메뉴 건너뛰기




Volumn 48, Issue 31, 2009, Pages 7373-7382

Mechanisms of DNA binding and regulation of Bacillus anthracis DNA primase

Author keywords

[No Author keywords available]

Indexed keywords

ANTHRACIS; BACILLUS ANTHRACIS; DNA BINDING; DNA HELICASE; DNA REPLICATIONS; DNA-BINDING PROTEIN; DNAB HELICASE; DNAB PROTEIN; E. COLI; HELICASES; MECHANISM OF ACTION; RECOMBINANT DNA; RNA PRIMERS; SINGLE-STRANDED DNA (SS-DNA);

EID: 68249117713     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900086z     Document Type: Article
Times cited : (5)

References (43)
  • 2
    • 0032416608 scopus 로고    scopus 로고
    • Initiation of DNA replication in eukaryotic chromosomes
    • DePamphilis, M. L. (1998) Initiation of DNA replication in eukaryotic chromosomes. J. Cell. Biochem. Suppl. 30-31, 8-17.
    • (1998) J. Cell. Biochem. Suppl. , vol.30-31 , pp. 8-17
    • DePamphilis, M.L.1
  • 3
    • 0033524411 scopus 로고    scopus 로고
    • Mechanism of recruitment of DnaB helicase to the replication origin of the plasmid pSC101
    • Datta, H. J., Khatri, G. S., and Bastia, D. (1999) Mechanism of recruitment of DnaB helicase to the replication origin of the plasmid pSC101. Proc. Natl. Acad. Sci. U.S.A. 96, 73-78.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 73-78
    • Datta, H.J.1    Khatri, G.S.2    Bastia, D.3
  • 4
    • 0024284091 scopus 로고
    • Duplex opening by dnaA protein at novel sequences in initiation of replication at the origin of the E. coli chromosome
    • Bramhill, D., and Kornberg, A. (1988) Duplex opening by dnaA protein at novel sequences in initiation of replication at the origin of the E. coli chromosome. Cell 52, 743-755.
    • (1988) Cell , vol.52 , pp. 743-755
    • Bramhill, D.1    Kornberg, A.2
  • 5
    • 0023766613 scopus 로고
    • A model for initiation at origins of DNA replication
    • DOI 10.1016/0092-8674(88)90102-X
    • Bramhill, D., and Kornberg, A. (1988) A model for initiation at origins of DNA replication. Cell 54, 915-918. (Pubitemid 18229429)
    • (1988) Cell , vol.54 , Issue.7 , pp. 915-918
    • Bramhill, D.1    Kornberg, A.2
  • 6
    • 0020842897 scopus 로고
    • Purified dnaA protein in initiation of replication at the Escherichia coli chromosomal origin of replication
    • Fuller, R. S., and Kornberg, A. (1983) Purified dnaA protein in initiation of replication at the Escherichia coli chromosomal origin of replication. Proc. Natl. Acad. Sci. U.S.A. 80, 5817-5821.
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 5817-5821
    • Fuller, R.S.1    Kornberg, A.2
  • 7
    • 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., and Bishop, J. E. (1986) The dnaB protein of Escherichia coli: Mechanism of nucleotide binding, hydrolysis, and modulation by dnaC protein. Biochemistry 25, 7368-7374.
    • (1986) Biochemistry , vol.25 , pp. 7368-7374
    • Biswas, E.E.1    Biswas, S.B.2    Bishop, J.E.3
  • 8
    • 0023644941 scopus 로고
    • Regulation of dnaB function in DNA replication in Escherichia coli by dnaC and lambda P gene products
    • Biswas, S. B., and Biswas, E. E. (1987) Regulation of dnaB function in DNA replication in Escherichia coli by dnaC and lambda P gene products. J. Biol. Chem. 262, 7831-7838.
    • (1987) J. Biol. Chem. , vol.262 , pp. 7831-7838
    • Biswas, S.B.1    Biswas, E.E.2
  • 9
    • 0000579776 scopus 로고
    • Interaction of Escherichia coli dnaB and dnaC(D) gene products in vitro
    • Wickner, S., and Hurwitz, J. (1975) Interaction of Escherichia coli dnaB and dnaC(D) gene products in vitro. Proc. Natl. Acad. Sci. U.S.A. 72, 921-925.
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 921-925
    • Wickner, S.1    Hurwitz, J.2
  • 10
    • 33749008780 scopus 로고    scopus 로고
    • Quantitative analysis of binding of single-stranded DNA by Escherichia coli DnaB helicase and the DnaB 3 DnaC complex
    • Biswas, S. B., and Biswas-Fiss, E. E. (2006) Quantitative analysis of binding of single-stranded DNA by Escherichia coli DnaB helicase and the DnaB 3 DnaC complex. Biochemistry 45, 11505-11513.
    • (2006) Biochemistry , vol.45 , pp. 11505-11513
    • Biswas, S.B.1    Biswas-Fiss, E.E.2
  • 11
    • 0023425204 scopus 로고
    • DnaA protein is required for replication of the minimal replicon of the broad-hostrange plasmid RK2 in Escherichia coli
    • Gaylo, P. J., Turjman, N., and Bastia, D. (1987) DnaA protein is required for replication of the minimal replicon of the broad-hostrange plasmid RK2 in Escherichia coli. J. Bacteriol. 169, 4703-4709.
    • (1987) J. Bacteriol. , vol.169 , pp. 4703-4709
    • Gaylo, P.J.1    Turjman, N.2    Bastia, D.3
  • 12
    • 0031467674 scopus 로고    scopus 로고
    • Helicase delivery and activation by DnaA and TrfA proteins during the initiation of replication of the broad host range plasmid RK2
    • Konieczny, I., and Helinski, D. R. (1997) Helicase delivery and activation by DnaA and TrfA proteins during the initiation of replication of the broad host range plasmid RK2. J. Biol. Chem. 272, 33312-33318.
    • (1997) J. Biol. Chem. , vol.272 , pp. 33312-33318
    • Konieczny, I.1    Helinski, D.R.2
  • 13
    • 0242664945 scopus 로고    scopus 로고
    • A specific region in the N terminus of a replication initiation protein of plasmid RK2 is required for recruitment of Pseudomonas aeruginosa DnaB helicase to the plasmid origin
    • Zhong, Z., Helinski, D., and Toukdarian, A. (2003) A specific region in the N terminus of a replication initiation protein of plasmid RK2 is required for recruitment of Pseudomonas aeruginosa DnaB helicase to the plasmid origin. J. Biol. Chem. 278, 45305-45310.
    • (2003) J. Biol. Chem. , vol.278 , pp. 45305-45310
    • Zhong, Z.1    Helinski, D.2    Toukdarian, A.3
  • 14
    • 0024978379 scopus 로고
    • Ordered assembly of nucleoprotein structures at the bacteriophage lambda replication origin during the initiation of DNA replication
    • Alfano, C., and McMacken, R. (1989) Ordered assembly of nucleoprotein structures at the bacteriophage lambda replication origin during the initiation of DNA replication. J. Biol. Chem. 264, 10699-10708.
    • (1989) J. Biol. Chem. , vol.264 , pp. 10699-10708
    • Alfano, C.1    McMacken, R.2
  • 15
    • 0022351547 scopus 로고
    • Specialized nucleoprotein structures at the origin of replication of bacteriophage lambda: Complexes with lambda O protein and with lambda O, lambda P, and Escherichia coli DnaB proteins
    • Dodson, M., Roberts, J., McMacken, R., and Echols, H. (1985) Specialized nucleoprotein structures at the origin of replication of bacteriophage lambda: Complexes with lambda O protein and with lambda O, lambda P, and Escherichia coli DnaB proteins. Proc. Natl. Acad. Sci. U.S.A. 82, 4678-4682.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 4678-4682
    • Dodson, M.1    Roberts, J.2    McMacken, R.3    Echols, H.4
  • 16
    • 0024297218 scopus 로고
    • The role of template superhelicity in the initiation of bacteriophage lambda DNA replication
    • Alfano, C., and McMacken, R. (1988) The role of template superhelicity in the initiation of bacteriophage lambda DNA replication. Nucleic Acids Res. 16, 9611-9630.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 9611-9630
    • Alfano, C.1    McMacken, R.2
  • 17
    • 0023038675 scopus 로고
    • Specialized nucleoprotein structures at the origin of replication of bacteriophage lambda: Localized unwinding of duplex DNA by a sixprotein reaction
    • Dodson, M., Echols, H., Wickner, S., Alfano, C., Mensa-Wilmot, K., Gomes, B., LeBowitz, J., Roberts, J. D., and McMacken, R. (1986) Specialized nucleoprotein structures at the origin of replication of bacteriophage lambda: Localized unwinding of duplex DNA by a sixprotein reaction. Proc. Natl. Acad. Sci. U.S.A. 83, 7638-7642.
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 7638-7642
    • Dodson, M.1    Echols, H.2    Wickner, S.3    Alfano, C.4    Mensa-Wilmot, K.5    Gomes, B.6    LeBowitz, J.7    Roberts, J.D.8    McMacken, R.9
  • 18
    • 0038931706 scopus 로고
    • A general priming system employing only dnaB protein and primase for DNA replication
    • Arai, K., and Kornberg, A. (1979) A general priming system employing only dnaB protein and primase for DNA replication. Proc. Natl. Acad. Sci. U.S.A. 76, 4308-4312.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4308-4312
    • Arai, K.1    Kornberg, A.2
  • 19
    • 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., and Biswas, S. B. (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.
    • (2003) J. Biol. Chem. , vol.278 , pp. 52253-52261
    • Mitkova, A.V.1    Khopde, S.M.2    Biswas, S.B.3
  • 21
    • 0021100251 scopus 로고
    • Complexes of Escherichia coli primase with the replication origin of G4 phage DNA
    • Stayton, M. M., and Kornberg, A. (1983) Complexes of Escherichia coli primase with the replication origin of G4 phage DNA. J. Biol. Chem. 258, 13205-13212.
    • (1983) J. Biol. Chem. , vol.258 , pp. 13205-13212
    • Stayton, M.M.1    Kornberg, A.2
  • 22
    • 0015366533 scopus 로고
    • RNA-linked nascent DNA fragments in Escherichia coli
    • Sugino, A., Hirose, S., and Okazaki, R. (1972) RNA-linked nascent DNA fragments in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 69, 1863-1867.
    • (1972) Proc. Natl. Acad. Sci. U.S.A. , vol.69 , pp. 1863-1867
    • Sugino, A.1    Hirose, S.2    Okazaki, R.3
  • 23
    • 0019405284 scopus 로고
    • Movement and site selection for priming by the primosome in phage phi X174 DNA replication
    • Arai, K., Low, R. L., and Kornberg, A. (1981) Movement and site selection for priming by the primosome in phage phi X174 DNA replication. Proc. Natl. Acad. Sci. U.S.A. 78, 707-711.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 707-711
    • Arai, K.1    Low, R.L.2    Kornberg, A.3
  • 24
    • 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., Mohanty, B. K., and Bastia, D. (1996) Direct physical interaction between DnaG primase and DnaB helicase of Escherichia coli is necessary for optimal synthesis of primer RNA. Proc. Natl. Acad. Sci. U.S.A. 93, 12902-12907.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 12902-12907
    • Lu, Y.B.1    Ratnakar, P.V.2    Mohanty, B.K.3    Bastia, D.4
  • 25
    • 0025782760 scopus 로고
    • Specificity of recognition sequence for Escherichia coli primase
    • Yoda, K., and Okazaki, T. (1991) Specificity of recognition sequence for Escherichia coli primase. Mol. Gen. Genet. 227, 1-8.
    • (1991) Mol. Gen. Genet. , vol.227 , pp. 1-8
    • Yoda, K.1    Okazaki, T.2
  • 26
    • 0023733709 scopus 로고
    • RNA-primed initiation sites of DNA replication in the origin region of bacteriophage lambda genome
    • Yoda, K., Yasuda, H., Jiang, X. W., and Okazaki, T. (1988) RNAprimed initiation sites of DNA replication in the origin region of bacteriophage lambda genome. Nucleic Acids Res. 16, 6531-6546. (Pubitemid 18182944)
    • (1988) Nucleic Acids Research , vol.16 , Issue.14 A , pp. 6531-6546
    • Yoda, K.1    Yasuda, H.2    Jiang, X.-W.3    Okazaki, T.4
  • 27
    • 0028267688 scopus 로고
    • Multiple-antibiotic-resistant pathogenic bacteria. A report on the Rockefeller University Workshop
    • Tomasz, A. (1994) Multiple-antibiotic-resistant pathogenic bacteria. A report on the Rockefeller University Workshop. N. Engl. J. Med. 330, 1247-1251.
    • (1994) N. Engl. J. Med. , vol.330 , pp. 1247-1251
    • Tomasz, A.1
  • 30
    • 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
  • 31
    • 44249097571 scopus 로고    scopus 로고
    • Staphylococcus aureus primase has higher initiation specificity, interacts with single-stranded DNA stronger, but is less stimulated by its helicase than 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 helicase 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
  • 32
    • 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, 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. (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
  • 33
    • 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, W. K., and Steitz, T. A. (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
  • 34
    • 0033600561 scopus 로고    scopus 로고
    • Mechanism of DNA binding by the DnaB helicase of Escherichia coli: Analysis of the roles of domain γ in DNA binding
    • DOI 10.1021/bi990049l
    • Biswas, E. E., and Biswas, S. B. (1999) Mechanism ofDNAbinding by the DnaB helicase of Escherichia coli: Analysis of the roles of domain γ in DNA binding. Biochemistry 38, 10929-10939. (Pubitemid 29411583)
    • (1999) Biochemistry , vol.38 , Issue.34 , pp. 10929-10939
    • Biswas, E.E.1    Biswas, S.B.2
  • 36
    • 12344314307 scopus 로고    scopus 로고
    • A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon
    • DOI 10.1016/j.molcel.2004.11.051, PII S1097276504007737
    • Maag, D., Fekete, C. A., Gryczynski, Z., and Lorsch, J. R. (2005) A conformational change in the eukaryotic translation preinitiation complex and release of eIF1 signal recognition of the start codon. Mol. Cell 17, 265-275. (Pubitemid 40138620)
    • (2005) Molecular Cell , vol.17 , Issue.2 , pp. 265-275
    • Maag, D.1    Fekete, C.A.2    Gryczynski, Z.3    Lorsch, J.R.4
  • 37
    • 46749083458 scopus 로고    scopus 로고
    • Binding of 8-anilino-1-naphthalenesulfonate to lecithin:cholesterol acyltransferase studied by fluorescence techniques
    • Sarkar, P., Bharill, S., Gryczynski, I., Gryczynski, Z., Nair, M. P., and Lacko, A. G. (2008) Binding of 8-anilino-1-naphthalenesulfonate to lecithin:cholesterol acyltransferase studied by fluorescence techniques. J. Photochem. Photobiol., B 92, 19-23.
    • (2008) J. Photochem. Photobiol., B , vol.92 , pp. 19-23
    • Sarkar, P.1    Bharill, S.2    Gryczynski, I.3    Gryczynski, Z.4    Nair, M.P.5    Lacko, A.G.6
  • 39
    • 0037126718 scopus 로고    scopus 로고
    • Affinity and sequence specificity of DNA binding and site selection for primer synthesis by Escherichia coli primase
    • DOI 10.1021/bi026711m
    • Khopde, S., Biswas, E., and Biswas, S. (2002) Affinity and sequence specificity of DNA binding and site selection for primer synthesis by Escherichia coli primase. Biochemistry 41, 14820-14830. (Pubitemid 35470660)
    • (2002) Biochemistry , vol.41 , Issue.50 , pp. 14820-14830
    • Khopde, S.1    Biswas, E.E.2    Biswas, S.B.3
  • 40
    • 0025100292 scopus 로고
    • The ABC-primosome. A novel priming system employing dnaA, dnaB, dnaC, and primase on a hairpin containing a dnaA box sequence
    • Masai, H., Nomura, N., and Arai, K. (1990) The ABC-primosome. A novel priming system employing dnaA, dnaB, dnaC, and primase on a hairpin containing a dnaA box sequence. J. Biol. Chem. 265, 15134-15144.
    • (1990) J. Biol. Chem. , vol.265 , pp. 15134-15144
    • Masai, H.1    Nomura, N.2    Arai, K.3
  • 41
    • 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. (1996) The extreme C terminus of primase is required for interaction with DnaB at the replication fork. J. Biol. Chem. 271, 21391-21397.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21391-21397
    • Tougu, K.1    Marians, K.J.2
  • 42
    • 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. (1994) Identification of a domain of Escherichia coli primase required for functional interaction with the DnaB helicase at the replication fork. J. Biol. Chem. 269, 4675-4682.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4675-4682
    • Tougu, K.1    Peng, H.2    Marians, K.J.3
  • 43
    • 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., and 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    Arai, N.2    Kaziro, Y.3    Arai, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.