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Volumn 41, Issue 10, 2013, Pages 5303-5320

Functional interplay of DnaE polymerase, DnaG primase and DnaC helicase within a ternary complex, and primase to polymerase hand-off during lagging strand DNA replication in Bacillus subtilis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DNAC HELICASE; DNAE POLYMERASE; DNAG PRIMASE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 84878622944     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkt207     Document Type: Article
Times cited : (28)

References (58)
  • 1
    • 0036229246 scopus 로고    scopus 로고
    • Structural basis for proofreading during replication of the Escherichia coli chromosome
    • Hamdan, S., Carr, P.D., Brown, S.E., Ollis, D. and Dixon, N.E. (2002) Structural basis for proofreading during replication of the Escherichia coli chromosome. Structure, 10, 535-546.
    • (2002) Structure , vol.10 , pp. 535-546
    • Hamdan, S.1    Carr, P.D.2    Brown, S.E.3    Ollis, D.4    Dixon, N.E.5
  • 2
    • 26444476481 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the Escherichia coli DNA polymerase III theta subunit
    • Mueller, G.A., Kirby, T.W., DeRose, E.F., Li, D., Schaaper, R.M. and London, R.E. (2005) Nuclear magnetic resonance solution structure of the Escherichia coli DNA polymerase III theta subunit. J. Bacteriol., 187, 7081-7089.
    • (2005) J. Bacteriol. , vol.187 , pp. 7081-7089
    • Mueller, G.A.1    Kirby, T.W.2    DeRose, E.F.3    Li, D.4    Schaaper, R.M.5    London, R.E.6
  • 3
    • 80053560927 scopus 로고    scopus 로고
    • Bacterial replicases and related polymerases
    • McHenry, C.S. (2011) Bacterial replicases and related polymerases. Curr. Opin. Chem. Biol., 15, 587-594.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 587-594
    • McHenry, C.S.1
  • 4
    • 34547730912 scopus 로고    scopus 로고
    • Characterization of a triple DNA polymerase replisome
    • McInerney, P., Johnson, A., Katz, F. and O'Donnell, M. (2007) Characterization of a triple DNA polymerase replisome. Cell, 27, 527-538.
    • (2007) Cell , vol.27 , pp. 527-538
    • McInerney, P.1    Johnson, A.2    Katz, F.3    O'Donnell, M.4
  • 6
    • 33646787455 scopus 로고    scopus 로고
    • The replicative polymerases PolC and DnaE are required for theta replication of the Bacillus subtilis plasmid pBS72
    • Titok, M., Suski, C., Dalmais, B., Ehrlich, S.D. and Jannière, L. (2006) The replicative polymerases PolC and DnaE are required for theta replication of the Bacillus subtilis plasmid pBS72. Microbiology, 152, 1471-1478.
    • (2006) Microbiology , vol.152 , pp. 1471-1478
    • Titok, M.1    Suski, C.2    Dalmais, B.3    Ehrlich, S.D.4    Jannière, L.5
  • 7
    • 74749100156 scopus 로고    scopus 로고
    • Reconstitution of the B subtilis replisome with 13 proteins including two distinct replicases
    • Sanders, G.M., Dallmann, G. and McHenry, C.S. (2010) Reconstitution of the B. subtilis replisome with 13 proteins including two distinct replicases. Mol. Cell, 37, 273-281.
    • (2010) Mol. Cell , vol.37 , pp. 273-281
    • Sanders, G.M.1    Dallmann, G.2    McHenry, C.S.3
  • 8
    • 54249092768 scopus 로고    scopus 로고
    • Dividing the workload at a eukaryotic replication fork
    • Kunkel, T.A. and Burgers, P.M. (2008) Dividing the workload at a eukaryotic replication fork. Trends Cell Biol., 18, 521-527.
    • (2008) Trends Cell Biol. , vol.18 , pp. 521-527
    • Kunkel, T.A.1    Burgers, P.M.2
  • 9
    • 84876319685 scopus 로고    scopus 로고
    • The pola-primase complex
    • Pellegrini, L. (2012) The pola-primase complex. Subcell. Biochem., 62, 157-169.
    • (2012) Subcell. Biochem. , vol.62 , pp. 157-169
    • Pellegrini, L.1
  • 11
    • 34248551243 scopus 로고    scopus 로고
    • Solution structure of domains IVa and V of the t subunit of Escherichia coli DNA polymerase III and interaction with the a subunit
    • Su, X.C., Jergic, S., Keniry, M.A., Dixon, N.E. and Otting, G. (2007) Solution structure of domains IVa and V of the t subunit of Escherichia coli DNA polymerase III and interaction with the a subunit. Nucleic Acids Res., 9, 2825-2832.
    • (2007) Nucleic Acids Res. , vol.9 , pp. 2825-2832
    • Su, X.C.1    Jergic, S.2    Keniry, M.A.3    Dixon, N.E.4    Otting, G.5
  • 12
    • 0025303309 scopus 로고
    • The g subunit of DNA polymerase III holoenzyme of Escherichia coli is produced by ribosomal frameshifting
    • Flower, A.M. and McHenry, C.S. (1990) The g subunit of DNA polymerase III holoenzyme of Escherichia coli is produced by ribosomal frameshifting. Proc. Natl Acad. Sci. USA, 87, 3713-3717.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 3713-3717
    • Flower, A.M.1    McHenry, C.S.2
  • 13
    • 0030763633 scopus 로고    scopus 로고
    • Thermus thermophilus dnaX homolog encoding g- and t-like proteins of the chromosomal replicase
    • Yurieva, O., Skangalis, M., Kuriyan, J. and O'Donnell, M. (1997) Thermus thermophilus dnaX homolog encoding g- and t-like proteins of the chromosomal replicase. J. Biol. Chem., 272, 27131-27139.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27131-27139
    • Yurieva, O.1    Skangalis, M.2    Kuriyan, J.3    O'Donnell, M.4
  • 14
    • 0034666303 scopus 로고    scopus 로고
    • The DNA replication machine of a Gram-positive organism
    • Bruck, I. and O'Donnell, M. (2000) The DNA replication machine of a Gram-positive organism. J. Biol. Chem., 275, 28971-28983.
    • (2000) J. Biol. Chem. , vol.275 , pp. 28971-28983
    • Bruck, I.1    O'Donnell, M.2
  • 15
    • 77951537332 scopus 로고    scopus 로고
    • Stoichiometry and architecture of active DNA replication machinery in Escherichia coli
    • Reyes-Lamothe, R., Sherratt, D.J. and Leake, M.C. (2010) Stoichiometry and architecture of active DNA replication machinery in Escherichia coli. Science, 328, 498-501.
    • (2010) Science , vol.328 , pp. 498-501
    • Reyes-Lamothe, R.1    Sherratt, D.J.2    Leake, M.C.3
  • 17
    • 0242666381 scopus 로고    scopus 로고
    • The essential C family DnaE polymerase is error-prone and efficient at lesion bypass
    • Bruck, I., Goodman, M.F. and O'Donnell, M. (2003) The essential C family DnaE polymerase is error-prone and efficient at lesion bypass. J. Biol. Chem., 278, 44361-44368.
    • (2003) J. Biol. Chem. , vol.278 , pp. 44361-44368
    • Bruck, I.1    Goodman, M.F.2    O'Donnell, M.3
  • 18
    • 78650691470 scopus 로고    scopus 로고
    • The C-terminal domain of the bacterial SSB protein acts as a DNA maintenance hub at active chromosome replication forks
    • Costes, A., Lecointe, F., McGovern, S., Quevillon-Cheruel, S. and Polard, P. (2010) The C-terminal domain of the bacterial SSB protein acts as a DNA maintenance hub at active chromosome replication forks. PLoS Genet., 6, e1001238.
    • (2010) PLoS Genet. , vol.6
    • Costes, A.1    Lecointe, F.2    McGovern, S.3    Quevillon-Cheruel, S.4    Polard, P.5
  • 19
    • 38949113141 scopus 로고    scopus 로고
    • Beta clamp directs localization of mismatch repair in Bacillus subtilis
    • Simmons, L.A., Davies, B.W., Grossman, A.D. and Walker, G.C. (2008) Beta clamp directs localization of mismatch repair in Bacillus subtilis. Mol. Cell, 29, 291-301.
    • (2008) Mol. Cell , vol.29 , pp. 291-301
    • Simmons, L.A.1    Davies, B.W.2    Grossman, A.D.3    Walker, G.C.4
  • 20
    • 35348979683 scopus 로고    scopus 로고
    • Helicase and its complex with a domain of DnaG primase
    • Bailey, S., Eliason, W.K. and Steitz, T.A. (2007) Helicase and its complex with a domain of DnaG primase. Science, 318, 459-463.
    • (2007) Science , vol.318 , pp. 459-463
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 21
    • 41049104425 scopus 로고    scopus 로고
    • Conserved residues of the C-terminal p16 domain of primase are involved in modulating the activity of the bacterial primosome
    • Chintakayala, K., Larson, M.A., Griep, M.A., Hinrichs, S.H. and Soultanas, P. (2008) Conserved residues of the C-terminal p16 domain of primase are involved in modulating the activity of the bacterial primosome. Mol. Microbiol., 68, 360-371.
    • (2008) Mol. Microbiol. , vol.68 , pp. 360-371
    • Chintakayala, K.1    Larson, M.A.2    Griep, M.A.3    Hinrichs, S.H.4    Soultanas, P.5
  • 22
    • 2942679433 scopus 로고    scopus 로고
    • DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric rings
    • Thirlway, J., Turner, I.J., Gibson, C.T., Gardiner, L., Brady, K., Allen, S., Roberts, C.J. and Soultanas, P. (2004) DnaG interacts with a linker region that joins the N- and C-domains of DnaB and induces the formation of 3-fold symmetric rings. Nucleic Acids Res., 32, 2977-2986.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 2977-2986
    • Thirlway, J.1    Turner, I.J.2    Gibson, C.T.3    Gardiner, L.4    Brady, K.5    Allen, S.6    Roberts, C.J.7    Soultanas, P.8
  • 23
    • 17044371192 scopus 로고    scopus 로고
    • The solution structure of the helicaseinteraction domain of the primase DnaG: A model for helicase activation
    • Syson, K., Thirlway, J., Hounslow, A.M., Soultanas, P. and Waltho, J.P. (2005) The solution structure of the helicaseinteraction domain of the primase DnaG: A model for helicase activation. Structure, 13, 609-616.
    • (2005) Structure , vol.13 , pp. 609-616
    • Syson, K.1    Thirlway, J.2    Hounslow, A.M.3    Soultanas, P.4    Waltho, J.P.5
  • 24
    • 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. (2005) Crosstalk between primase subunits can act to regulate primer synthesis in trans. Mol. Cell, 20, 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
  • 25
    • 0038637844 scopus 로고    scopus 로고
    • A two-protein strategy for the functional loading of a cellular replicative DNA helicase
    • Velten, M., McGovern, S., Marsin, S., Ehrlich, S.D., Noirot, P. and Polard, P. (2003) A two-protein strategy for the functional loading of a cellular replicative DNA helicase. Mol. Cell, 11, 1009-1020.
    • (2003) Mol. Cell , vol.11 , pp. 1009-1020
    • Velten, M.1    McGovern, S.2    Marsin, S.3    Ehrlich, S.D.4    Noirot, P.5    Polard, P.6
  • 26
    • 33750983641 scopus 로고    scopus 로고
    • Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis
    • Ioannou, C., Schaeffer, P.M., Dixon, N.E. and Soultanas, P. (2006) Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis. Nucleic Acids Res., 34, 5247-5258.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 5247-5258
    • Ioannou, C.1    Schaeffer, P.M.2    Dixon, N.E.3    Soultanas, P.4
  • 27
    • 84858860484 scopus 로고    scopus 로고
    • Loading mechanisms of ring helicases at replication origins
    • Soultanas, P. (2012) Loading mechanisms of ring helicases at replication origins. Mol. Microbiol., 84, 6-16.
    • (2012) Mol. Microbiol. , vol.84 , pp. 6-16
    • Soultanas, P.1
  • 28
  • 29
    • 52649177242 scopus 로고    scopus 로고
    • Hyperthermophilic Aquifex aeolicus initiates primer synthesis on a limited set of trinucleotides 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. (2008) Hyperthermophilic Aquifex aeolicus initiates primer synthesis on a limited set of trinucleotides comprised of cytosines and guanines. Nucleic Acids Res., 36, 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
  • 30
    • 44249097571 scopus 로고    scopus 로고
    • Staphylococcus aureus primase has higher initiation specificity, interacts with single-stranded DNA stronger, but is less stimulated by its helicse than Escherichia coli primase
    • Koepsell, S.A., Larson, M.A., Frey, C.A., Hinrichs, S.H. and Griep, M.A. (2008) Staphylococcus aureus primase has higher initiation specificity, interacts with single-stranded DNA stronger, but is less stimulated by its helicse than Escherichia coli primase. Mol. Microbiol., 68, 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
  • 31
    • 0042622380 scopus 로고    scopus 로고
    • Swissmodel: An automated protein-homology modelling server
    • Schwede, T., Kopp, J., Guex, N. and Peitsch, M.C. (2003) SWISSMODEL: An automated protein-homology modelling server. Nucleic Acids Res., 31, 3381-3385.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 32
    • 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. (2008) Identification of a DNA primase template tracking site redefines the geometry of primer synthesis. Nat. Struct. Mol. Biol., 15, 163-169.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 163-169
    • Corn, J.E.1    Pelton, J.G.2    Berger, J.M.3
  • 33
    • 51249093024 scopus 로고    scopus 로고
    • Insigths into the replisome from the structure of a ternary complex of the DNA polymerase IIIa-subunit
    • Wing, R.A., Bailey, S. and Steitz, T.A. (2008) Insigths into the replisome from the structure of a ternary complex of the DNA polymerase IIIa-subunit. J. Mol. Biol., 382, 859-869.
    • (2008) J. Mol. Biol. , vol.382 , pp. 859-869
    • Wing, R.A.1    Bailey, S.2    Steitz, T.A.3
  • 34
    • 33748146034 scopus 로고    scopus 로고
    • The structure of T. acquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases
    • Bailey, S., Wing, R.A. and Steitz, T.A. (2006) The structure of T. acquaticus DNA polymerase III is distinct from eukaryotic replicative DNA polymerases. Cell, 126, 893-904.
    • (2006) Cell , vol.126 , pp. 893-904
    • Bailey, S.1    Wing, R.A.2    Steitz, T.A.3
  • 36
    • 80053575452 scopus 로고    scopus 로고
    • Dynamic coupling between the motors of DNA replication: Hexameric helicase, DNA polymerase, and primase
    • Patel, S.S., Pandey, M. and Nandakumar, D. (2011) Dynamic coupling between the motors of DNA replication: Hexameric helicase, DNA polymerase, and primase. Curr. Opin. Chem. Biol., 15, 595-605.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 595-605
    • Patel, S.S.1    Pandey, M.2    Nandakumar, D.3
  • 37
    • 78650691470 scopus 로고    scopus 로고
    • The C-terminal domain of the bacterial SSB protein acts as a DNA maintenance hub at active chromosome replication forks
    • Costes, A., Lecointe, F., McGovern, S., Quevillon-Cheruel, S. and Polard, P. (2010) The C-terminal domain of the bacterial SSB protein acts as a DNA maintenance hub at active chromosome replication forks. PLoS Genet., 6, e1001238.
    • (2010) PLoS Genet. , vol.6
    • Costes, A.1    Lecointe, F.2    McGovern, S.3    Quevillon-Cheruel, S.4    Polard, P.5
  • 38
    • 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. (2006) 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, 1534-1539.
    • (2006) J. Bacteriol. , vol.188 , pp. 1534-1539
    • Thirlway, J.1    Soultanas, P.2
  • 39
    • 33745477005 scopus 로고    scopus 로고
    • Staphylococcus aureus helicase but not Escherichia coli helicase stimulates S. aureus primase activity and maintains initiation specificity
    • Koepsell, S.A., Larson, M.A., Griep, M.A. and Hinrichs, S.H. (2006) Staphylococcus aureus helicase but not Escherichia coli helicase stimulates S. aureus primase activity and maintains initiation specificity. J. Bacteriol., 188, 4673-4680.
    • (2006) J. Bacteriol. , vol.188 , pp. 4673-4680
    • Koepsell, S.A.1    Larson, M.A.2    Griep, M.A.3    Hinrichs, S.H.4
  • 40
    • 73649145533 scopus 로고    scopus 로고
    • Primase directs the release of DnaC from DnaB
    • Makowska-Grzyska, M. and Kaguni, J.M. (2010) Primase directs the release of DnaC from DnaB. Mol. Cell, 37, 90-101.
    • (2010) Mol. Cell , vol.37 , pp. 90-101
    • Makowska-Grzyska, M.1    Kaguni, J.M.2
  • 41
    • 0034636979 scopus 로고    scopus 로고
    • The 3 '-tail of a forked-duplex sterically determines whether one or two DNA strands pass through the central channel of a replication-fork helicase
    • Kaplan, D.L. (2000) The 3 '-tail of a forked-duplex sterically determines whether one or two DNA strands pass through the central channel of a replication-fork helicase. J. Mol Biol., 301, 285-299.
    • (2000) J. Mol Biol. , vol.301 , pp. 285-299
    • Kaplan, D.L.1
  • 42
    • 0017259005 scopus 로고
    • Purification and characterization of DNA polymerase III from Bacillus subtilis
    • Low, R.L., Rashbaum, S.A. and Cozzarelli, N.R. (1976) Purification and characterization of DNA polymerase III from Bacillus subtilis. J. Biol. Chem., 251, 1311-1325.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1311-1325
    • Low, R.L.1    Rashbaum, S.A.2    Cozzarelli, N.R.3
  • 43
    • 38949113141 scopus 로고    scopus 로고
    • Beta clamp directs localization of mismatch repair Bacillus subtilis
    • Simmons, L.A., Davies, B.W., Grossman, A.D. and Walker, G.C. (2008) Beta clamp directs localization of mismatch repair Bacillus subtilis. Mol. Cell, 29, 291-301.
    • (2008) Mol. Cell , vol.29 , pp. 291-301
    • Simmons, L.A.1    Davies, B.W.2    Grossman, A.D.3    Walker, G.C.4
  • 44
    • 67650741773 scopus 로고    scopus 로고
    • Motors switches, and contacts in the replisome
    • Hamdan, S.M. and Richardson, C.C. (2009) Motors, switches, and contacts in the replisome. Annu. Rev. Biochem., 78, 205-243.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 205-243
    • Hamdan, S.M.1    Richardson, C.C.2
  • 45
    • 0034635137 scopus 로고    scopus 로고
    • Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus
    • Bird, L.E., Pan, H., Soultanas, P. and Wigley, D.B. (2000) Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus. Biochemistry, 39, 171-182.
    • (2000) Biochemistry , vol.39 , pp. 171-182
    • Bird, L.E.1    Pan, H.2    Soultanas, P.3    Wigley, D.B.4
  • 46
    • 0347993077 scopus 로고    scopus 로고
    • Mechanisms and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis
    • Mitkova, A.V., Khopde, S.M. and Biswas, S.B. (2003) Mechanisms and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis. J. Biol. Chem., 278, 52253-52261.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52253-52261
    • Mitkova, A.V.1    Khopde, S.M.2    Biswas, S.B.3
  • 47
    • 68249117713 scopus 로고    scopus 로고
    • Mechanisms of DNA binding and regulation of Bacillus anthracis DNA primase
    • Biswas, S.B., Wydra, E. and Biswas, E.E. (2009) Mechanisms of DNA binding and regulation of Bacillus anthracis DNA primase. Biochemistry, 48, 7373-7382.
    • (2009) Biochemistry , vol.48 , pp. 7373-7382
    • Biswas, S.B.1    Wydra, E.2    Biswas, E.E.3
  • 48
    • 0034141871 scopus 로고    scopus 로고
    • DnaB helicase stimulates primer synthesis activity on short oligonucleotide templates
    • Johnson, S.K., Bhattacharyya, S. and Griep, M.A. (2000) DnaB helicase stimulates primer synthesis activity on short oligonucleotide templates. Biochemistry, 39, 736-744.
    • (2000) Biochemistry , vol.39 , pp. 736-744
    • Johnson, S.K.1    Bhattacharyya, S.2    Griep, M.A.3
  • 49
    • 0033534380 scopus 로고    scopus 로고
    • Trading places on DNA; a three-point switch undelies primer handoff from primase to the replicative DNA polymerase
    • Yuzhakov, A., Kelman, Z. and O'Donnell, M. (1999) Trading places on DNA; a three-point switch undelies primer handoff from primase to the replicative DNA polymerase. Cell, 96, 153-163.
    • (1999) Cell , vol.96 , pp. 153-163
    • Yuzhakov, A.1    Kelman, Z.2    O'Donnell, M.3
  • 50
    • 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. (1993) Enzymatic characterization of the individual mammalian primase subunits reveals a biphasic mechanism for initiation of DNA replication. J. Biol. Chem., 268, 26179-26189.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26179-26189
    • Copeland, W.C.1    Wang, T.S.2
  • 51
    • 0033613231 scopus 로고    scopus 로고
    • Interactions of DNA woth 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. (1999) Interactions of DNA woth human DNA primase monitored with photoactivatable cross-linking agents: Implications for the role of the p58 subunit. Biochemistry, 38, 12899-12907.
    • (1999) Biochemistry , vol.38 , pp. 12899-12907
    • Arezi, B.1    Kirk, B.W.2    Copeland, W.C.3    Kuchta, R.D.4
  • 52
    • 0037117724 scopus 로고    scopus 로고
    • The p58 subunit of human DNA primase is important for primer initiation, elongation, and counting
    • Zerbe, L.K. and Kuchta, R.D. (2002) The p58 subunit of human DNA primase is important for primer initiation, elongation, and counting. Biochemistry, 41, 4891-4900.
    • (2002) Biochemistry , vol.41 , pp. 4891-4900
    • Zerbe, L.K.1    Kuchta, R.D.2
  • 54
    • 79955549803 scopus 로고    scopus 로고
    • Breaking the rules: Bacteria that use several DNA polymerase IIIs
    • McHenry, C.S. (2011b) Breaking the rules: Bacteria that use several DNA polymerase IIIs. EMBO Rep., 12, 408-414.
    • (2011) EMBO Rep. , vol.12 , pp. 408-414
    • McHenry, C.S.1
  • 55
    • 80054843376 scopus 로고    scopus 로고
    • Mismatch repair causes the dynamic release of an essential DNA polymerase from the replication fork
    • Klocko, A.D., Schroeder, J.W., Walsh, B.W., Lenhart, J.S., Evans, M.L. and Simmons, L.A. (2011) Mismatch repair causes the dynamic release of an essential DNA polymerase from the replication fork. Mol. Microbiol., 82, 648-663.
    • (2011) Mol. Microbiol. , vol.82 , pp. 648-663
    • Klocko, A.D.1    Schroeder, J.W.2    Walsh, B.W.3    Lenhart, J.S.4    Evans, M.L.5    Simmons, L.A.6
  • 56
    • 84868306613 scopus 로고    scopus 로고
    • The chromosomal replication machinery of low G+C content Firmicutes
    • Briggs, G.S., Smits, W.K. and Soultanas, P. (2012) The chromosomal replication machinery of low G+C content Firmicutes. J. Bacteriol., 194, 5162-5170.
    • (2012) J. Bacteriol. , vol.194 , pp. 5162-5170
    • Briggs, G.S.1    Smits, W.K.2    Soultanas, P.3
  • 57
    • 84856982530 scopus 로고    scopus 로고
    • Distinct co-evolution patterns of genes associated to DNA polymerase III DnaE and PolC
    • Engelen, S., Vallenet, D., Me'digue, C. and Danchin, A. (2012) Distinct co-evolution patterns of genes associated to DNA polymerase III DnaE and PolC. BMC Genomics, 13, 69.
    • (2012) BMC Genomics , vol.13 , pp. 69
    • Engelen, S.1    Vallenet, D.2    Me'digue, C.3    Danchin, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.