메뉴 건너뛰기




Volumn 397, Issue 3, 2010, Pages 664-676

Characterization of a Functional DnaG-Type Primase in Archaea: Implications for a Dual-Primase System

Author keywords

archaea; DNA replication; DnaG; kinetics; primase

Indexed keywords

DNA; DNA PRIMASE; GLUTAMIC ACID;

EID: 77649339525     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.01.057     Document Type: Article
Times cited : (16)

References (52)
  • 2
    • 77949570959 scopus 로고    scopus 로고
    • Mechanism and evolution of DNA primases
    • 10.1016/j.bbapap.2009.06.0110 In press
    • Kuchta R.D., and Stengel G. Mechanism and evolution of DNA primases. Biochim. Biophys. Acta (2009) 10.1016/j.bbapap.2009.06.0110 In press
    • (2009) Biochim. Biophys. Acta
    • Kuchta, R.D.1    Stengel, G.2
  • 3
    • 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
  • 4
    • 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-Sirieix 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-Sirieix, S.H.1    Bell, S.D.2
  • 5
    • 36248984797 scopus 로고    scopus 로고
    • The heterodimeric primase from the euryarchaeon Pyrococcus abyssi: a multifunctional enzyme for initiation and repair?
    • Le Breton 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
    • Le Breton, M.1    Henneke, G.2    Norais, C.3    Flament, D.4    Myllykallio, H.5    Querellou, J.6    Raffin, J.P.7
  • 6
    • 33846953916 scopus 로고    scopus 로고
    • Molecular basis for the subunit assembly of the primase from an archaeon Pyrococcus horikoshii
    • Ito N., Matsui I., and Matsui E. Molecular basis for the subunit assembly of the primase from an archaeon Pyrococcus horikoshii. FEBS J. 274 (2007) 1340-1351
    • (2007) FEBS J. , vol.274 , pp. 1340-1351
    • Ito, N.1    Matsui, I.2    Matsui, E.3
  • 7
    • 0345733993 scopus 로고    scopus 로고
    • Distinct domain functions regulating de novo DNA synthesis of thermostable DNA primase from hyperthermophile Pyrococcus horikoshii
    • Matsui E., Nishio M., Yokoyama H., Harata K., Darnis S., and Matsui I. Distinct domain functions regulating de novo DNA synthesis of thermostable DNA primase from hyperthermophile Pyrococcus horikoshii. Biochemistry 42 (2003) 14968-14976
    • (2003) Biochemistry , vol.42 , pp. 14968-14976
    • Matsui, E.1    Nishio, M.2    Yokoyama, H.3    Harata, K.4    Darnis, S.5    Matsui, I.6
  • 9
    • 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 V.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, V.K.3    Benkovic, S.J.4
  • 10
    • 0026660979 scopus 로고
    • Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork: III. A polymerase-primase interaction governs primer size
    • Zechner E.L., Wu C.A., and Marians K.J. Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork: III. A polymerase-primase interaction governs primer size. J. Biol. Chem. 267 (1992) 4054-4063
    • (1992) J. Biol. Chem. , vol.267 , pp. 4054-4063
    • Zechner, E.L.1    Wu, C.A.2    Marians, K.J.3
  • 11
    • 0026698012 scopus 로고
    • Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork: II. Frequency of primer synthesis and efficiency of primer utilization control Okazaki fragment size
    • Zechner E.L., Wu C.A., and Marians K.J. Coordinated leading- and lagging-strand synthesis at the Escherichia coli DNA replication fork: II. Frequency of primer synthesis and efficiency of primer utilization control Okazaki fragment size. J. Biol. Chem. 267 (1992) 4045-4053
    • (1992) J. Biol. Chem. , vol.267 , pp. 4045-4053
    • Zechner, E.L.1    Wu, C.A.2    Marians, K.J.3
  • 12
    • 0025051277 scopus 로고
    • DNA primase. Processivity and the primase to polymerase alpha activity switch
    • Kuchta R.D., Reid B., and Chang L.M. 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.3
  • 13
    • 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 (2008) 163-169
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 163-169
    • Corn, J.E.1    Pelton, J.G.2    Berger, J.M.3
  • 15
    • 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
  • 16
    • 0034616957 scopus 로고    scopus 로고
    • A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases
    • Podobnik M., McInerney P., O'Donnell M., and Kuriyan J. A TOPRIM domain in the crystal structure of the catalytic core of Escherichia coli primase confirms a structural link to DNA topoisomerases. J. Mol. Biol. 300 (2000) 353-362
    • (2000) J. Mol. Biol. , vol.300 , pp. 353-362
    • Podobnik, M.1    McInerney, P.2    O'Donnell, M.3    Kuriyan, J.4
  • 17
    • 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
  • 18
    • 0032473420 scopus 로고    scopus 로고
    • Roles of the helicase and primase domain of the gene 4 protein of bacteriophage T7 in accessing the primase recognition site
    • Kusakabe T., Baradaran K., Lee J., and Richardson C.C. Roles of the helicase and primase domain of the gene 4 protein of bacteriophage T7 in accessing the primase recognition site. EMBO J. 17 (1998) 1542-1552
    • (1998) EMBO J. , vol.17 , pp. 1542-1552
    • Kusakabe, T.1    Baradaran, K.2    Lee, J.3    Richardson, C.C.4
  • 19
    • 0029776368 scopus 로고    scopus 로고
    • The role of the zinc motif in sequence recognition by DNA primases
    • Kusakabe T., and Richardson C.C. The role of the zinc motif in sequence recognition by DNA primases. J. Biol. Chem. 271 (1996) 19563-19570
    • (1996) J. Biol. Chem. , vol.271 , pp. 19563-19570
    • Kusakabe, T.1    Richardson, C.C.2
  • 20
    • 0029832926 scopus 로고    scopus 로고
    • The extreme C terminus of primase is required for interaction with DnaB at the replication fork
    • Tougu K., and Marians K.J. The extreme C terminus of primase is required for interaction with DnaB at the replication fork. J. Biol. Chem. 271 (1996) 21391-21397
    • (1996) J. Biol. Chem. , vol.271 , pp. 21391-21397
    • Tougu, K.1    Marians, K.J.2
  • 21
    • 0028998313 scopus 로고
    • Identification of the primase active site of the herpes simplex virus type 1 helicase-primase
    • Dracheva S., Koonin E.V., and Crute J.J. Identification of the primase active site of the herpes simplex virus type 1 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
  • 22
    • 0028049949 scopus 로고
    • Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork
    • Tougu K., Peng H., and Marians K.J. Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork. J. Biol. Chem. 269 (1994) 4675-4682
    • (1994) J. Biol. Chem. , vol.269 , pp. 4675-4682
    • Tougu, K.1    Peng, H.2    Marians, K.J.3
  • 23
    • 33750440205 scopus 로고    scopus 로고
    • Characterization of native and reconstituted exosome complexes from the hyperthermophilic archaeon Sulfolobus solfataricus
    • Walter P., Klein F., Lorentzen E., Ilchmann A., Klug G., and Evguenieva-Hackenberg E. Characterization of native and reconstituted exosome complexes from the hyperthermophilic archaeon Sulfolobus solfataricus. Mol. Microbiol. 62 (2006) 1076-1089
    • (2006) Mol. Microbiol. , vol.62 , pp. 1076-1089
    • Walter, P.1    Klein, F.2    Lorentzen, E.3    Ilchmann, A.4    Klug, G.5    Evguenieva-Hackenberg, E.6
  • 25
    • 0030953880 scopus 로고    scopus 로고
    • Gene duplications in evolution of archaeal family B DNA polymerases
    • Edgell D.R., Klenk H.P., and Doolittle W.F. Gene duplications in evolution of archaeal family B DNA polymerases. J. Bacteriol. 179 (1997) 2632-2640
    • (1997) J. Bacteriol. , vol.179 , pp. 2632-2640
    • Edgell, D.R.1    Klenk, H.P.2    Doolittle, W.F.3
  • 26
    • 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
  • 27
    • 26944435616 scopus 로고    scopus 로고
    • Organization of the archaeal MCM complex on DNA and implications for the helicase mechanism
    • McGeoch A.T., Trakselis M.A., Laskey R.A., and Bell S.D. Organization of the archaeal MCM complex on DNA and implications for the helicase mechanism. Nat. Struct. Mol. Biol. 12 (2005) 756-762
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 756-762
    • McGeoch, A.T.1    Trakselis, M.A.2    Laskey, R.A.3    Bell, S.D.4
  • 28
    • 0032555592 scopus 로고    scopus 로고
    • Primase activity of human DNA polymerase alpha-primase. Divalent cations stabilize the enzyme activity of the p48 subunit
    • Schneider A., Smith R.W., Kautz A.R., Weisshart K., Grosse F., and Nasheuer H.P. Primase activity of human DNA polymerase alpha-primase. Divalent cations stabilize the enzyme activity of the p48 subunit. J. Biol. Chem. 273 (1998) 21608-21615
    • (1998) J. Biol. Chem. , vol.273 , pp. 21608-21615
    • Schneider, A.1    Smith, R.W.2    Kautz, A.R.3    Weisshart, K.4    Grosse, F.5    Nasheuer, H.P.6
  • 29
    • 0017849604 scopus 로고
    • A ribo-deoxyribonucleotide primer synthesized by primase
    • Rowen L., and Kornberg A. A ribo-deoxyribonucleotide primer synthesized by primase. J. Biol. Chem. 253 (1978) 770-774
    • (1978) J. Biol. Chem. , vol.253 , pp. 770-774
    • Rowen, L.1    Kornberg, A.2
  • 30
    • 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
  • 31
    • 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
  • 32
    • 0037126718 scopus 로고    scopus 로고
    • Affinity and sequence specificity of DNA binding and site selection for primer synthesis by Escherichia coli primase
    • Khopde S., Biswas E.E., and Biswas S.B. Affinity and sequence specificity of DNA binding and site selection for primer synthesis by Escherichia coli primase. Biochemistry 41 (2002) 14820-14830
    • (2002) Biochemistry , vol.41 , pp. 14820-14830
    • Khopde, S.1    Biswas, E.E.2    Biswas, S.B.3
  • 33
    • 0026708136 scopus 로고
    • A common sequence motif, -E-G-Y-A-T-A-, identified within the primase domains of plasmid-encoded I- and P-type DNA primases and the alpha protein of the Escherichia coli satellite phage P4
    • Strack B., Lessl M., Calendar R., and Lanka E. A common sequence motif, -E-G-Y-A-T-A-, identified within the primase domains of plasmid-encoded I- and P-type DNA primases and the alpha protein of the Escherichia coli satellite phage P4. J. Biol. Chem. 267 (1992) 13062-13072
    • (1992) J. Biol. Chem. , vol.267 , pp. 13062-13072
    • Strack, B.1    Lessl, M.2    Calendar, R.3    Lanka, E.4
  • 35
    • 0021859620 scopus 로고
    • Evidence that discontinuous DNA replication in Escherichia coli is primed by approximately 10 to 12 residues of RNA starting with a purine
    • Kitani T., Yoda K., Ogawa T., and Okazaki T. Evidence that discontinuous DNA replication in Escherichia coli is primed by approximately 10 to 12 residues of RNA starting with a purine. J. Mol. Biol. 184 (1985) 45-52
    • (1985) J. Mol. Biol. , vol.184 , pp. 45-52
    • Kitani, T.1    Yoda, K.2    Ogawa, T.3    Okazaki, T.4
  • 36
    • 0034142263 scopus 로고    scopus 로고
    • DnaB helicase affects the initiation specificity of Escherichia coli primase on single-stranded DNA templates
    • Bhattacharyya S., and Griep M.A. DnaB helicase affects the initiation specificity of Escherichia coli primase on single-stranded DNA templates. Biochemistry 39 (2000) 745-752
    • (2000) Biochemistry , vol.39 , pp. 745-752
    • Bhattacharyya, S.1    Griep, M.A.2
  • 37
    • 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
  • 38
    • 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
  • 39
    • 0037007636 scopus 로고    scopus 로고
    • A new phylum of Archaea represented by a nanosized hyperthermophilic symbiont
    • Huber H., Hohn M.J., Rachel R., Fuchs T., Wimmer V.C., and Stetter K.O. A new phylum of Archaea represented by a nanosized hyperthermophilic symbiont. Nature 417 (2002) 63-67
    • (2002) Nature , vol.417 , pp. 63-67
    • Huber, H.1    Hohn, M.J.2    Rachel, R.3    Fuchs, T.4    Wimmer, V.C.5    Stetter, K.O.6
  • 42
    • 74949137952 scopus 로고    scopus 로고
    • A single-base resolution map of an archaeal transcriptome
    • 10.1101/gr.100396.109 In Press
    • Wurtzel O., Sapra R., Chen F., Zhu Y., Simmons B.A., and Sorek R. A single-base resolution map of an archaeal transcriptome. Genome Res (2009) 10.1101/gr.100396.109 In Press
    • (2009) Genome Res
    • Wurtzel, O.1    Sapra, R.2    Chen, F.3    Zhu, Y.4    Simmons, B.A.5    Sorek, R.6
  • 43
    • 49849095152 scopus 로고    scopus 로고
    • Identification and characterization of Sulfolobus solfataricus P2 proteome using multidimensional liquid phase protein separations
    • Assiddiq B.F., Snijders A.P., Chong P.K., Wright P.C., and Dickman M.J. Identification and characterization of Sulfolobus solfataricus P2 proteome using multidimensional liquid phase protein separations. J. Proteome Res. 7 (2008) 2253-2261
    • (2008) J. Proteome Res. , vol.7 , pp. 2253-2261
    • Assiddiq, B.F.1    Snijders, A.P.2    Chong, P.K.3    Wright, P.C.4    Dickman, M.J.5
  • 44
    • 34447319079 scopus 로고    scopus 로고
    • Essential and non-essential DNA replication genes in the model halophilic archaeon, Halobacterium sp. NRC-1
    • Berquist B.R., DasSarma P., and DasSarma S. Essential and non-essential DNA replication genes in the model halophilic archaeon, Halobacterium sp. NRC-1. BMC Genet. 8 (2007) 31
    • (2007) BMC Genet. , vol.8 , pp. 31
    • Berquist, B.R.1    DasSarma, P.2    DasSarma, S.3
  • 45
    • 33846207401 scopus 로고    scopus 로고
    • Interplay between primase and replication factor C in the hyperthermophilic archaeon Sulfolobus solfataricus
    • Wu K., Lai X., Guo X., Hu J., Xiang X., and Huang L. Interplay between primase and replication factor C in the hyperthermophilic archaeon Sulfolobus solfataricus. Mol. Microbiol. 63 (2007) 826-837
    • (2007) Mol. Microbiol. , vol.63 , pp. 826-837
    • Wu, K.1    Lai, X.2    Guo, X.3    Hu, J.4    Xiang, X.5    Huang, L.6
  • 46
    • 8444222286 scopus 로고    scopus 로고
    • Thermally denaturing high-performance liquid chromatography analysis of primase activity
    • Koepsell S., Bastola D., Hinrichs S.H., and Griep M.A. Thermally denaturing high-performance liquid chromatography analysis of primase activity. Anal. Biochem. 332 (2004) 330-336
    • (2004) Anal. Biochem. , vol.332 , pp. 330-336
    • Koepsell, S.1    Bastola, D.2    Hinrichs, S.H.3    Griep, M.A.4
  • 47
    • 34848826636 scopus 로고    scopus 로고
    • Properties of an unusual DNA primase from an archaeal plasmid
    • Beck K., and Lipps G. Properties of an unusual DNA primase from an archaeal plasmid. Nucleic Acids Res. 35 (2007) 5635-5645
    • (2007) Nucleic Acids Res. , vol.35 , pp. 5635-5645
    • Beck, K.1    Lipps, G.2
  • 48
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut T.W. Physiological concentrations of purines and pyrimidines. Mol. Cell. Biochem. 140 (1994) 1-22
    • (1994) Mol. Cell. Biochem. , vol.140 , pp. 1-22
    • Traut, T.W.1
  • 49
    • 22444435033 scopus 로고    scopus 로고
    • Origin and evolution of the archaeo-eukaryotic primase superfamily and related palm-domain proteins: structural insights and new members
    • Iyer L.M., 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) 3875-3896
    • (2005) Nucleic Acids Res. , vol.33 , pp. 3875-3896
    • Iyer, L.M.1    Koonin, E.V.2    Leipe, D.D.3    Aravind, L.4
  • 50
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino acid sequence data
    • Gill S.C., and von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 182 (1989) 319-326
    • (1989) Anal. Biochem. , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 51
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A., Tomas H., Havlis J., Olsen J.V., and Mann M. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1 (2006) 2856-2860
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.