메뉴 건너뛰기




Volumn 52, Issue 6, 2013, Pages 844-854

Nucleotide and partner-protein control of bacterial replicative helicase structure and function

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DNAB HELICASE; MOLECULAR MOTOR; NUCLEOTIDE;

EID: 84891136745     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2013.11.016     Document Type: Article
Times cited : (47)

References (61)
  • 2
    • 84876286140 scopus 로고    scopus 로고
    • The bacterial DnaC helicase loader is a DnaB ring breaker
    • Arias-Palomo E., O'Shea V.L., Hood I.V., Berger J.M. The bacterial DnaC helicase loader is a DnaB ring breaker. Cell 2013, 153:438-448.
    • (2013) Cell , vol.153 , pp. 438-448
    • Arias-Palomo, E.1    O'Shea, V.L.2    Hood, I.V.3    Berger, J.M.4
  • 3
    • 34547886124 scopus 로고    scopus 로고
    • The crystal structure of the Thermus aquaticus DnaB helicase monomer
    • Bailey S., Eliason W.K., Steitz T.A. The crystal structure of the Thermus aquaticus DnaB helicase monomer. Nucleic Acids Res. 2007, 35:4728-4736.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 4728-4736
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 4
    • 35348979683 scopus 로고    scopus 로고
    • Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase
    • Bailey S., Eliason W.K., Steitz T.A. Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science 2007, 318:459-463.
    • (2007) Science , vol.318 , pp. 459-463
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 5
    • 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., Wigley D.B. Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus. Biochemistry 2000, 39:171-182.
    • (2000) Biochemistry , vol.39 , pp. 171-182
    • Bird, L.E.1    Pan, H.2    Soultanas, P.3    Wigley, D.B.4
  • 6
    • 0033600561 scopus 로고    scopus 로고
    • Mechanism of DNA binding by the DnaB helicase of Escherichia coli: analysis of the roles of domain gamma in DNA binding
    • Biswas E.E., Biswas S.B. Mechanism of DNA binding by the DnaB helicase of Escherichia coli: analysis of the roles of domain gamma in DNA binding. Biochemistry 1999, 38:10929-10939.
    • (1999) Biochemistry , vol.38 , pp. 10929-10939
    • Biswas, E.E.1    Biswas, S.B.2
  • 7
    • 0033600551 scopus 로고    scopus 로고
    • Mechanism of DnaB helicase of Escherichia coli: structural domains involved in ATP hydrolysis, DNA binding, and oligomerization
    • Biswas E.E., Biswas S.B. Mechanism of DnaB helicase of Escherichia coli: structural domains involved in ATP hydrolysis, DNA binding, and oligomerization. Biochemistry 1999, 38:10919-10928.
    • (1999) Biochemistry , vol.38 , pp. 10919-10928
    • Biswas, E.E.1    Biswas, S.B.2
  • 8
    • 44349172245 scopus 로고    scopus 로고
    • Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase
    • Biswas T., Tsodikov O.V. Hexameric ring structure of the N-terminal domain of Mycobacterium tuberculosis DnaB helicase. FEBS J. 2008, 275:3064-3071.
    • (2008) FEBS J. , vol.275 , pp. 3064-3071
    • Biswas, T.1    Tsodikov, O.V.2
  • 9
    • 0022829375 scopus 로고
    • The dnaB protein of Escherichia coli: mechanism of nucleotide binding, hydrolysis, and modulation by dnaC protein
    • Biswas E.E., Biswas S.B., Bishop J.E. The dnaB protein of Escherichia coli: mechanism of nucleotide binding, hydrolysis, and modulation by dnaC protein. Biochemistry 1986, 25:7368-7374.
    • (1986) Biochemistry , vol.25 , pp. 7368-7374
    • Biswas, E.E.1    Biswas, S.B.2    Bishop, J.E.3
  • 10
    • 0028068822 scopus 로고
    • Structure and function of Escherichia coli DnaB protein: role of the N-terminal domain in helicase activity
    • Biswas S.B., Chen P.H., Biswas E.E. Structure and function of Escherichia coli DnaB protein: role of the N-terminal domain in helicase activity. Biochemistry 1994, 33:11307-11314.
    • (1994) Biochemistry , vol.33 , pp. 11307-11314
    • Biswas, S.B.1    Chen, P.H.2    Biswas, E.E.3
  • 11
    • 77952809666 scopus 로고    scopus 로고
    • Insights into the MCM functional mechanism: lessons learned from the archaeal MCM complex
    • Brewster A.S., Chen X.S. Insights into the MCM functional mechanism: lessons learned from the archaeal MCM complex. Crit. Rev. Biochem. Mol. Biol. 2010, 45:243-256.
    • (2010) Crit. Rev. Biochem. Mol. Biol. , vol.45 , pp. 243-256
    • Brewster, A.S.1    Chen, X.S.2
  • 12
    • 0034714241 scopus 로고    scopus 로고
    • Identification of a region of Escherichia coli DnaB required for functional interaction with DnaG at the replication fork
    • Chang P., Marians K.J. Identification of a region of Escherichia coli DnaB required for functional interaction with DnaG at the replication fork. J.Biol. Chem. 2000, 275:26187-26195.
    • (2000) J.Biol. Chem. , vol.275 , pp. 26187-26195
    • Chang, P.1    Marians, K.J.2
  • 15
    • 84878939444 scopus 로고    scopus 로고
    • Mechanisms for initiating cellular DNA replication
    • Costa A., Hood I.V., Berger J.M. Mechanisms for initiating cellular DNA replication. Annu. Rev. Biochem. 2013, 82:25-54.
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 25-54
    • Costa, A.1    Hood, I.V.2    Berger, J.M.3
  • 16
    • 0034686075 scopus 로고    scopus 로고
    • Characterization of the unique C terminus of the Escherichia coli tau DnaX protein. Monomeric C-tau binds alpha AND DnaB and can partially replace tau in reconstituted replication forks
    • Dallmann H.G., Kim S., Pritchard A.E., Marians K.J., McHenry C.S. Characterization of the unique C terminus of the Escherichia coli tau DnaX protein. Monomeric C-tau binds alpha AND DnaB and can partially replace tau in reconstituted replication forks. J.Biol. Chem. 2000, 275:15512-15519.
    • (2000) J.Biol. Chem. , vol.275 , pp. 15512-15519
    • Dallmann, H.G.1    Kim, S.2    Pritchard, A.E.3    Marians, K.J.4    McHenry, C.S.5
  • 17
    • 0033152872 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal domain of the DnaB hexameric helicase
    • Fass D., Bogden C.E., Berger J.M. Crystal structure of the N-terminal domain of the DnaB hexameric helicase. Structure 1999, 7:691-698.
    • (1999) Structure , vol.7 , pp. 691-698
    • Fass, D.1    Bogden, C.E.2    Berger, J.M.3
  • 18
    • 0037616144 scopus 로고    scopus 로고
    • Interactions of the Escherichia coli DnaB helicase hexamer with the replication factor the DnaC protein. Effect of nucleotide cofactors and the ssDNA on protein-protein interactions and the topology of the complex
    • Galletto R., Jezewska M.J., Bujalowski W. Interactions of the Escherichia coli DnaB helicase hexamer with the replication factor the DnaC protein. Effect of nucleotide cofactors and the ssDNA on protein-protein interactions and the topology of the complex. J.Mol. Biol. 2003, 329:441-465.
    • (2003) J.Mol. Biol. , vol.329 , pp. 441-465
    • Galletto, R.1    Jezewska, M.J.2    Bujalowski, W.3
  • 19
    • 0742306908 scopus 로고    scopus 로고
    • The clamp-loader-helicase interaction in Bacillus. Atomic force microscopy reveals the structural organisation of the DnaB-tau complex in Bacillus
    • Haroniti A., Anderson C., Doddridge Z., Gardiner L., Roberts C.J., Allen S., Soultanas P. The clamp-loader-helicase interaction in Bacillus. Atomic force microscopy reveals the structural organisation of the DnaB-tau complex in Bacillus. J.Mol. Biol. 2004, 336:381-393.
    • (2004) J.Mol. Biol. , vol.336 , pp. 381-393
    • Haroniti, A.1    Anderson, C.2    Doddridge, Z.3    Gardiner, L.4    Roberts, C.J.5    Allen, S.6    Soultanas, P.7
  • 20
    • 0026704305 scopus 로고
    • Organization and evolution of bacterial and bacteriophage primase-helicase systems
    • Ilyina T.V., Gorbalenya A.E., Koonin E.V. Organization and evolution of bacterial and bacteriophage primase-helicase systems. J.Mol. Evol. 1992, 34:351-357.
    • (1992) J.Mol. Evol. , vol.34 , pp. 351-357
    • Ilyina, T.V.1    Gorbalenya, A.E.2    Koonin, E.V.3
  • 21
    • 84867538324 scopus 로고    scopus 로고
    • The hexameric helicase DnaB adopts a nonplanar conformation during translocation
    • Itsathitphaisarn O., Wing R.A., Eliason W.K., Wang J., Steitz T.A. The hexameric helicase DnaB adopts a nonplanar conformation during translocation. Cell 2012, 151:267-277.
    • (2012) Cell , vol.151 , pp. 267-277
    • Itsathitphaisarn, O.1    Wing, R.A.2    Eliason, W.K.3    Wang, J.4    Steitz, T.A.5
  • 22
    • 1642325936 scopus 로고    scopus 로고
    • Evolutionary history and higher order classification of AAA+ ATPases
    • Iyer L.M., Leipe D.D., Koonin E.V., Aravind L. Evolutionary history and higher order classification of AAA+ ATPases. J.Struct. Biol. 2004, 146:11-31.
    • (2004) J.Struct. Biol. , vol.146 , pp. 11-31
    • Iyer, L.M.1    Leipe, D.D.2    Koonin, E.V.3    Aravind, L.4
  • 23
    • 0032562822 scopus 로고    scopus 로고
    • Does single-stranded DNA pass through the inner channel of the protein hexamer in the complex with the Escherichia coli DnaB Helicase? Fluorescence energy transfer studies
    • Jezewska M.J., Rajendran S., Bujalowska D., Bujalowski W. Does single-stranded DNA pass through the inner channel of the protein hexamer in the complex with the Escherichia coli DnaB Helicase? Fluorescence energy transfer studies. J.Biol. Chem. 1998, 273:10515-10529.
    • (1998) J.Biol. Chem. , vol.273 , pp. 10515-10529
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowska, D.3    Bujalowski, W.4
  • 24
    • 0034141871 scopus 로고    scopus 로고
    • DnaB helicase stimulates primer synthesis activity on short oligonucleotide templates
    • Johnson S.K., Bhattacharyya S., Griep M.A. DnaB helicase stimulates primer synthesis activity on short oligonucleotide templates. Biochemistry 2000, 39:736-744.
    • (2000) Biochemistry , vol.39 , pp. 736-744
    • Johnson, S.K.1    Bhattacharyya, S.2    Griep, M.A.3
  • 25
    • 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. 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. 2000, 301:285-299.
    • (2000) J.Mol. Biol. , vol.301 , pp. 285-299
    • Kaplan, D.L.1
  • 26
    • 0036753338 scopus 로고    scopus 로고
    • DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands
    • Kaplan D.L., O'Donnell M. DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands. Mol. Cell 2002, 10:647-657.
    • (2002) Mol. Cell , vol.10 , pp. 647-657
    • Kaplan, D.L.1    O'Donnell, M.2
  • 27
    • 0033548710 scopus 로고    scopus 로고
    • DnaB from Thermus aquaticus unwinds forked duplex DNA with an asymmetric tail length dependence
    • Kaplan D.L., Steitz T.A. DnaB from Thermus aquaticus unwinds forked duplex DNA with an asymmetric tail length dependence. J.Biol. Chem. 1999, 274:6889-6897.
    • (1999) J.Biol. Chem. , vol.274 , pp. 6889-6897
    • Kaplan, D.L.1    Steitz, T.A.2
  • 28
    • 70449570532 scopus 로고    scopus 로고
    • Three-dimensional structure of N-terminal domain of DnaB helicase and helicase-primase interactions in Helicobacter pylori
    • Kashav T., Nitharwal R., Abdulrehman S.A., Gabdoulkhakov A., Saenger W., Dhar S.K., Gourinath S. Three-dimensional structure of N-terminal domain of DnaB helicase and helicase-primase interactions in Helicobacter pylori. PLoS ONE 2009, 4:e7515.
    • (2009) PLoS ONE , vol.4
    • Kashav, T.1    Nitharwal, R.2    Abdulrehman, S.A.3    Gabdoulkhakov, A.4    Saenger, W.5    Dhar, S.K.6    Gourinath, S.7
  • 29
    • 0030070356 scopus 로고    scopus 로고
    • Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement
    • Kim S., Dallmann H.G., McHenry C.S., Marians K.J. Coupling of a replicative polymerase and helicase: a tau-DnaB interaction mediates rapid replication fork movement. Cell 1996, 84:643-650.
    • (1996) Cell , vol.84 , pp. 643-650
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 31
    • 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., Hinrichs S.H. Staphylococcus aureus helicase but not Escherichia coli helicase stimulates S. aureus primase activity and maintains initiation specificity. J.Bacteriol. 2006, 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
  • 32
    • 0022977660 scopus 로고
    • The Escherichia coli dnaB replication protein is a DNA helicase
    • LeBowitz J.H., McMacken R. The Escherichia coli dnaB replication protein is a DNA helicase. J.Biol. Chem. 1986, 261:4738-4748.
    • (1986) J.Biol. Chem. , vol.261 , pp. 4738-4748
    • LeBowitz, J.H.1    McMacken, R.2
  • 33
    • 0033975419 scopus 로고    scopus 로고
    • The bacterial replicative helicase DnaB evolved from a RecA duplication
    • Leipe D.D., Aravind L., Grishin N.V., Koonin E.V. The bacterial replicative helicase DnaB evolved from a RecA duplication. Genome Res. 2000, 10:5-16.
    • (2000) Genome Res. , vol.10 , pp. 5-16
    • Leipe, D.D.1    Aravind, L.2    Grishin, N.V.3    Koonin, E.V.4
  • 34
    • 0142011067 scopus 로고    scopus 로고
    • Evolution and classification of P-loop kinases and related proteins
    • Leipe D.D., Koonin E.V., Aravind L. Evolution and classification of P-loop kinases and related proteins. J.Mol. Biol. 2003, 333:781-815.
    • (2003) J.Mol. Biol. , vol.333 , pp. 781-815
    • Leipe, D.D.1    Koonin, E.V.2    Aravind, L.3
  • 35
    • 63349092249 scopus 로고    scopus 로고
    • The crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNA
    • Lo Y.H., Tsai K.L., Sun Y.J., Chen W.T., Huang C.Y., Hsiao C.D. The crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNA. Nucleic Acids Res. 2009, 37:804-814.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 804-814
    • Lo, Y.H.1    Tsai, K.L.2    Sun, Y.J.3    Chen, W.T.4    Huang, C.Y.5    Hsiao, C.D.6
  • 36
    • 0029803922 scopus 로고    scopus 로고
    • Direct physical interaction between DnaG primase and DnaB helicase of Escherichia coli is necessary for optimal synthesis of primer RNA
    • Lu Y.B., Ratnakar P.V.A.L., Mohanty B.K., Bastia D. Direct physical interaction between DnaG primase and DnaB helicase of Escherichia coli is necessary for optimal synthesis of primer RNA. Proc. Natl. Acad. Sci. USA 1996, 93:12902-12907.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12902-12907
    • Lu, Y.B.1    Ratnakar, P.V.A.L.2    Mohanty, B.K.3    Bastia, D.4
  • 38
    • 73649145533 scopus 로고    scopus 로고
    • Primase directs the release of DnaC from DnaB
    • Makowska-Grzyska M., Kaguni J.M. Primase directs the release of DnaC from DnaB. Mol. Cell 2010, 37:90-101.
    • (2010) Mol. Cell , vol.37 , pp. 90-101
    • Makowska-Grzyska, M.1    Kaguni, J.M.2
  • 39
    • 0036930209 scopus 로고    scopus 로고
    • Bacillus subtilis tau subunit of DNA polymerase III interacts with bacteriophage SPP1 replicative DNA helicase G40P
    • Martínez-Jiménez M.I., Mesa P., Alonso J.C. Bacillus subtilis tau subunit of DNA polymerase III interacts with bacteriophage SPP1 replicative DNA helicase G40P. Nucleic Acids Res. 2002, 30:5056-5064.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 5056-5064
    • Martínez-Jiménez, M.I.1    Mesa, P.2    Alonso, J.C.3
  • 40
    • 0347993077 scopus 로고    scopus 로고
    • Mechanism and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis
    • Mitkova A.V., Khopde S.M., Biswas S.B. Mechanism and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis. J.Biol. Chem. 2003, 278:52253-52261.
    • (2003) J.Biol. Chem. , vol.278 , pp. 52253-52261
    • Mitkova, A.V.1    Khopde, S.M.2    Biswas, S.B.3
  • 41
    • 0021759104 scopus 로고
    • Structural and functional studies of the dnaB protein using limited proteolysis. Characterization of domains for DNA-dependent ATP hydrolysis and for protein association in the primosome
    • Nakayama N., Arai N., Kaziro Y., Arai K. Structural and functional studies of the dnaB protein using limited proteolysis. Characterization of domains for DNA-dependent ATP hydrolysis and for protein association in the primosome. J.Biol. Chem. 1984, 259:88-96.
    • (1984) J.Biol. Chem. , vol.259 , pp. 88-96
    • Nakayama, N.1    Arai, N.2    Kaziro, Y.3    Arai, K.4
  • 42
    • 84855440021 scopus 로고    scopus 로고
    • DNA binding activity of Helicobacter pylori DnaB helicase: the role of the N-terminal domain in modulating DNA binding activities
    • Nitharwal R.G., Verma V., Subbarao N., Dasgupta S., Choudhury N.R., Dhar S.K. DNA binding activity of Helicobacter pylori DnaB helicase: the role of the N-terminal domain in modulating DNA binding activities. FEBS J. 2012, 279:234-250.
    • (2012) FEBS J. , vol.279 , pp. 234-250
    • Nitharwal, R.G.1    Verma, V.2    Subbarao, N.3    Dasgupta, S.4    Choudhury, N.R.5    Dhar, S.K.6
  • 44
    • 34047149973 scopus 로고    scopus 로고
    • Replisome mechanics: insights into a twin DNA polymerase machine
    • Pomerantz R.T., O'Donnell M. Replisome mechanics: insights into a twin DNA polymerase machine. Trends Microbiol. 2007, 15:156-164.
    • (2007) Trends Microbiol. , vol.15 , pp. 156-164
    • Pomerantz, R.T.1    O'Donnell, M.2
  • 45
    • 70549085855 scopus 로고    scopus 로고
    • Eukaryotic DNA replication control: lock and load, then fire
    • Remus D., Diffley J.F. Eukaryotic DNA replication control: lock and load, then fire. Curr. Opin. Cell Biol. 2009, 21:771-777.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 771-777
    • Remus, D.1    Diffley, J.F.2
  • 46
    • 0029147295 scopus 로고
    • A structural model for the Escherichia coli DnaB helicase based on electron microscopy data
    • San Martin M.C., Stamford N.P., Dammerova N., Dixon N.E., Carazo J.M. A structural model for the Escherichia coli DnaB helicase based on electron microscopy data. J.Struct. Biol. 1995, 114:167-176.
    • (1995) J.Struct. Biol. , vol.114 , pp. 167-176
    • San Martin, M.C.1    Stamford, N.P.2    Dammerova, N.3    Dixon, N.E.4    Carazo, J.M.5
  • 47
    • 0032522423 scopus 로고    scopus 로고
    • Three-dimensional reconstructions from cryoelectron microscopy images reveal an intimate complex between helicase DnaB and its loading partner DnaC
    • San Martin C., Radermacher M., Wolpensinger B., Engel A., Miles C.S., Dixon N.E., Carazo J.M. Three-dimensional reconstructions from cryoelectron microscopy images reveal an intimate complex between helicase DnaB and its loading partner DnaC. Structure 1998, 6:501-509.
    • (1998) Structure , vol.6 , pp. 501-509
    • San Martin, C.1    Radermacher, M.2    Wolpensinger, B.3    Engel, A.4    Miles, C.S.5    Dixon, N.E.6    Carazo, J.M.7
  • 48
    • 0033812649 scopus 로고    scopus 로고
    • The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli
    • Seitz H., Weigel C., Messer W. The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli. Mol. Microbiol. 2000, 37:1270-1279.
    • (2000) Mol. Microbiol. , vol.37 , pp. 1270-1279
    • Seitz, H.1    Weigel, C.2    Messer, W.3
  • 49
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • Singleton M.R., Sawaya M.R., Ellenberger T., Wigley D.B. Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides. Cell 2000, 101:589-600.
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 50
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton M.R., Dillingham M.S., Wigley D.B. Structure and mechanism of helicases and nucleic acid translocases. Annu. Rev. Biochem. 2007, 76:23-50.
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 51
    • 17044371192 scopus 로고    scopus 로고
    • Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation
    • Syson K., Thirlway J., Hounslow A.M., Soultanas P., Waltho J.P. Solution structure of the helicase-interaction domain of the primase DnaG: a model for helicase activation. Structure 2005, 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
  • 52
    • 0025690281 scopus 로고
    • Characterization of the ATP binding site on Escherichia coli DNA gyrase. Affinity labeling of Lys-103 and Lys-110 of the B subunit by pyridoxal 5'-diphospho-5'-adenosine
    • Tamura J.K., Gellert M. Characterization of the ATP binding site on Escherichia coli DNA gyrase. Affinity labeling of Lys-103 and Lys-110 of the B subunit by pyridoxal 5'-diphospho-5'-adenosine. J.Biol. Chem. 1990, 265:21342-21349.
    • (1990) J.Biol. Chem. , vol.265 , pp. 21342-21349
    • Tamura, J.K.1    Gellert, M.2
  • 53
    • 70350344051 scopus 로고    scopus 로고
    • Running in reverse: the structural basis for translocation polarity in hexameric helicases
    • Thomsen N.D., Berger J.M. Running in reverse: the structural basis for translocation polarity in hexameric helicases. Cell 2009, 139:523-534.
    • (2009) Cell , vol.139 , pp. 523-534
    • Thomsen, N.D.1    Berger, J.M.2
  • 54
    • 0029788209 scopus 로고    scopus 로고
    • The interaction between helicase and primase sets the replication fork clock
    • Tougu K., Marians K.J. The interaction between helicase and primase sets the replication fork clock. J.Biol. Chem. 1996, 271:21398-21405.
    • (1996) J.Biol. Chem. , vol.271 , pp. 21398-21405
    • Tougu, K.1    Marians, K.J.2
  • 55
    • 0024520416 scopus 로고
    • The dnaB-dnaC replication protein complex of Escherichia coli. II. Role of the complex in mobilizing dnaB functions
    • Wahle E., Lasken R.S., Kornberg A. The dnaB-dnaC replication protein complex of Escherichia coli. II. Role of the complex in mobilizing dnaB functions. J.Biol. Chem. 1989, 264:2469-2475.
    • (1989) J.Biol. Chem. , vol.264 , pp. 2469-2475
    • Wahle, E.1    Lasken, R.S.2    Kornberg, A.3
  • 56
    • 7444249512 scopus 로고    scopus 로고
    • Nucleotide-dependent domain motions within rings of the RecA/AAA(+) superfamily
    • Wang J. Nucleotide-dependent domain motions within rings of the RecA/AAA(+) superfamily. J.Struct. Biol. 2004, 148:259-267.
    • (2004) J.Struct. Biol. , vol.148 , pp. 259-267
    • Wang, J.1
  • 58
    • 1542563746 scopus 로고    scopus 로고
    • NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer
    • Weigelt J., Brown S.E., Miles C.S., Dixon N.E., Otting G. NMR structure of the N-terminal domain of E. coli DnaB helicase: implications for structure rearrangements in the helicase hexamer. Structure 1999, 7:681-690.
    • (1999) Structure , vol.7 , pp. 681-690
    • Weigelt, J.1    Brown, S.E.2    Miles, C.S.3    Dixon, N.E.4    Otting, G.5
  • 59
    • 74849098714 scopus 로고    scopus 로고
    • Characterization of physical interaction between replication initiator protein DnaA and replicative helicase from Mycobacterium tuberculosis H37Rv
    • Xie Y., He Z.G. Characterization of physical interaction between replication initiator protein DnaA and replicative helicase from Mycobacterium tuberculosis H37Rv. Biochemistry (Mosc). 2009, 74:1320-1327.
    • (2009) Biochemistry (Mosc). , vol.74 , pp. 1320-1327
    • Xie, Y.1    He, Z.G.2
  • 61
    • 0029984117 scopus 로고    scopus 로고
    • The hexameric E. coli DnaB helicase can exist in different Quaternary states
    • Yu X., Jezewska M.J., Bujalowski W., Egelman E.H. The hexameric E. coli DnaB helicase can exist in different Quaternary states. J.Mol. Biol. 1996, 259:7-14.
    • (1996) J.Mol. Biol. , vol.259 , pp. 7-14
    • Yu, X.1    Jezewska, M.J.2    Bujalowski, W.3    Egelman, E.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.