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Volumn 185, Issue 22, 2003, Pages 6633-6639

Purification and Characterization of the PcrA Helicase of Bacillus anthracis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; HELICASE; PCRA HELICASE; UNCLASSIFIED DRUG;

EID: 0242407470     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.185.22.6633-6639.2003     Document Type: Article
Times cited : (28)

References (38)
  • 4
    • 0033958431 scopus 로고    scopus 로고
    • UvrD-dependent replication of rolling-circle plasmids in Escherichia coli
    • Bruand, C., and S. D. Ehrlich. 2000. UvrD-dependent replication of rolling-circle plasmids in Escherichia coli. Mol. Microbiol. 35:204-210.
    • (2000) Mol. Microbiol. , vol.35 , pp. 204-210
    • Bruand, C.1    Ehrlich, S.D.2
  • 5
    • 0034666303 scopus 로고    scopus 로고
    • The DNA replication machine of a gram-positive organism
    • Bruck, I., and M. O'Donnell. 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
  • 6
    • 0035977018 scopus 로고    scopus 로고
    • Stoichiometry of DnaA and DnaB protein in initiation at the Escherichia coli chromosomal origin
    • Carr, K. M., and J. M. Kaguni. 2001. Stoichiometry of DnaA and DnaB protein in initiation at the Escherichia coli chromosomal origin. J. Biol. Chem. 276:44919-44925.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44919-44925
    • Carr, K.M.1    Kaguni, J.M.2
  • 7
    • 0037195801 scopus 로고    scopus 로고
    • Biochemical characterization of the Staphylococcus aureus PcrA helicase and its role in plasmid rolling-circle replication
    • Chang, T.-L, A. Naqvi, S. P. Anand, M. G. Kramer, R. Munshi, and S. A, Khan. 2002. Biochemical characterization of the Staphylococcus aureus PcrA helicase and its role in plasmid rolling-circle replication. J. Biol. Chem. 277:45880-45886.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45880-45886
    • Chang, T.-L.1    Naqvi, A.2    Anand, S.P.3    Kramer, M.G.4    Munshi, R.5    Khan, S.A.6
  • 8
    • 0035816217 scopus 로고    scopus 로고
    • E. coli Rep oligomers are required to initiate DNA unwinding in vitro
    • Cheng, W., J. Hsieh, K. M. Brendza, and T. M. Lohman. 2001. E. coli Rep oligomers are required to initiate DNA unwinding in vitro. J. Mol. Biol. 310:327-350.
    • (2001) J. Mol. Biol. , vol.310 , pp. 327-350
    • Cheng, W.1    Hsieh, J.2    Brendza, K.M.3    Lohman, T.M.4
  • 9
    • 0037294467 scopus 로고    scopus 로고
    • Helicase mechanisms and coupling of helicases within macromolecular machines. Part II: Integration of helicases into cellular processes
    • Delagoutte, E., and P. H. von Hippel. 2003. Helicase mechanisms and coupling of helicases within macromolecular machines. Part II: integration of helicases into cellular processes. Q. Rev. Biophys. 36:1-69.
    • (2003) Q. Rev. Biophys. , vol.36 , pp. 1-69
    • Delagoutte, E.1    Von Hippel, P.H.2
  • 11
    • 0034635172 scopus 로고    scopus 로고
    • Demonstration of single-stranded DNA translocation by PcrA helicase: Measurement of step size and translocation speed
    • Dillingham, M. S., D. B. Wigley, and M. R. Webb. 2000. Demonstration of single-stranded DNA translocation by PcrA helicase: measurement of step size and translocation speed. Biochemistry 39:205-212.
    • (2000) Biochemistry , vol.39 , pp. 205-212
    • Dillingham, M.S.1    Wigley, D.B.2    Webb, M.R.3
  • 12
    • 0033428970 scopus 로고    scopus 로고
    • Helicase motifs: The engine that powers DNA unwinding
    • Hall, M. C., and S. W. Matson. 1999. Helicase motifs: the engine that powers DNA unwinding. Mol. Microbiol. 34:867-877.
    • (1999) Mol. Microbiol. , vol.34 , pp. 867-877
    • Hall, M.C.1    Matson, S.W.2
  • 13
    • 0030796341 scopus 로고    scopus 로고
    • Anthrax pathogenesis and host response
    • Hanna, P. 1998. Anthrax pathogenesis and host response. Curr. Top. Microbiol. Immunol. 225:13-35.
    • (1998) Curr. Top. Microbiol. Immunol. , vol.225 , pp. 13-35
    • Hanna, P.1
  • 14
    • 0027507727 scopus 로고
    • Characterization of the Staphylococcus aureus chromosomal gene pcrA, identified by mutations affecting plasmid pT181 replication
    • Iordanescu, S. 1993. Characterization of the Staphylococcus aureus chromosomal gene pcrA, identified by mutations affecting plasmid pT181 replication. Mol. Gen. Genet. 241:185-192.
    • (1993) Mol. Gen. Genet. , vol.241 , pp. 185-192
    • Iordanescu, S.1
  • 15
    • 0027154579 scopus 로고
    • Plasmid pT181-linked suppressors of the Staphylococcus aureus pcrA3 chromosomal mutation
    • Iordanescu, S. 1993. Plasmid pT181-linked suppressors of the Staphylococcus aureus pcrA3 chromosomal mutation. J. Bacteriol. 175:3916-3917.
    • (1993) J. Bacteriol. , vol.175 , pp. 3916-3917
    • Iordanescu, S.1
  • 16
    • 0030837968 scopus 로고    scopus 로고
    • Why is the initiation site of an AT-rich rolling circle plasmid at the tip of a GC-rich cruciform?
    • Jin, R., M.-E. Fernandez-Beros, and R. P. Novick. 1997. Why is the initiation site of an AT-rich rolling circle plasmid at the tip of a GC-rich cruciform? EMBO J. 16:4456-4466.
    • (1997) EMBO J. , vol.16 , pp. 4456-4466
    • Jin, R.1    Fernandez-Beros, M.-E.2    Novick, R.P.3
  • 17
    • 0034776111 scopus 로고    scopus 로고
    • Role of the double-strand origin cruciform in pT181 replication
    • Jin, R., and R. P. Novick. 2001. Role of the double-strand origin cruciform in pT181 replication. Plasmid 46:95-105.
    • (2001) Plasmid , vol.46 , pp. 95-105
    • Jin, R.1    Novick, R.P.2
  • 18
    • 0031440479 scopus 로고    scopus 로고
    • Rolling-circle replication of bacterial plasmids
    • Khan, S. A. 1997. Rolling-circle replication of bacterial plasmids. Microbiol. Mol. Biol. Rev. 61:442-455.
    • (1997) Microbiol. Mol. Biol. Rev. , vol.61 , pp. 442-455
    • Khan, S.A.1
  • 19
    • 0033868154 scopus 로고    scopus 로고
    • Plasmid rolling-circle replication: Recent developments
    • Khan, S. A. 2000. Plasmid rolling-circle replication: recent developments. Mol. Microbiol. 37:477-484.
    • (2000) Mol. Microbiol. , vol.37 , pp. 477-484
    • Khan, S.A.1
  • 20
    • 0036022860 scopus 로고    scopus 로고
    • Bacillus anthracis genetics and virulence gene regulation
    • Koehler, T. M. 2002. Bacillus anthracis genetics and virulence gene regulation. Curr. Top. Microbiol. Immunol. 271:143-164.
    • (2002) Curr. Top. Microbiol. Immunol. , vol.271 , pp. 143-164
    • Koehler, T.M.1
  • 22
    • 0027518667 scopus 로고
    • Helicase-catalyzed DNA unwinding
    • Lohman, T. M. 1993. Helicase-catalyzed DNA unwinding. J. Biol. Chem. 268:2269-2272.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2269-2272
    • Lohman, T.M.1
  • 23
    • 0029893874 scopus 로고    scopus 로고
    • Mechanisms of helicase-catalyzed DNA unwinding
    • Lohman, T. M., and K. P. Bjornson. 1996. Mechanisms of helicase-catalyzed DNA unwinding. Annu. Rev. Biochem. 65:169-214.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 169-214
    • Lohman, T.M.1    Bjornson, K.P.2
  • 24
    • 0034479416 scopus 로고    scopus 로고
    • Crawling and wiggling on DNA: Structural insights to the mechanism of DNA unwinding by helicases
    • Marians, K. J. 2000. Crawling and wiggling on DNA: structural insights to the mechanism of DNA unwinding by helicases. Structure 8:R227-R235.
    • (2000) Structure , vol.8
    • Marians, K.J.1
  • 25
    • 0033617191 scopus 로고    scopus 로고
    • Escherichia coli DNA helicase II is active as a monomer
    • Mechanic, L. E., M. C. Hall, and S. W. Matson. 1999. Escherichia coli DNA helicase II is active as a monomer. J. Biol. Chem. 30:12488-12498.
    • (1999) J. Biol. Chem. , vol.30 , pp. 12488-12498
    • Mechanic, L.E.1    Hall, M.C.2    Matson, S.W.3
  • 28
    • 0032958074 scopus 로고    scopus 로고
    • Regulation of initiation of Bacillus subtilis chromosome replication
    • Moriya, S., Y. Imai, A. K. Hassan, and N. Ogasawara. 1999. Regulation of initiation of Bacillus subtilis chromosome replication, Plasmid 41:17-29.
    • (1999) Plasmid , vol.41 , pp. 17-29
    • Moriya, S.1    Imai, Y.2    Hassan, A.K.3    Ogasawara, N.4
  • 29
    • 0031854048 scopus 로고    scopus 로고
    • PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication
    • Petit, M. A., E. Dervyn, M. Rose, K. D. Entian, S. McGovern, S. D. Ehrlich, and C. Bruand. 1998. PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication. Mol. Microbiol. 29:261-273.
    • (1998) Mol. Microbiol. , vol.29 , pp. 261-273
    • Petit, M.A.1    Dervyn, E.2    Rose, M.3    Entian, K.D.4    McGovern, S.5    Ehrlich, S.D.6    Bruand, C.7
  • 30
    • 0037124327 scopus 로고    scopus 로고
    • Essential bacterial helicases that counteract the toxicity of recombination proteins
    • Petit, M. A., and S. D. Ehrlich. 2002. Essential bacterial helicases that counteract the toxicity of recombination proteins, EMBO J. 21:3137-3147.
    • (2002) EMBO J. , vol.21 , pp. 3137-3147
    • Petit, M.A.1    Ehrlich, S.D.2
  • 33
    • 0033812649 scopus 로고    scopus 로고
    • The interaction domains of the DnaA and DnaB replication proteins of Escherichia coli
    • Seitz, H., C. Weige, and W. Messer. 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    Weige, C.2    Messer, W.3
  • 35
    • 0034679815 scopus 로고    scopus 로고
    • Uncoupling DNA translocation and helicase activity in PcrA: Direct evidence for an active mechanism
    • Soultanas, P., M. S. Dillingham, P. Wiley, M. R. Webb, and D. B. Wigley. 2000. Uncoupling DNA translocation and helicase activity in PcrA: direct evidence for an active mechanism. EMBO J. 19:3799-3810.
    • (2000) EMBO J. , vol.19 , pp. 3799-3810
    • Soultanas, P.1    Dillingham, M.S.2    Wiley, P.3    Webb, M.R.4    Wigley, D.B.5
  • 36
    • 0035150184 scopus 로고    scopus 로고
    • Unwinding the "Gordian knot" of helicase action
    • Soultanas, P., and D. B. Wigley. 2001. Unwinding the "Gordian knot" of helicase action. Trends Biochem. Sci. 26:47-54.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 47-54
    • Soultanas, P.1    Wigley, D.B.2
  • 37
    • 0037673943 scopus 로고    scopus 로고
    • The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments
    • Veaute, X., J. Jeusset, C. Soustelle, S. C. Kowalczykowski, E. L. Cam, and F. Fabre. 2003. The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments. Nature 423:309-312.
    • (2003) Nature , vol.423 , pp. 309-312
    • Veaute, X.1    Jeusset, J.2    Soustelle, C.3    Kowalczykowski, S.C.4    Cam, E.L.5    Fabre, F.6
  • 38
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar, S. S., P. Soultanas, M. S. Dillingham, H. S. Subramanya, and D. B. Wigley. 1999. Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism. Cell 97:75-84.
    • (1999) Cell , vol.97 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5


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