메뉴 건너뛰기




Volumn 279, Issue 2, 2012, Pages 234-250

DNA binding activity of Helicobacter pylori DnaB helicase: The role of the N-terminal domain in modulating DNA binding activities

Author keywords

DNA binding; DNA replication; DnaB helicase; Helicobacter pylori; ssDNA

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL DNA; DNAB HELICASE; SINGLE STRANDED DNA;

EID: 84855440021     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08418.x     Document Type: Article
Times cited : (12)

References (58)
  • 1
    • 0022977660 scopus 로고
    • The Escherichia coli dnaB replication protein is a DNA helicase
    • LeBowitz JM, &, McMacken R, (1986) The Escherichia coli DnaB protein is a DNA helicase. J Biol Chem 261, 4738-4748. (Pubitemid 17207386)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.10 , pp. 4738-4748
    • LeBowitz, J.H.1    McMacken, R.2
  • 2
    • 0036753338 scopus 로고    scopus 로고
    • DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands
    • DOI 10.1016/S1097-2765(02)00642-1
    • Kaplan DL, &, O'Donnell M, (2002) DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands. Mol Cell 10, 647-657. (Pubitemid 35284180)
    • (2002) Molecular Cell , vol.10 , Issue.3 , pp. 647-657
    • Kaplan, D.L.1    O'Donnell, M.2
  • 3
    • 35348979683 scopus 로고    scopus 로고
    • Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase
    • DOI 10.1126/science.1147353
    • Bailey S, Eliason WK, &, Steitz TA, (2007) Structure of hexameric DnaB helicase and its complex with a domain of DnaG primase. Science 318, 459-463. (Pubitemid 47614533)
    • (2007) Science , vol.318 , Issue.5849 , pp. 459-463
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 4
    • 0033786801 scopus 로고    scopus 로고
    • Structure and function of hexameric helicases
    • Patel SS, &, Picha KM, (2000) structure and function of hexameric helicases. Annu Rev Biochem 69, 651-697.
    • (2000) Annu Rev Biochem , vol.69 , pp. 651-697
    • Patel, S.S.1    Picha, K.M.2
  • 5
    • 34547886124 scopus 로고    scopus 로고
    • The crystal structure of the Thermus aquaticus DnaB helicase monomer
    • DOI 10.1093/nar/gkm507
    • Bailey S, Eliason WK, &, Steitz TA, (2007) The crystal structure of the Thermus aquaticus DnaB helicase monomer. Nucleic Acids Res 35, 4728-4736. (Pubitemid 47250344)
    • (2007) Nucleic Acids Research , vol.35 , Issue.14 , pp. 4728-4736
    • Bailey, S.1    Eliason, W.K.2    Steitz, T.A.3
  • 7
    • 63349092249 scopus 로고    scopus 로고
    • The crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNA
    • Lo YH, Tsai KL, Sun YJ, Huang CY, &, Hasiao CD, (2009) The crystal structure of a replicative hexameric helicase DnaC and its complex with single-stranded DNA. Nucleic Acids Res 37, 804-814.
    • (2009) Nucleic Acids Res , vol.37 , pp. 804-814
    • Lo, Y.H.1    Tsai, K.L.2    Sun, Y.J.3    Huang, C.Y.4    Hasiao, C.D.5
  • 8
    • 0032716810 scopus 로고    scopus 로고
    • Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7
    • Sawaya MR, Guo S, Tabor S, Richardson CC, &, Ellenberger T, (1999) Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7. Cell 99, 167-177.
    • (1999) Cell , vol.99 , pp. 167-177
    • Sawaya, M.R.1    Guo, S.2    Tabor, S.3    Richardson, C.C.4    Ellenberger, T.5
  • 9
    • 0033975419 scopus 로고    scopus 로고
    • The bacterial replicative helicase DnaB evolved from a RecA duplication
    • Leipe DD, Aravind L, Grishin NV, &, Koonin EV, (2000) The bacterial replicative helicase DnaB evolved from a RecA duplication. Genome Res 10, 5-16. (Pubitemid 30095250)
    • (2000) Genome Research , vol.10 , Issue.1 , pp. 5-16
    • Leipe, D.D.1    Aravind, L.2    Grishin, N.V.3    Koonin, E.V.4
  • 10
    • 0026704305 scopus 로고
    • Organization and evolution of bacterial and bacteriophage primase-helicase systems
    • Ilyina TV, Gorbalenya AE, &, Koonin EV, (1992) Organization and evolution of bacterial and bacteriophage primase-helicase systems. J Mol Evol 34, 351-357.
    • (1992) J Mol Evol , vol.34 , pp. 351-357
    • Ilyina, T.V.1    Gorbalenya, A.E.2    Koonin, E.V.3
  • 11
    • 0001607723 scopus 로고
    • Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker JE, Saraste M, Runswick MJ, &, Gay NJ, (1982) Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J 1, 945-951.
    • (1982) EMBO J , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 12
    • 0037106446 scopus 로고    scopus 로고
    • Site directed mutagenesis reveals roles for conserved amino acid residues in the hexameric DNA helicase DnaB from Bacillus stearothermophilus
    • Soultanas P, &, Wigley DB, (2002) Site directed mutagenesis reveals roles for conserved amino acid residues in the hexameric DNA helicase DnaB from Bacillus stearothermophilus. Nucleic Acids Res 30, 4051-4060.
    • (2002) Nucleic Acids Res , vol.30 , pp. 4051-4060
    • Soultanas, P.1    Wigley, D.B.2
  • 13
  • 14
    • 0028102357 scopus 로고
    • DnaA protein directs the binding of DnaB protein in initiation of DNA replication in Escherichia coli
    • Marszalek J, &, Kaguni JM, (1994) DnaA protein directs the binding of DnaB protein in initiation of DNA replication in Escherichia coli. J Biol Chem 269, 4883-4890. (Pubitemid 24239465)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.7 , pp. 4883-4890
    • Marszalek, J.1    Kaguni, J.M.2
  • 15
    • 0000579776 scopus 로고
    • Interaction of Escherichia coli dnaB and dnaC(D) gene product in vitro
    • Wickner S, &, Hurwitz J, (1975) Interaction of Escherichia coli dnaB and dnaC(D) gene product in vitro. Proc Natl Acad Sci USA 72, 921-925.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 921-925
    • Wickner, S.1    Hurwitz, J.2
  • 16
    • 0030070356 scopus 로고    scopus 로고
    • Coupling of a replicative polymerase and helicase: A τ-DnaB interaction mediates rapid replication fork movement
    • DOI 10.1016/S0092-8674(00)81039-9
    • Kim S, Dallmann HG, McHenry CS, &, Marians KJ, (1996) Coupling of a replicative polymerase and helicase: a τ-DnaB interaction mediates rapid replication fork movement. Cell 84, 643-650. (Pubitemid 26071744)
    • (1996) Cell , vol.84 , Issue.4 , pp. 643-650
    • Kim, S.1    Dallmann, H.G.2    McHenry, C.S.3    Marians, K.J.4
  • 18
    • 0347993077 scopus 로고    scopus 로고
    • Mechanism and Stoichiometry of Interaction of DnaG Primase with DnaB Helicase of Escherichia coli in RNA Primer Synthesis
    • DOI 10.1074/jbc.M308956200
    • Mitkova AV, Khopde SM, &, Biswas SB, (2003) Mechanism and stoichiometry of interaction of DnaG primase with DnaB helicase of Escherichia coli in RNA primer synthesis. J Biol Chem 278, 52253-52261. (Pubitemid 38035813)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.52 , pp. 52253-52261
    • Mitkova, A.V.1    Khopde, S.M.2    Biswas, S.B.3
  • 19
    • 0034635137 scopus 로고    scopus 로고
    • Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus
    • DOI 10.1021/bi9918801
    • Bird LE, Hu P, Soultanas P, &, Wigley DB, (2000) Mapping protein-protein interactions within a stable complex of DnaG primase and DnaB helicase from Bacillus stearothermophilus. Biochemistry 39, 171-182. (Pubitemid 30033332)
    • (2000) Biochemistry , vol.39 , Issue.1 , pp. 171-182
    • Bird, L.E.1    Pan, H.2    Soultanas, P.3    Wigley, D.B.4
  • 20
    • 0029832926 scopus 로고    scopus 로고
    • The extreme C terminus of primase is required for interaction with DnaB at the replication fork
    • DOI 10.1074/jbc.271.35.21391
    • Tougu K, &, Marians KJ, (1996) The extreme C terminus of primase is required for interaction with DnaB at the replication fork. J Biol Chem 271, 21391-21397. (Pubitemid 26293002)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.35 , pp. 21391-21397
    • Tougu, K.1    Marians, K.J.2
  • 21
    • 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 EL, Wu CA, &, Marians KJ, (1992) 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, 4054-4063.
    • (1992) J Biol Chem , vol.267 , pp. 4054-4063
    • Zechner, E.L.1    Wu, C.A.2    Marians, K.J.3
  • 22
    • 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
    • DOI 10.1111/j.1365-2958.2008.06155.x
    • Chintakayala K, Marilynn AL, Mark AG, Steven HH, &, 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. (Pubitemid 351422958)
    • (2008) Molecular Microbiology , vol.68 , Issue.2 , pp. 360-371
    • Chintakayala, K.1    Larson, M.A.2    Griep, M.A.3    Hinrichs, S.H.4    Soultanas, P.5
  • 24
    • 0019400815 scopus 로고
    • Mechanism of dnaB protein action. II. ATP hydrolysis by dnaB protein dependent on single- or double-stranded DNA
    • Arait K, &, Kornberg A, (1981) Mechanism of dnaB Protein Action, II. ATP hydrolysis by dnaB protein dependent on single- or double-stranded DNA. J Biol Chem 256, 5253-5259. (Pubitemid 11057904)
    • (1981) Journal of Biological Chemistry , vol.256 , Issue.10 , pp. 5253-5259
    • Arai, K.1    Kornberg, A.2
  • 25
    • 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, Araig N, Kaziro Y, &, Arai K, (1984) 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 259, 88-96.
    • (1984) J Biol Chem , vol.259 , pp. 88-96
    • Nakayama, N.1    Araig, N.2    Kaziro, Y.3    Arai, K.4
  • 26
    • 0028068822 scopus 로고
    • Structure and function of Escherichia coli DnaB protein: Role of the N- terminal domain in helicase activity
    • DOI 10.1021/bi00203a028
    • Biswas SB, Chen PH, &, Biswas EE, (1994) Structure and function of Escherichia coli DnaB protein: role of the N-terminal domain in helicase activity. Biochemistry 33, 11307-11314. (Pubitemid 24304296)
    • (1994) Biochemistry , vol.33 , Issue.37 , pp. 11307-11314
    • Biswas, S.B.1    Chen, P.-H.2    Biswas, E.E.3
  • 27
    • 0033600551 scopus 로고    scopus 로고
    • Mechanism of DnaB helicase of Escherichia coli: Structural domains involved in ATP hydrolysis, DNA binding, and oligomerization
    • Biswas EE, &, Biswas SB, (1999) Mechanism of DnaB helicase of Escherichia coli: structural domains involved in ATP hydrolysis, DNA binding, and oligomerization. Biochemistry 38, 10919-10928.
    • (1999) Biochemistry , vol.38 , pp. 10919-10928
    • Biswas, E.E.1    Biswas, S.B.2
  • 28
    • 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 EE, &, Biswas SB, (1999) Mechanism of DNA binding by the DnaB helicase of Escherichia coli: analysis of the roles of domain gamma in DNA binding. Biochemistry 38, 10929-10939.
    • (1999) Biochemistry , vol.38 , pp. 10929-10939
    • Biswas, E.E.1    Biswas, S.B.2
  • 29
    • 58149495961 scopus 로고    scopus 로고
    • An essential DnaB helicase of Bacillus anthracis: Identification, characterization, and mechanism of action
    • Biswas EE, Barnes MH, Moir DT, &, Biswas SB, (2009) An essential DnaB helicase of Bacillus anthracis: identification, characterization, and mechanism of action. J Bacteriol 191, 249-260.
    • (2009) J Bacteriol , vol.191 , pp. 249-260
    • Biswas, E.E.1    Barnes, M.H.2    Moir, D.T.3    Biswas, S.B.4
  • 30
    • 0027373139 scopus 로고
    • Interactions of bacteriophage T7 DNA primase/helicase protein with single- stranded and double-stranded DNAs
    • DOI 10.1021/bi00097a028
    • Hingorani MM, &, Patel SS, (1993) Interactions of bacteriophage T7 DNA primase/helicase protein with single-stranded and double-stranded DNAs. Biochemistry 32, 12478-12487. (Pubitemid 23357971)
    • (1993) Biochemistry , vol.32 , Issue.46 , pp. 12478-12487
    • Hingorani, M.M.1    Patel, S.S.2
  • 31
    • 0036607462 scopus 로고    scopus 로고
    • Bacillus subtilis bacteriophage SPP1 hexameric DNA helicase, G40P, interacts with forked DNA
    • Ayora S, Weise F, Mesa P, Stasiak A, &, Alonso JC, (2002) Bacillus subtilis bacteriophage SPP1 hexameric DNA helicase, G40P, interacts with forked DNA. Nucleic Acids Res 30, 2280-2289. (Pubitemid 34624562)
    • (2002) Nucleic Acids Research , vol.30 , Issue.11 , pp. 2280-2289
    • Ayora, S.1    Weise, F.2    Mesa, P.3    Stasiak, A.4    Alonso, J.C.5
  • 32
    • 0345531091 scopus 로고    scopus 로고
    • Functional characterization of Helicobacter pylori DnaB helicase
    • DOI 10.1093/nar/gkg895
    • Soni RK, Mehra P, Choudhury NR, Mukhopadhyay G, &, Dhar SK, (2003) Functional characterization of Helicobacter pylori DnaB helicase. Nucleic Acids Res 31, 6828-6840. (Pubitemid 37508790)
    • (2003) Nucleic Acids Research , vol.31 , Issue.23 , pp. 6828-6840
    • Soni, R.K.1    Mehra, P.2    Choudhury, N.R.3    Mukhopadhyay, G.4    Dhar, S.K.5
  • 33
    • 34250632433 scopus 로고    scopus 로고
    • The domain structure of Helicobacter pylori DnaB helicase: The N-terminal domain can be dispensable for helicase activity whereas the extreme C-terminal region is essential for its function
    • DOI 10.1093/nar/gkm167
    • Nitharwal RG, Paul S, Dar A, Chaudhuri NR, Soni RK, Prusty D, Sinha S, Kashav T, Mukhopadhyay G, Chaudhuri T, et al. (2007) The domain structure of Helicobacter pylori DnaB helicase: the N-terminal domain can be dispensable for helicase activity whereas the extreme C-terminal region is essential for its function. Nucleic Acids Res 35, 2861-2874. (Pubitemid 47073625)
    • (2007) Nucleic Acids Research , vol.35 , Issue.9 , pp. 2861-2874
    • Nitharwal, R.G.1    Paul, S.2    Dar, A.3    Choudhury, N.R.4    Soni, R.K.5    Prusty, D.6    Sinha, S.7    Kashav, T.8    Mukhopadhyay, G.9    Chaudhuri, T.K.10    Gourinath, S.11    Dhar, S.K.12
  • 34
    • 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
    • DOI 10.1074/jbc.273.17.10515
    • Jezewska MJ, Rajendran S, Bujalowska D, &, Bujalowski W, (1998) Does single-stranded DNA pass through the inner channel of the protein hexamer in the complex with the Escherichia coli. Biochemistry 273, 10515-10529. (Pubitemid 28227662)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.17 , pp. 10515-10529
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowska, D.3    Bujalowski, W.4
  • 35
    • 4143151757 scopus 로고    scopus 로고
    • Twin DNA pumps of a hexameric helicase provide power to simultaneously melt two duplexes
    • DOI 10.1016/j.molcel.2004.06.039, PII S1097276504003995
    • Kaplan DL, &, O'Donnell M, (2004) Twin DNA pumps of a hexameric helicase provide power to simultaneously melt two duplexes. Mol Cell 15, 453-465. (Pubitemid 39092760)
    • (2004) Molecular Cell , vol.15 , Issue.3 , pp. 453-465
    • Kaplan, D.L.1    O'Donnell, M.2
  • 36
    • 0033812649 scopus 로고    scopus 로고
    • The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli
    • Seitz H, Weigel C, &, Messer W, (2000) The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli. Mol Microbiol 37, 1270-1279.
    • (2000) Mol Microbiol , vol.37 , pp. 1270-1279
    • Seitz, H.1    Weigel, C.2    Messer, W.3
  • 37
    • 0037222240 scopus 로고    scopus 로고
    • Strategies for helicase recruitment and loading in bacteria
    • DOI 10.1038/sj.embor.embor703
    • Konieczny I, (2003) Strategies for helicase recruitment and loading in bacteria. EMBO J 4, 37-41. (Pubitemid 36305375)
    • (2003) EMBO Reports , vol.4 , Issue.1 , pp. 37-41
    • Konieczny, I.1
  • 38
    • 0036843139 scopus 로고    scopus 로고
    • The bacterial replication initiator DnaA. DnaA and oriC, the bacterial mode to initiate DNA replication
    • DOI 10.1016/S0168-6445(02)00127-4, PII S0168644502001274
    • Messer W, (2002) The bacterial replication initiator DnaA and oriC, the bacterial mode to initiate DNA replication. FEMS Microbiol Rev 26, 355-374. (Pubitemid 35284468)
    • (2002) FEMS Microbiology Reviews , vol.26 , Issue.4 , pp. 355-374
    • Messer, W.1
  • 39
    • 29744452137 scopus 로고    scopus 로고
    • Regulatory network of the initiation of chromosomal replication in Escherichia coli
    • DOI 10.1080/10409230500366090
    • Kato J, (2005) Regulatory network of the initiation of chromosomal replication in Escherichia coli. Crit Rev Biochem Mol Biol 40, 331-342. (Pubitemid 43030918)
    • (2005) Critical Reviews in Biochemistry and Molecular Biology , vol.40 , Issue.6 , pp. 331-342
    • Kato, J.-I.1
  • 40
    • 33750312968 scopus 로고    scopus 로고
    • DnaA: Controlling the initiation of bacterial DNA replication and more
    • Kaguni JM, (2006) DnaA: controlling the initiation of bacterial DNA replication and more. Annu Rev Microbiol 60, 351-375.
    • (2006) Annu Rev Microbiol , vol.60 , pp. 351-375
    • Kaguni, J.M.1
  • 41
    • 67349097766 scopus 로고    scopus 로고
    • Dynamics of the ssDNA recognition by the RepA hexameric helicase of plasmid RSF1010: Analyses using fluorescence stopped-flow intensity and anisotropy methods
    • Andreeva IE, Szymanski MR, Jezewska MJ, Galletto R, &, Bujalowski W, (2009) Dynamics of the ssDNA recognition by the RepA hexameric helicase of plasmid RSF1010: analyses using fluorescence stopped-flow intensity and anisotropy methods. J Mol Biol 388, 751-775.
    • (2009) J Mol Biol , vol.388 , pp. 751-775
    • Andreeva, I.E.1    Szymanski, M.R.2    Jezewska, M.J.3    Galletto, R.4    Bujalowski, W.5
  • 42
    • 0034723155 scopus 로고    scopus 로고
    • Kinetic mechanism of the single-stranded DNA recognition by Escherichia coli replicative helicase dnab protein. application of the matrix projection operator technique to analyze stopped-flow kinetics
    • Bujalowski W, &, Jezewska MJ, (2000) Kinetic mechanism of the single-stranded DNA recognition by Escherichia coli replicative helicase dnab protein. application of the matrix projection operator technique to analyze stopped-flow kinetics. J Mol Biol 295, 831-852.
    • (2000) J Mol Biol , vol.295 , pp. 831-852
    • Bujalowski, W.1    Jezewska, M.J.2
  • 43
    • 0032502678 scopus 로고    scopus 로고
    • Functional and structural heterogeneity of the DNA binding site of the Escherichia coli primary replicative helicase DnaB protein
    • DOI 10.1074/jbc.273.15.9058
    • Jezewska MJ, Rajendran S, &, Bujalowski W, (1998) Functional and structural heterogeneity of the DNA binding site of the Escherichia coli primary replicative helicase DnaB protein. J Biol Chem 273, 9058-9069. (Pubitemid 28176194)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.15 , pp. 9058-9069
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 44
    • 0029072199 scopus 로고
    • Interactions of Escherichia coli primary replicative helicase DnaB protein with single-stranded DNA. The nucleic acid does not wrap around the protein hexamer
    • Bujalowski W, &, Jezewska MJ, (1995) Interactions of Escherichia coli primary replicative helicase DnaB protein with single-stranded DNA. The nucleic acid does not wrap around the protein hexamer. Biochemistry 34, 8513-8519.
    • (1995) Biochemistry , vol.34 , pp. 8513-8519
    • Bujalowski, W.1    Jezewska, M.J.2
  • 45
    • 78650871483 scopus 로고    scopus 로고
    • Helicobacter pylori chromosomal DNA replication: Current status and future perspectives
    • Nitharwal RG, Verma V, Dasgupta S, &, Dhar SK, (2011) Helicobacter pylori chromosomal DNA replication: current status and future perspectives. FEBS Lett 585, 7-17.
    • (2011) FEBS Lett , vol.585 , pp. 7-17
    • Nitharwal, R.G.1    Verma, V.2    Dasgupta, S.3    Dhar, S.K.4
  • 47
    • 75849129293 scopus 로고    scopus 로고
    • The structure of a DnaA/HobA complex from Helicobacter pylori provides insight into regulation of DNA replication in bacteria
    • Natrajan G, Noirot-gros MF, Zawilak-pawlik A, Kapp U, &, Terradot L, (2009) The structure of a DnaA/HobA complex from Helicobacter pylori provides insight into regulation of DNA replication in bacteria. Proc Natl Acad Sci USA 106, 1-6.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 1-6
    • Natrajan, G.1    Noirot-Gros, M.F.2    Zawilak-Pawlik, A.3    Kapp, U.4    Terradot, L.5
  • 48
    • 22544460494 scopus 로고    scopus 로고
    • Helicobacter pylori DnaB helicase can bypass Escherichia coli DnaC function in vivo
    • DOI 10.1042/BJ20050062
    • Soni RK, Mehra P, Mukhopadhyay G, &, Dhar SK, (2005) Helicobacter pylori DnaB helicase can bypass Escherichia coli DnaC function in vivo. Biochem J 548, 541-548. (Pubitemid 41021157)
    • (2005) Biochemical Journal , vol.389 , Issue.2 , pp. 541-548
    • Soni, R.K.1    Mehra, P.2    Mukhopadhyay, G.3    Kumar Dhar, S.4
  • 49
    • 0028046581 scopus 로고
    • Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein
    • Bujalowski W, Klonowska MM, &, Jezewska MJ, (1994) Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein. J Biol Chem 269, 31350-31358. (Pubitemid 24379486)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.50 , pp. 31350-31358
    • Bujalowski, W.1    Klonowska, M.M.2    Jezewska, M.J.3
  • 50
    • 0030064012 scopus 로고    scopus 로고
    • Global conformational transitions in Escherichia coli primary replicative helicase DnaB protein induced by ATP, ADP, and single-stranded DNA binding
    • Jezewska MJ, &, Bujalowski W, (1996) Global conformational transitions in Escherichia coli primary replicative helicase DnaB protein induced by ATP, ADP, and single-stranded DNA binding. J Biol Chem 271, 4261-4265.
    • (1996) J Biol Chem , vol.271 , pp. 4261-4265
    • Jezewska, M.J.1    Bujalowski, W.2
  • 51
    • 70449570532 scopus 로고    scopus 로고
    • Three-dimensional structure of N-terminal domain of DnaB helicase and helicase-primase interactions in Helicobacter pylori
    • doi.
    • Kashav T, Nitharwal R, Abdulrehman SA, Gabdoulkhakov A, Saenger W, Dhar SK, &, Gourinath S, (2009) Three-dimensional structure of N-terminal domain of DnaB helicase and helicase-primase interactions in Helicobacter pylori. PLoS ONE 4, e7515. doi:.
    • (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
  • 52
    • 0032478286 scopus 로고    scopus 로고
    • Complex of Escherichia coli primary replicative helicase DnaB protein with a replication fork: Recognition and structure
    • DOI 10.1021/bi972564u
    • Jezewska MJ, Rajendran S, &, Bujalowski W, (1998) Complex of Escherichia coli primary replicative helicase DnaB protein with a replication fork: recognition and structure. Biochemistry 37, 3116-3136. (Pubitemid 28145766)
    • (1998) Biochemistry , vol.37 , Issue.9 , pp. 3116-3136
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 53
    • 0034600838 scopus 로고    scopus 로고
    • A ring-opening mechanism for DNA binding in the central channel of the T7 helicase-primase protein
    • Ahnert P, Picha KM, &, Patel SS, (2000) A ring-opening mechanism for DNA binding in the central channel of the T7 helicase-primase protein. EMBO J 19, 3418-3427. (Pubitemid 30428219)
    • (2000) EMBO Journal , vol.19 , Issue.13 , pp. 3418-3427
    • Ahnert, P.1    Picha, K.M.2    Patel, S.S.3
  • 56
    • 31844453991 scopus 로고    scopus 로고
    • DNA primase acts as a molecular brake in DNA replication
    • DOI 10.1038/nature04317, PII NATURE04317
    • Lee JB, Hite RK, Hamdan SK, Xie XS, Richardson CC, &, van Oijen AM, (2006) DNA primase acts as a molecular brake in DNA replication. Nature 439, 621-624. (Pubitemid 43185389)
    • (2006) Nature , vol.439 , Issue.7076 , pp. 621-624
    • Lee, J.-B.1    Hite, R.K.2    Hamdan, S.M.3    Xie, X.S.4    Richardson, C.C.5    Van Oijen, A.M.6
  • 57
    • 0023684064 scopus 로고
    • A general method of in vitro preparation and specific mutagenesis of DNA fragments: Study of protein and DNA interactions
    • Higuchi R, Krummel B, &, Saiki RK, (1988) A general method of in vitro preparation and specific mutagenesis of DNA fragments: study of protein and DNA interactions. Nucleic Acids Res 16, 7351-7367.
    • (1988) Nucleic Acids Res , vol.16 , pp. 7351-7367
    • Higuchi, R.1    Krummel, B.2    Saiki, R.K.3
  • 58
    • 35948988110 scopus 로고    scopus 로고
    • A critical role for the C-terminus of Nej1 protein in Lif1p association, DNA binding and non-homologous end-joining
    • DOI 10.1016/j.dnarep.2007.07.009, PII S1568786407002571
    • Sulek M, Yarrington R, McGibbon G, Boeke JD, &, Junop M, (2007) A critical role for the C-terminus of Nej1 protein in Lif1p association, DNA binding and non-homologous end-joining. DNA Repair 6, 1805-1818. (Pubitemid 350064586)
    • (2007) DNA Repair , vol.6 , Issue.12 , pp. 1805-1818
    • Sulek, M.1    Yarrington, R.2    McGibbon, G.3    Boeke, J.D.4    Junop, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.