984
    • Keller, K.E.1    Cavanaugh, N.A.2    Kuchta, R.D.3
  • 79
    • 3142732108 scopus 로고    scopus 로고
    • A molecular handoff between bacteriophage T7 DNA primase and T7 DNA polymerase initiates DNA synthesis
    • Kato M., Ito T., Wagner G., and Ellenberger T. A molecular handoff between bacteriophage T7 DNA primase and T7 DNA polymerase initiates DNA synthesis. J. Biol. Chem. 279 (2004) 30554-30562
    • (2004) J. Biol. Chem. , vol.279 , pp. 30554-30562
    • Kato, M.1    Ito, T.2    Wagner, G.3    Ellenberger, T.4
  • 81
    • 0033534380 scopus 로고    scopus 로고
    • Trading places on DNA - a three-point switch underlies primer handoff from primase to the replicative DNA polymerase
    • Yuzhakov A., Kelman Z., and O'Donnell M. Trading places on DNA - a three-point switch underlies primer handoff from primase to the replicative DNA polymerase. Cell 96 (1999) 153-163
    • (1999) Cell , vol.96 , pp. 153-163
    • Yuzhakov, A.1    Kelman, Z.2    O'Donnell, M.3
  • 82
    • 10144219958 scopus 로고    scopus 로고
    • The herpes simplex virus type 1 UL8 protein influences the intracellular localization of the UL52 but not the ICP8 or POL replication proteins in virus-infected cells
    • Marsden H.S., Cross A.M., Francis G.J., Patel A.J., MacEachran K., Murphy M., McVey G., Haydon D., Abbotts A., and Stow N.D. The herpes simplex virus type 1 UL8 protein influences the intracellular localization of the UL52 but not the ICP8 or POL replication proteins in virus-infected cells. J. Gen. Virol. 77 (1996) 2241-2249
    • (1996) J. Gen. Virol. , vol.77 , pp. 2241-2249
    • Marsden, H.S.1    Cross, A.M.2    Francis, G.J.3    Patel, A.J.4    MacEachran, K.5    Murphy, M.6    McVey, G.7    Haydon, D.8    Abbotts, A.9    Stow, N.D.10
  • 83
    • 59449102872 scopus 로고    scopus 로고
    • Initiation of new DNA strands by the herpes primase-helicase complex and either herpes DNA polymerase or human DNA polymerase alpha
    • Cavanaugh N.A., and Kuchta R.D. Initiation of new DNA strands by the herpes primase-helicase complex and either herpes DNA polymerase or human DNA polymerase alpha. J. Biol. Chem. 284 (2009) 1523-1532
    • (2009) J. Biol. Chem. , vol.284 , pp. 1523-1532
    • Cavanaugh, N.A.1    Kuchta, R.D.2
  • 84
    • 0023665284 scopus 로고
    • DNA polymerase-primase from embryos of Drosophila melanogaster
    • Cotterill S., Chui G., and Lehman I.R. DNA polymerase-primase from embryos of Drosophila melanogaster. J. Biol. Chem. 262 (1987) 16105-16108
    • (1987) J. Biol. Chem. , vol.262 , pp. 16105-16108
    • Cotterill, S.1    Chui, G.2    Lehman, I.R.3
  • 85
    • 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. 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 (1994) 19225-19231
    • (1994) J. Biol. Chem. , vol.269 , pp. 19225-19231
    • Sheaff, R.1    Kuchta, R.D.2
  • 86
    • 0037180395 scopus 로고    scopus 로고
    • Synthesis of nucleotide analogs that potently and selectively inhibit human DNA primase
    • Moore C.L., Chiaramonte M., Higgins T., and Kuchta R.D. Synthesis of nucleotide analogs that potently and selectively inhibit human DNA primase. Biochemistry 41 (2002) 14066-14075
    • (2002) Biochemistry , vol.41 , pp. 14066-14075
    • Moore, C.L.1    Chiaramonte, M.2    Higgins, T.3    Kuchta, R.D.4
  • 87
    • 4644289452 scopus 로고    scopus 로고
    • Human DNA primase uses Watson-Crick hydrogen bonding groups to distinguish between correct and incorrect NTPs
    • Moore C.L., Zivkovic A., Engels J., and Kuchta R.D. Human DNA primase uses Watson-Crick hydrogen bonding groups to distinguish between correct and incorrect NTPs. Biochemistry 43 (2004) 12367-12374
    • (2004) Biochemistry , vol.43 , pp. 12367-12374
    • Moore, C.L.1    Zivkovic, A.2    Engels, J.3    Kuchta, R.D.4
  • 88
    • 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. herpes simplex virus I primase employs Watson-Crick hydrogen bonding to identify cognate NTPs. Biochemistry 44 (2005) 15585-15593
    • (2005) Biochemistry , vol.44 , pp. 15585-15593
    • Ramirez-Aguilar, K.A.1    Moore, C.L.2    Kuchta, R.D.3
  • 89
    • 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. Inhibition of DNA primase and polymerase alpha by arabinofuranosylnucleoside triphosphates and related compounds. Biochemistry 31 (1992) 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
  • 90
    • 0023100542 scopus 로고
    • Inhibition of DNA primase by nucleoside triphosphates and their arabinofuranosyl analogs
    • Parker W.B., and Cheng Y.C. Inhibition of DNA primase by nucleoside triphosphates and their arabinofuranosyl analogs,. Mol. Pharmacol. 31 (1987) 146-151
    • (1987) Mol. Pharmacol. , vol.31 , pp. 146-151
    • Parker, W.B.1    Cheng, Y.C.2
  • 93
    • 33947286682 scopus 로고    scopus 로고
    • Superior efficacy of helicase-primase inhibitor BAY57-1293 for herpes infection and latency in the guinea pig model of human genital herpes disease
    • Baumeister J., Fischer R., Eckenberg P., Henninger K., Rubsamen-Waigmann H., and Kleymann G. Superior efficacy of helicase-primase inhibitor BAY57-1293 for herpes infection and latency in the guinea pig model of human genital herpes disease. Antivir. Chem. Chemother. 18 (2007) 35-48
    • (2007) Antivir. Chem. Chemother. , vol.18 , pp. 35-48
    • Baumeister, J.1    Fischer, R.2    Eckenberg, P.3    Henninger, K.4    Rubsamen-Waigmann, H.5    Kleymann, G.6
  • 94
    • 34147112254 scopus 로고    scopus 로고
    • Concise synthesis of the bacterial DNA primase inhibitor (+)-Sch642305
    • Wilson E.M., and Trauner D. Concise synthesis of the bacterial DNA primase inhibitor (+)-Sch642305. Org. Lett. 9 (2007) 1327-1329
    • (2007) Org. Lett. , vol.9 , pp. 1327-1329
    • Wilson, E.M.1    Trauner, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.