메뉴 건너뛰기




Volumn 72, Issue 4, 2008, Pages 642-671

RecBCD enzyme and the repair of double-stranded DNA breaks

Author keywords

[No Author keywords available]

Indexed keywords

EXODEOXYRIBONUCLEASE V; HELICASE; HOLOENZYME;

EID: 57349157777     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/MMBR.00020-08     Document Type: Review
Times cited : (432)

References (329)
  • 2
    • 0021929046 scopus 로고
    • Manipulation of intracellular magnesium content in polymyxin B nonapeptide-sensitized Escherichia coli by ionophore A23187
    • Alatossava, T., H. Jutte, A. Kuhn, and E. Kellenberger. 1985. Manipulation of intracellular magnesium content in polymyxin B nonapeptide-sensitized Escherichia coli by ionophore A23187. J. Bacteriol. 162:413-419.
    • (1985) J. Bacteriol , vol.162 , pp. 413-419
    • Alatossava, T.1    Jutte, H.2    Kuhn, A.3    Kellenberger, E.4
  • 3
    • 47749093168 scopus 로고    scopus 로고
    • Helicobacter pylori AddAB helicase-nuclease and RecA promote recombination-related DNA repair and survival during stomach colonization
    • Amundsen, S. K., J. Fero, L. M. Hansen, G. A. Cromie, J. V. Solnick, G. R. Smith, and N. R. Salama. 2008. Helicobacter pylori AddAB helicase-nuclease and RecA promote recombination-related DNA repair and survival during stomach colonization. Mol. Microbiol. 69:994-1007.
    • (2008) Mol. Microbiol , vol.69 , pp. 994-1007
    • Amundsen, S.K.1    Fero, J.2    Hansen, L.M.3    Cromie, G.A.4    Solnick, J.V.5    Smith, G.R.6    Salama, N.R.7
  • 4
    • 0025163199 scopus 로고
    • Genetic dissection of the biochemical activities of RecBCD enzyme
    • Amundsen, S. K., A. M. Neiman, S. M. Thibodeaux, and G. R. Smith. 1990. Genetic dissection of the biochemical activities of RecBCD enzyme. Genetics 126:25-40.
    • (1990) Genetics , vol.126 , pp. 25-40
    • Amundsen, S.K.1    Neiman, A.M.2    Thibodeaux, S.M.3    Smith, G.R.4
  • 5
    • 33846555471 scopus 로고    scopus 로고
    • Chi hotspot activity in Escherichia coli without RecBCD exonuclease activity: Implications for the mechanism of recombination
    • Amundsen, S. K., and G. R. Smith. 2007. Chi hotspot activity in Escherichia coli without RecBCD exonuclease activity: implications for the mechanism of recombination. Genetics 175:41-54.
    • (2007) Genetics , vol.175 , pp. 41-54
    • Amundsen, S.K.1    Smith, G.R.2
  • 6
    • 0037459374 scopus 로고    scopus 로고
    • Interchangeable parts of the Escherichia coli recombination machinery
    • Amundsen, S. K., and G. R. Smith. 2003. Interchangeable parts of the Escherichia coli recombination machinery. Cell 112:741-744.
    • (2003) Cell , vol.112 , pp. 741-744
    • Amundsen, S.K.1    Smith, G.R.2
  • 8
    • 37249047064 scopus 로고    scopus 로고
    • Intersubunit signaling in RecBCD enzyme, a complex protein machine regulated by Chi hot spots
    • Amundsen, S. K., A. F. Taylor, M. Reddy, and G. R. Smith. 2007. Intersubunit signaling in RecBCD enzyme, a complex protein machine regulated by Chi hot spots. Genes Dev. 21:3296-3307.
    • (2007) Genes Dev , vol.21 , pp. 3296-3307
    • Amundsen, S.K.1    Taylor, A.F.2    Reddy, M.3    Smith, G.R.4
  • 9
    • 0035989351 scopus 로고    scopus 로고
    • A domain of RecC required for assembly of the regulatory RecD subunit into the Escherichia coli RecBCD holoenzyme
    • Amundsen, S. K., A. F. Taylor, and G. R. Smith. 2002. A domain of RecC required for assembly of the regulatory RecD subunit into the Escherichia coli RecBCD holoenzyme. Genetics 161:483-492.
    • (2002) Genetics , vol.161 , pp. 483-492
    • Amundsen, S.K.1    Taylor, A.F.2    Smith, G.R.3
  • 10
    • 0034691091 scopus 로고    scopus 로고
    • The RecD subunit of the Escherichia coli RecBCD enzyme inhibits RecA loading, homologous recombination, and DNA repair
    • Amundsen, S. K., A. F. Taylor, and G. R. Smith. 2000. The RecD subunit of the Escherichia coli RecBCD enzyme inhibits RecA loading, homologous recombination, and DNA repair. Proc. Natl. Acad. Sci. USA 97:7399-7404.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7399-7404
    • Amundsen, S.K.1    Taylor, A.F.2    Smith, G.R.3
  • 11
    • 0032077531 scopus 로고    scopus 로고
    • A stimulatory RNA associated with RecBCD enzyme
    • Amundsen, S. K., A. F. Taylor, and G. R. Smith. 1998. A stimulatory RNA associated with RecBCD enzyme. Nucleic Acids Res. 26:2125-2131.
    • (1998) Nucleic Acids Res , vol.26 , pp. 2125-2131
    • Amundsen, S.K.1    Taylor, A.F.2    Smith, G.R.3
  • 12
    • 0031064615 scopus 로고    scopus 로고
    • Chiactivated RecBCD enzyme possesses 5′→3′ nucleolytic activity, but RecBC enzyme does not: Evidence suggesting that the alteration induced by Chi is not simply ejection of the RecD subunit
    • Anderson, D. G., J. J. Churchill, and S. C. Kowalczykowski. 1997. Chiactivated RecBCD enzyme possesses 5′→3′ nucleolytic activity, but RecBC enzyme does not: evidence suggesting that the alteration induced by Chi is not simply ejection of the RecD subunit. Genes Cells 2:117-128.
    • (1997) Genes Cells , vol.2 , pp. 117-128
    • Anderson, D.G.1    Churchill, J.J.2    Kowalczykowski, S.C.3
  • 13
    • 0033578824 scopus 로고    scopus 로고
    • A single mutation, RecB(D1080A), eliminates RecA protein loading but not Chi recognition by RecBCD enzyme
    • Anderson, D. G., J. J. Churchill, and S. C. Kowalczykowski. 1999. A single mutation, RecB(D1080A), eliminates RecA protein loading but not Chi recognition by RecBCD enzyme. J. Biol. Chem. 274:27139-27144.
    • (1999) J. Biol. Chem , vol.274 , pp. 27139-27144
    • Anderson, D.G.1    Churchill, J.J.2    Kowalczykowski, S.C.3
  • 14
    • 0030969429 scopus 로고    scopus 로고
    • The recombination hot spot χ is a regulatory element that switches the polarity of DNA degradation by the RecBCD enzyme
    • Anderson, D. G., and S. C. Kowalczykowski. 1997. The recombination hot spot χ is a regulatory element that switches the polarity of DNA degradation by the RecBCD enzyme. Genes Dev. 11:571-581.
    • (1997) Genes Dev , vol.11 , pp. 571-581
    • Anderson, D.G.1    Kowalczykowski, S.C.2
  • 15
    • 0032428175 scopus 로고    scopus 로고
    • Reconstitution of an SOS response pathway: Derepression of transcription in response to DNA breaks
    • Anderson, D. G., and S. C. Kowalczykowski. 1998. Reconstitution of an SOS response pathway: derepression of transcription in response to DNA breaks. Cell 95:975-979.
    • (1998) Cell , vol.95 , pp. 975-979
    • Anderson, D.G.1    Kowalczykowski, S.C.2
  • 16
    • 0032544662 scopus 로고    scopus 로고
    • SSB protein controls RecBCD enzyme nuclease activity during unwinding: A new role for looped intermediates
    • Anderson, D. G., and S. C. Kowalczykowski. 1998. SSB protein controls RecBCD enzyme nuclease activity during unwinding: a new role for looped intermediates. J. Mol. Biol. 282:275-285.
    • (1998) J. Mol. Biol , vol.282 , pp. 275-285
    • Anderson, D.G.1    Kowalczykowski, S.C.2
  • 17
    • 0031444642 scopus 로고    scopus 로고
    • The translocating RecBCD enzyme stimulates recombination by directing RecA protein onto ssDNA in a χ-regulated manner
    • Anderson, D. G., and S. C. Kowalczykowski. 1997. The translocating RecBCD enzyme stimulates recombination by directing RecA protein onto ssDNA in a χ-regulated manner. Cell 90:77-86.
    • (1997) Cell , vol.90 , pp. 77-86
    • Anderson, D.G.1    Kowalczykowski, S.C.2
  • 18
    • 0032986887 scopus 로고    scopus 로고
    • Bacteriophage T4 gp2 interferes with cell viability and with bacteriophage lambda Red recombination
    • Appasani, K., D. S. Thaler, and E. B. Goldberg. 1999. Bacteriophage T4 gp2 interferes with cell viability and with bacteriophage lambda Red recombination. J. Bacteriol. 181:1352-1355.
    • (1999) J. Bacteriol , vol.181 , pp. 1352-1355
    • Appasani, K.1    Thaler, D.S.2    Goldberg, E.B.3
  • 19
    • 33947587178 scopus 로고    scopus 로고
    • Validating the significance of genomic properties of Chi sites from the distribution of all octamers in Escherichia coli
    • Arakawa, K., R. Uno, Y. Nakayama, and M. Tomita. 2007. Validating the significance of genomic properties of Chi sites from the distribution of all octamers in Escherichia coli. Gene 392:239-246.
    • (2007) Gene , vol.392 , pp. 239-246
    • Arakawa, K.1    Uno, R.2    Nakayama, Y.3    Tomita, M.4
  • 20
    • 0034664813 scopus 로고    scopus 로고
    • Holliday junction resolvases and related nucleases: Identification of new families, phyletic distribution and evolutionary trajectories
    • Aravind, L., K. S. Makarova, and E. V. Koonin. 2000. Holliday junction resolvases and related nucleases: identification of new families, phyletic distribution and evolutionary trajectories. Nucleic Acids Res. 28:3417-3432.
    • (2000) Nucleic Acids Res , vol.28 , pp. 3417-3432
    • Aravind, L.1    Makarova, K.S.2    Koonin, E.V.3
  • 22
    • 0034647421 scopus 로고    scopus 로고
    • A novel, 11 nucleotide variant of χ, χ*: One of a class of sequences defining the Escherichia coli recombination hotspot χ
    • Arnold, D. A., N. Handa, I. Kobayashi, and S. C. Kowalczykowski. 2000. A novel, 11 nucleotide variant of χ, χ*: one of a class of sequences defining the Escherichia coli recombination hotspot χ. J. Mol. Biol. 300:469-479.
    • (2000) J. Mol. Biol , vol.300 , pp. 469-479
    • Arnold, D.A.1    Handa, N.2    Kobayashi, I.3    Kowalczykowski, S.C.4
  • 23
    • 0034697325 scopus 로고    scopus 로고
    • Facilitated loading of RecA protein is essential to recombination by RecBCD enzyme
    • Arnold, D. A., and S. C. Kowalczykowski. 2000. Facilitated loading of RecA protein is essential to recombination by RecBCD enzyme. J. Biol. Chem. 275:12261-12265.
    • (2000) J. Biol. Chem , vol.275 , pp. 12261-12265
    • Arnold, D.A.1    Kowalczykowski, S.C.2
  • 24
    • 57349174834 scopus 로고    scopus 로고
    • Arnold, D. A., and S. C. Kowalczykowski. 19 April 2001, posting date. RecBCD helicase/nuclease. In Encyclopedia of life sciences. John Wiley & Sons, Chichester, United Kingdom.http://www.els.net.
    • Arnold, D. A., and S. C. Kowalczykowski. 19 April 2001, posting date. RecBCD helicase/nuclease. In Encyclopedia of life sciences. John Wiley & Sons, Chichester, United Kingdom.http://www.els.net.
  • 25
    • 0034528196 scopus 로고    scopus 로고
    • Characterization of the enzymatic properties of the yeast dna2 helicase/endonuclease suggests a new model for Okazaki fragment processing
    • Bae, S. H., and Y. S. Seo. 2000. Characterization of the enzymatic properties of the yeast dna2 helicase/endonuclease suggests a new model for Okazaki fragment processing. J. Biol. Chem. 275:38022-38031.
    • (2000) J. Biol. Chem , vol.275 , pp. 38022-38031
    • Bae, S.H.1    Seo, Y.S.2
  • 27
    • 0017286062 scopus 로고
    • Postinfection control by bacteriophage T4 of Escherichia coli recBC nuclease activity
    • Behme, M. T., G. D. Lilley, and K. Ebisuzaki. 1976. Postinfection control by bacteriophage T4 of Escherichia coli recBC nuclease activity. J. Virol. 18:20-25.
    • (1976) J. Virol , vol.18 , pp. 20-25
    • Behme, M.T.1    Lilley, G.D.2    Ebisuzaki, K.3
  • 28
    • 26944459614 scopus 로고    scopus 로고
    • Structure and mechanism of Escherichia coli RecA ATPase
    • Bell, C. E. 2005. Structure and mechanism of Escherichia coli RecA ATPase. Mol. Microbiol. 58:358-366.
    • (2005) Mol. Microbiol , vol.58 , pp. 358-366
    • Bell, C.E.1
  • 29
    • 0032584913 scopus 로고    scopus 로고
    • Correlation of chi orientation with transcription indicates a fundamental relationship between recombination and transcription
    • Bell, S. J., Y. C. Chow, J. Y. K. Ho, and D. R. Forsdyke. 1998. Correlation of chi orientation with transcription indicates a fundamental relationship between recombination and transcription. Gene 216:285-292.
    • (1998) Gene , vol.216 , pp. 285-292
    • Bell, S.J.1    Chow, Y.C.2    Ho, J.Y.K.3    Forsdyke, D.R.4
  • 30
    • 0016807042 scopus 로고
    • - spheroplasts measured with different forms of bacteriophage DNA
    • - spheroplasts measured with different forms of bacteriophage DNA. J. Virol. 15:861-871.
    • (1975) J. Virol , vol.15 , pp. 861-871
    • Benzinger, R.1    Enquist, L.W.2    Skalka, A.3
  • 32
    • 57349126600 scopus 로고    scopus 로고
    • Bianco, P. R., and S. C. Kowalczykowski. 23 September 2005, posting date. RecA protein. In Encyclopedia of life sciences. John Wiley & Sons, Chichester, United Kingdom. http://www.els.net.
    • Bianco, P. R., and S. C. Kowalczykowski. 23 September 2005, posting date. RecA protein. In Encyclopedia of life sciences. John Wiley & Sons, Chichester, United Kingdom. http://www.els.net.
  • 33
    • 0030917148 scopus 로고    scopus 로고
    • The recombination hotspot Chi is recognized by the translocating RecBCD enzyme as the single strand of DNA containing the sequence 5′-GCTGGTGG-3′
    • Bianco, P. R., and S. C. Kowalczykowski. 1997. The recombination hotspot Chi is recognized by the translocating RecBCD enzyme as the single strand of DNA containing the sequence 5′-GCTGGTGG-3′. Proc. Natl. Acad. Sci. USA 94:6706-6711.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 6706-6711
    • Bianco, P.R.1    Kowalczykowski, S.C.2
  • 34
    • 0034682407 scopus 로고    scopus 로고
    • Translocation step size and mechanism of the RecBC DNA helicase
    • Bianco, P. R., and S. C. Kowalczykowski. 2000. Translocation step size and mechanism of the RecBC DNA helicase. Nature 405:368-372.
    • (2000) Nature , vol.405 , pp. 368-372
    • Bianco, P.R.1    Kowalczykowski, S.C.2
  • 35
    • 0001865832 scopus 로고    scopus 로고
    • DNA strand exchange proteins: A biochemical and physical comparison
    • Bianco, P. R., R. B. Tracy, and S. C. Kowalczykowski. 1998. DNA strand exchange proteins: a biochemical and physical comparison. Front. Biosci. 3:D570-D603.
    • (1998) Front. Biosci , vol.3
    • Bianco, P.R.1    Tracy, R.B.2    Kowalczykowski, S.C.3
  • 36
    • 0032939636 scopus 로고    scopus 로고
    • RecD function is required for high-pressure growth of a deep-sea bacterium
    • Bidle, K. A., and D. H. Bartlett. 1999. RecD function is required for high-pressure growth of a deep-sea bacterium. J. Bacteriol. 181:2330-2337.
    • (1999) J. Bacteriol , vol.181 , pp. 2330-2337
    • Bidle, K.A.1    Bartlett, D.H.2
  • 37
    • 0022509196 scopus 로고
    • Identification and characterization of recD, a gene affecting plasmid maintenance and recombination in Escherichia coli
    • Biek, D. P., and S. N. Cohen. 1986. Identification and characterization of recD, a gene affecting plasmid maintenance and recombination in Escherichia coli. J. Bacteriol. 167:594-603.
    • (1986) J. Bacteriol , vol.167 , pp. 594-603
    • Biek, D.P.1    Cohen, S.N.2
  • 39
    • 0020443521 scopus 로고
    • Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography
    • Bochner, B. R., and B. N. Ames. 1982. Complete analysis of cellular nucleotides by two-dimensional thin layer chromatography. J. Biol. Chem. 257:9759-9769.
    • (1982) J. Biol. Chem , vol.257 , pp. 9759-9769
    • Bochner, B.R.1    Ames, B.N.2
  • 40
    • 0026646152 scopus 로고
    • The RecB subunit of the Escherichia coli RecBCD enzyme couples ATP hydrolysis to DNA unwinding
    • Boehmer, P. E., and P. T. Emmerson. 1992. The RecB subunit of the Escherichia coli RecBCD enzyme couples ATP hydrolysis to DNA unwinding. J. Biol. Chem. 267:4981-4987.
    • (1992) J. Biol. Chem , vol.267 , pp. 4981-4987
    • Boehmer, P.E.1    Emmerson, P.T.2
  • 41
    • 0024586396 scopus 로고
    • Strand specificity of DNA unwinding by RecBCD enzyme
    • Braedt, G., and G. R. Smith. 1989. Strand specificity of DNA unwinding by RecBCD enzyme. Proc. Natl. Acad. Sci. USA 86:871-875.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 871-875
    • Braedt, G.1    Smith, G.R.2
  • 43
    • 0026586307 scopus 로고
    • Overproduction of the RecD polypeptide sensitizes Escherichia coli cells to gamma-radiation
    • Brcic-Kostic, K., I. Stojiljkovic, E. Salaj-Smic, and Z. Trgovcevic. 1992. Overproduction of the RecD polypeptide sensitizes Escherichia coli cells to gamma-radiation. Mutat. Res. 281:123-127.
    • (1992) Mutat. Res , vol.281 , pp. 123-127
    • Brcic-Kostic, K.1    Stojiljkovic, I.2    Salaj-Smic, E.3    Trgovcevic, Z.4
  • 44
    • 0027416848 scopus 로고
    • Recombination-deficient mutants of Salmonella typhimurium are avirulent and sensitive to the oxidative burst of macrophages
    • Buchmeier, N. A., C. J. Lipps, M. Y. So, and F. Heffron. 1993. Recombination-deficient mutants of Salmonella typhimurium are avirulent and sensitive to the oxidative burst of macrophages. Mol. Microbiol. 7:933-936.
    • (1993) Mol. Microbiol , vol.7 , pp. 933-936
    • Buchmeier, N.A.1    Lipps, C.J.2    So, M.Y.3    Heffron, F.4
  • 45
    • 0029098312 scopus 로고
    • A yeast gene required for DNA replication encodes a protein with homology to DNA helicases
    • Budd, M. E., and J. L. Campbell. 1995. A yeast gene required for DNA replication encodes a protein with homology to DNA helicases. Proc. Natl. Acad. Sci. USA 92:7642-7646.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7642-7646
    • Budd, M.E.1    Campbell, J.L.2
  • 46
    • 0034596053 scopus 로고    scopus 로고
    • The nuclease activity of the yeast DNA2 protein, which is related to the RecB-like nucleases, is essential in vivo
    • Budd, M. E., W. Choe, and J. L. Campbell. 2000. The nuclease activity of the yeast DNA2 protein, which is related to the RecB-like nucleases, is essential in vivo. J. Biol. Chem. 275:16518-16529.
    • (2000) J. Biol. Chem , vol.275 , pp. 16518-16529
    • Budd, M.E.1    Choe, W.2    Campbell, J.L.3
  • 47
    • 85015087906 scopus 로고    scopus 로고
    • Ten years of tension: Single-molecule DNA mechanics
    • Bustamante, C., Z. Bryant, and S. B. Smith. 2003. Ten years of tension: single-molecule DNA mechanics. Nature 421:423-427.
    • (2003) Nature , vol.421 , pp. 423-427
    • Bustamante, C.1    Bryant, Z.2    Smith, S.B.3
  • 48
    • 25444456899 scopus 로고    scopus 로고
    • Increasing the length of the single-stranded overhang enhances unwinding of duplex DNA by bacteriophage T4 Dda helicase
    • Byrd, A. K., and K. D. Raney. 2005. Increasing the length of the single-stranded overhang enhances unwinding of duplex DNA by bacteriophage T4 Dda helicase. Biochemistry 44:12990-12997.
    • (2005) Biochemistry , vol.44 , pp. 12990-12997
    • Byrd, A.K.1    Raney, K.D.2
  • 49
    • 2542432027 scopus 로고    scopus 로고
    • Protein displacement by an assembly of helicase molecules aligned along single-stranded DNA
    • Byrd, A. K., and K. D. Raney. 2004. Protein displacement by an assembly of helicase molecules aligned along single-stranded DNA. Nat. Struct. Mol. Biol. 11:531-538.
    • (2004) Nat. Struct. Mol. Biol , vol.11 , pp. 531-538
    • Byrd, A.K.1    Raney, K.D.2
  • 51
    • 0015044799 scopus 로고
    • Involvement of recombination genes in growth and viability of Escherichia coli K-12
    • Capaldo-Kimball, F., and S. D. Barbour. 1971. Involvement of recombination genes in growth and viability of Escherichia coli K-12. J. Bacteriol. 106:204-212.
    • (1971) J. Bacteriol , vol.106 , pp. 204-212
    • Capaldo-Kimball, F.1    Barbour, S.D.2
  • 52
    • 0016607211 scopus 로고
    • The role of the rec genes in the viability of Escherichia coli K12
    • Capaldo, F. N., and S. D. Barbour. 1975. The role of the rec genes in the viability of Escherichia coli K12. Basic Life Sci. 5A:405-418.
    • (1975) Basic Life Sci , vol.5 A , pp. 405-418
    • Capaldo, F.N.1    Barbour, S.D.2
  • 53
    • 0016379860 scopus 로고
    • Analysis of the growth of recombination-deficient strains of Escherichia coli K-12
    • Capaldo, F. N., G. Ramsey, and S. D. Barbour. 1974. Analysis of the growth of recombination-deficient strains of Escherichia coli K-12. J. Bacteriol. 118:242-249.
    • (1974) J. Bacteriol , vol.118 , pp. 242-249
    • Capaldo, F.N.1    Ramsey, G.2    Barbour, S.D.3
  • 54
    • 0023661673 scopus 로고
    • Kinetic studies of recA protein binding to a fluorescent single-stranded polynucleotide
    • Chabbert, M., C. Cazenave, and C. Helene. 1987. Kinetic studies of recA protein binding to a fluorescent single-stranded polynucleotide. Biochemistry 26:2218-2225.
    • (1987) Biochemistry , vol.26 , pp. 2218-2225
    • Chabbert, M.1    Cazenave, C.2    Helene, C.3
  • 55
    • 0021702028 scopus 로고
    • A new class of Escherichia coli recBC mutants: Implications for the role of RecBC enzyme in homologous recombination
    • Chaudhury, A. M., and G. R. Smith. 1984. A new class of Escherichia coli recBC mutants: implications for the role of RecBC enzyme in homologous recombination. Proc. Natl. Acad. Sci. USA 81:7850-7854.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 7850-7854
    • Chaudhury, A.M.1    Smith, G.R.2
  • 56
    • 0033022756 scopus 로고    scopus 로고
    • Characterization of the recD gene of Neisseria gonorrhoeae MS11 and the effect of recD inactivation on pilin variation and DNA transformation
    • Chaussee, M. S., J. Wilson, and S. A. Hill. 1999. Characterization of the recD gene of Neisseria gonorrhoeae MS11 and the effect of recD inactivation on pilin variation and DNA transformation. Microbiology 145:389-400.
    • (1999) Microbiology , vol.145 , pp. 389-400
    • Chaussee, M.S.1    Wilson, J.2    Hill, S.A.3
  • 57
    • 0034696750 scopus 로고    scopus 로고
    • The Bacillus subtilis AddAB helicase/nuclease is regulated by its cognate Chi sequence in vitro
    • Chédin, F., S. D. Ehrlich, and S. C. Kowalczykowski. 2000. The Bacillus subtilis AddAB helicase/nuclease is regulated by its cognate Chi sequence in vitro. J. Mol. Biol. 298:7-20.
    • (2000) J. Mol. Biol , vol.298 , pp. 7-20
    • Chédin, F.1    Ehrlich, S.D.2    Kowalczykowski, S.C.3
  • 58
    • 33745838577 scopus 로고    scopus 로고
    • The AddAB helicase/nuclease forms a stable complex with its cognate χ sequence during translocation
    • Chédin, F., N. Handa, M. S. Dillingham, and S. C. Kowalczykowski. 2006. The AddAB helicase/nuclease forms a stable complex with its cognate χ sequence during translocation. J. Biol. Chem. 281:18610-18617.
    • (2006) J. Biol. Chem , vol.281 , pp. 18610-18617
    • Chédin, F.1    Handa, N.2    Dillingham, M.S.3    Kowalczykowski, S.C.4
  • 59
    • 0036228220 scopus 로고    scopus 로고
    • A novel family of regulated helicases/nucleases from gram-positive bacteria: Insights into the initiation of DNA recombination
    • Chédin, F., and S. C. Kowalczykowski. 2002. A novel family of regulated helicases/nucleases from gram-positive bacteria: insights into the initiation of DNA recombination. Mol. Microbiol. 43:823-834.
    • (2002) Mol. Microbiol , vol.43 , pp. 823-834
    • Chédin, F.1    Kowalczykowski, S.C.2
  • 60
    • 0031713244 scopus 로고    scopus 로고
    • A five-nucleotide sequence protects DNA from exonucleolytic degradation by AddAB, the RecBCD analogue of Bacillus subtilis
    • Chédin, F., P. Noirot, V. Biaudet, and S. D. Ehrlich. 1998. A five-nucleotide sequence protects DNA from exonucleolytic degradation by AddAB, the RecBCD analogue of Bacillus subtilis. Mol. Microbiol. 29:1369-1377.
    • (1998) Mol. Microbiol , vol.29 , pp. 1369-1377
    • Chédin, F.1    Noirot, P.2    Biaudet, V.3    Ehrlich, S.D.4
  • 61
    • 0032562543 scopus 로고    scopus 로고
    • Functions of the ATP hydrolysis subunits (RecB and RecD) in the nuclease reactions catalyzed by the RecBCD enzyme from Escherichia coli
    • Chen, H. W., D. E. Randle, M. Gabbidon, and D. A. Julin. 1998. Functions of the ATP hydrolysis subunits (RecB and RecD) in the nuclease reactions catalyzed by the RecBCD enzyme from Escherichia coli. J. Mol. Biol. 278:89-104.
    • (1998) J. Mol. Biol , vol.278 , pp. 89-104
    • Chen, H.W.1    Randle, D.E.2    Gabbidon, M.3    Julin, D.A.4
  • 62
    • 0030943197 scopus 로고    scopus 로고
    • The RecD subunit of the RecBCD enzyme from Escherichia coli is a single-stranded DNA-dependent ATPase
    • Chen, H. W., B. Ruan, M. Yu, J. Wang, and D. A. Julin. 1997. The RecD subunit of the RecBCD enzyme from Escherichia coli is a single-stranded DNA-dependent ATPase. J. Biol. Chem. 272:10072-10079.
    • (1997) J. Biol. Chem , vol.272 , pp. 10072-10079
    • Chen, H.W.1    Ruan, B.2    Yu, M.3    Wang, J.4    Julin, D.A.5
  • 63
    • 0023660273 scopus 로고
    • Cutting of Chi-like sequences by the RecBCD enzyme of Escherichia coli
    • Cheng, K. C., and G. R. Smith. 1987. Cutting of Chi-like sequences by the RecBCD enzyme of Escherichia coli. J. Mol. Biol. 194:747-750.
    • (1987) J. Mol. Biol , vol.194 , pp. 747-750
    • Cheng, K.C.1    Smith, G.R.2
  • 64
    • 0024722243 scopus 로고
    • Distribution of Chi-stimulated recombinational exchanges and heteroduplex endpoints in phage lambda
    • Cheng, K. C., and G. R. Smith. 1989. Distribution of Chi-stimulated recombinational exchanges and heteroduplex endpoints in phage lambda. Genetics 123:5-17.
    • (1989) Genetics , vol.123 , pp. 5-17
    • Cheng, K.C.1    Smith, G.R.2
  • 65
    • 0021755950 scopus 로고
    • Recombinational hotspot activity of Chi-like sequences
    • Cheng, K. C., and G. R. Smith. 1984. Recombinational hotspot activity of Chi-like sequences. J. Mol. Biol. 180:371-377.
    • (1984) J. Mol. Biol , vol.180 , pp. 371-377
    • Cheng, K.C.1    Smith, G.R.2
  • 66
    • 0033119260 scopus 로고    scopus 로고
    • The RecBC enzyme loads RecA protein onto ssDNA asymmetrically and independently of Chi, resulting in constitutive recombination activation
    • Churchill, J. J., D. G. Anderson, and S. C. Kowalczykowski. 1999. The RecBC enzyme loads RecA protein onto ssDNA asymmetrically and independently of Chi, resulting in constitutive recombination activation. Genes Dev. 13:901-911.
    • (1999) Genes Dev , vol.13 , pp. 901-911
    • Churchill, J.J.1    Anderson, D.G.2    Kowalczykowski, S.C.3
  • 67
    • 0034737310 scopus 로고    scopus 로고
    • Identification of the RecA protein-loading domain of RecBCD enzyme
    • Churchill, J. J., and S. C. Kowalczykowski. 2000. Identification of the RecA protein-loading domain of RecBCD enzyme. J. Mol. Biol. 297:537-542.
    • (2000) J. Mol. Biol , vol.297 , pp. 537-542
    • Churchill, J.J.1    Kowalczykowski, S.C.2
  • 68
    • 0028292327 scopus 로고
    • Homologous genetic recombination: The pieces begin to fall into place
    • Clark, A. J., and S. J. Sandler. 1994. Homologous genetic recombination: the pieces begin to fall into place. Crit. Rev. Microbiol. 20:125-142.
    • (1994) Crit. Rev. Microbiol , vol.20 , pp. 125-142
    • Clark, A.J.1    Sandler, S.J.2
  • 70
    • 0031791115 scopus 로고    scopus 로고
    • Genomics, Chi sites and codons: 'islands of preferred DNA pairing' are oceans of ORFs
    • Colbert, T., A. F. Taylor, and G. R. Smith. 1998. Genomics, Chi sites and codons: 'islands of preferred DNA pairing' are oceans of ORFs. Trends Genet. 14:485-488.
    • (1998) Trends Genet , vol.14 , pp. 485-488
    • Colbert, T.1    Taylor, A.F.2    Smith, G.R.3
  • 71
    • 0015040643 scopus 로고
    • Properties of F′ factor deoxyribonucleic acid transferred from ultraviolet-irradiated donors: Photoreactivation in the recipient and the influence of recA, recB, recC, and uvr genes
    • Cole, R. S. 1971. Properties of F′ factor deoxyribonucleic acid transferred from ultraviolet-irradiated donors: photoreactivation in the recipient and the influence of recA, recB, recC, and uvr genes. J. Bacteriol. 106:143-149.
    • (1971) J. Bacteriol , vol.106 , pp. 143-149
    • Cole, R.S.1
  • 72
    • 24044441920 scopus 로고    scopus 로고
    • Recs preventing wrecks
    • Courcelle, J. 2005. Recs preventing wrecks. Mutat. Res. 577:217-227.
    • (2005) Mutat. Res , vol.577 , pp. 217-227
    • Courcelle, J.1
  • 73
    • 0030890705 scopus 로고    scopus 로고
    • recF and recR are required for the resumption of replication at DNA replication forks in Escherichia coli
    • Courcelle, J., C. Carswell-Crumpton, and P. C. Hanawalt. 1997. recF and recR are required for the resumption of replication at DNA replication forks in Escherichia coli. Proc. Natl. Acad. Sci. USA 94:3714-3719.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3714-3719
    • Courcelle, J.1    Carswell-Crumpton, C.2    Hanawalt, P.C.3
  • 74
    • 0037436108 scopus 로고    scopus 로고
    • DNA damage-induced replication fork regression and processing in Escherichia coli
    • Courcelle, J., J. R. Donaldson, K. H. Chow, and C. T. Courcelle. 2003. DNA damage-induced replication fork regression and processing in Escherichia coli. Science 299:1064-1067.
    • (2003) Science , vol.299 , pp. 1064-1067
    • Courcelle, J.1    Donaldson, J.R.2    Chow, K.H.3    Courcelle, C.T.4
  • 75
    • 34447290425 scopus 로고    scopus 로고
    • The crystal structure of lambda-Gam protein suggests a model for RecBCD inhibition
    • Court, R., N. Cook, K. Saikrishnan, and D. Wigley. 2007. The crystal structure of lambda-Gam protein suggests a model for RecBCD inhibition. J. Mol. Biol. 371:25-33.
    • (2007) J. Mol. Biol , vol.371 , pp. 25-33
    • Court, R.1    Cook, N.2    Saikrishnan, K.3    Wigley, D.4
  • 77
    • 0343551289 scopus 로고
    • RecA protein of Escherichia coli promotes branch migration, a kinetically distinct phase of DNA strand exchange
    • Cox, M. M., and I. R. Lehman. 1981. RecA protein of Escherichia coli promotes branch migration, a kinetically distinct phase of DNA strand exchange. Proc. Natl. Acad. Sci. USA 78:3433-3437.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 3433-3437
    • Cox, M.M.1    Lehman, I.R.2
  • 78
    • 0027096279 scopus 로고
    • Chi sequence protects against RecBCD degradation of DNA in vivo
    • Dabert, P., S. D. Ehrlich, and A. Gruss. 1992. Chi sequence protects against RecBCD degradation of DNA in vivo. Proc. Natl. Acad. Sci. USA 89:12073-12077.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 12073-12077
    • Dabert, P.1    Ehrlich, S.D.2    Gruss, A.3
  • 80
    • 33646182576 scopus 로고    scopus 로고
    • Functions of multiple exonucleases are essential for cell viability, DNA repair and homologous recombination in recD mutants of Escherichia coli
    • Dermić, D. 2006. Functions of multiple exonucleases are essential for cell viability, DNA repair and homologous recombination in recD mutants of Escherichia coli. Genetics 172:2057-2069.
    • (2006) Genetics , vol.172 , pp. 2057-2069
    • Dermić, D.1
  • 81
    • 33645963437 scopus 로고    scopus 로고
    • - phenocopies for extrachromosomal DNA processing due to prolonged titration of RecBCD enzyme on damaged Escherichia coli chromosome
    • - phenocopies for extrachromosomal DNA processing due to prolonged titration of RecBCD enzyme on damaged Escherichia coli chromosome. Biochimie 88:379-386.
    • (2006) Biochimie , vol.88 , pp. 379-386
    • Dermić, D.1    Dermić, E.2    Zahradka, D.3    Petranović, M.4    Lerš, N.5
  • 82
    • 16844376190 scopus 로고    scopus 로고
    • RecBCD enzyme overproduction impairs DNA repair and homologous recombination in Escherichia coli
    • Dermić, D., E. Halupecki, D. Zahradka, and M. Petranović. 2005. RecBCD enzyme overproduction impairs DNA repair and homologous recombination in Escherichia coli. Res. Microbiol. 156:304-311.
    • (2005) Res. Microbiol , vol.156 , pp. 304-311
    • Dermić, D.1    Halupecki, E.2    Zahradka, D.3    Petranović, M.4
  • 83
    • 33747832754 scopus 로고    scopus 로고
    • Exonuclease requirements for recombination of λ-phage in recD mutants of Escherichia coli
    • Dermić, D., D. Zahradka, and M. Petranović. 2006. Exonuclease requirements for recombination of λ-phage in recD mutants of Escherichia coli. Genetics 173:2399-2402.
    • (2006) Genetics , vol.173 , pp. 2399-2402
    • Dermić, D.1    Zahradka, D.2    Petranović, M.3
  • 84
    • 1642524565 scopus 로고    scopus 로고
    • The bacterial condensin/cohesin- like protein complex acts in DNA repair and regulation of gene expression
    • Dervyn, E., M. F. Noirot-Gros, P. Mervelet, S. McGovern, S. D. Ehrlich, P. Polard, and P. Noirot. 2004. The bacterial condensin/cohesin- like protein complex acts in DNA repair and regulation of gene expression. Mol. Microbiol. 51:1629-1640.
    • (2004) Mol. Microbiol , vol.51 , pp. 1629-1640
    • Dervyn, E.1    Noirot-Gros, M.F.2    Mervelet, P.3    McGovern, S.4    Ehrlich, S.D.5    Polard, P.6    Noirot, P.7
  • 85
    • 0017226423 scopus 로고
    • Mechanism localisation and control of restriction cleavage of phage T4 and lambda chromosomes in vivo
    • Dharmalingam, K., and E. B. Goldberg. 1976. Mechanism localisation and control of restriction cleavage of phage T4 and lambda chromosomes in vivo. Nature 260:406-410.
    • (1976) Nature , vol.260 , pp. 406-410
    • Dharmalingam, K.1    Goldberg, E.B.2
  • 86
    • 0035902592 scopus 로고    scopus 로고
    • Defining the roles of individual residues in the single-stranded DNA binding site of PcrA helicase
    • Dillingham, M. S., P. Soultanas, P. Wiley, M. R. Webb, and D. B. Wigley. 2001. Defining the roles of individual residues in the single-stranded DNA binding site of PcrA helicase. Proc. Natl. Acad. Sci. USA 98:8381-8387.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8381-8387
    • Dillingham, M.S.1    Soultanas, P.2    Wiley, P.3    Webb, M.R.4    Wigley, D.B.5
  • 87
  • 88
    • 27744469165 scopus 로고    scopus 로고
    • Bipolar DNA translocation contributes to highly processive DNA unwinding by RecBCD enzyme
    • Dillingham, M. S., M. R. Webb, and S. C. Kowalczykowski. 2005. Bipolar DNA translocation contributes to highly processive DNA unwinding by RecBCD enzyme. J. Biol. Chem. 280:37069-37077.
    • (2005) J. Biol. Chem , vol.280 , pp. 37069-37077
    • Dillingham, M.S.1    Webb, M.R.2    Kowalczykowski, S.C.3
  • 89
    • 0034635172 scopus 로고    scopus 로고
    • Demonstration of unidirectional 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 unidirectional 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
  • 90
    • 0028345348 scopus 로고
    • Reversible inactivation of the Escherichia coli RecBCD enzyme by the recombination hotspot χ in vitro: Evidence for functional inactivation or loss of the RecD subunit
    • Dixon, D. A., J. J. Churchill, and S. C. Kowalczykowski. 1994. Reversible inactivation of the Escherichia coli RecBCD enzyme by the recombination hotspot χ in vitro: evidence for functional inactivation or loss of the RecD subunit. Proc. Natl. Acad. Sci. USA 91:2980-2984.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2980-2984
    • Dixon, D.A.1    Churchill, J.J.2    Kowalczykowski, S.C.3
  • 91
    • 0025902330 scopus 로고    scopus 로고
    • Dixon, D. A., and S. C. Kowalczykowski. 1991. Homologous pairing in vitro stimulated by the recombination hotspot, Chi. Cell 66:361-371.
    • Dixon, D. A., and S. C. Kowalczykowski. 1991. Homologous pairing in vitro stimulated by the recombination hotspot, Chi. Cell 66:361-371.
  • 92
    • 0027511858 scopus 로고
    • The recombination hotspot χ is a regulatory sequence that acts by attenuating the nuclease activity of the E. coli RecBCD enzyme
    • Dixon, D. A., and S. C. Kowalczykowski. 1993. The recombination hotspot χ is a regulatory sequence that acts by attenuating the nuclease activity of the E. coli RecBCD enzyme. Cell 73:87-96.
    • (1993) Cell , vol.73 , pp. 87-96
    • Dixon, D.A.1    Kowalczykowski, S.C.2
  • 93
    • 0029038312 scopus 로고
    • Role of the Escherichia coli recombination hotspot, χ, in RecABCD-dependent homologous pairing
    • Dixon, D. A., and S. C. Kowalczykowski. 1995. Role of the Escherichia coli recombination hotspot, χ, in RecABCD-dependent homologous pairing. J. Biol. Chem. 270:16360-16370.
    • (1995) J. Biol. Chem , vol.270 , pp. 16360-16370
    • Dixon, D.A.1    Kowalczykowski, S.C.2
  • 94
    • 0035905807 scopus 로고    scopus 로고
    • Chi-sequence recognition and DNA translocation by single RecBCD helicase/nuclease molecules
    • Dohoney, K. M., and J. Gelles. 2001. Chi-sequence recognition and DNA translocation by single RecBCD helicase/nuclease molecules. Nature 409:370-374.
    • (2001) Nature , vol.409 , pp. 370-374
    • Dohoney, K.M.1    Gelles, J.2
  • 95
    • 0027240259 scopus 로고
    • 2109CD enzyme, which lacks χ-specific, but not non-specific, nuclease activity
    • 2109CD enzyme, which lacks χ-specific, but not non-specific, nuclease activity. J. Mol. Biol. 231:605-620.
    • (1993) J. Mol. Biol , vol.231 , pp. 605-620
    • Eggleston, A.K.1    Kowalczykowski, S.C.2
  • 96
    • 0027296790 scopus 로고
    • 2109CD enzyme, has helicase activity but does not promote efficient joint molecule formation in vitro
    • 2109CD enzyme, has helicase activity but does not promote efficient joint molecule formation in vitro. J. Mol. Biol. 231:621-633.
    • (1993) J. Mol. Biol , vol.231 , pp. 621-633
    • Eggleston, A.K.1    Kowalczykowski, S.C.2
  • 97
    • 0029879214 scopus 로고    scopus 로고
    • A helicase assay based on the displacement of fluorescent, nucleic acid-binding ligands
    • Eggleston, A. K., N. A. Rahim, and S. C. Kowalczykowski. 1996. A helicase assay based on the displacement of fluorescent, nucleic acid-binding ligands. Nucleic Acids Res. 24:1179-1186.
    • (1996) Nucleic Acids Res , vol.24 , pp. 1179-1186
    • Eggleston, A.K.1    Rahim, N.A.2    Kowalczykowski, S.C.3
  • 98
    • 0031470610 scopus 로고    scopus 로고
    • Recombination initiation: Easy as A, B, C, D, χ? Curr. Biol
    • Eggleston, A. K., and S. C. West. 1997. Recombination initiation: easy as A, B, C, D, χ? Curr. Biol. 7:R745-R749.
    • (1997) , vol.7
    • Eggleston, A.K.1    West, S.C.2
  • 99
    • 0017598588 scopus 로고
    • On the role of ATP in phosphodiester bond hydrolysis catalyzed by the recBC deoxyribonuclease of Escherichia coli
    • Eichler, D. C., and I. R. Lehman. 1977. On the role of ATP in phosphodiester bond hydrolysis catalyzed by the recBC deoxyribonuclease of Escherichia coli. J. Biol. Chem. 252:499-503.
    • (1977) J. Biol. Chem , vol.252 , pp. 499-503
    • Eichler, D.C.1    Lehman, I.R.2
  • 100
    • 0033374593 scopus 로고    scopus 로고
    • Characteristics of Chi distribution on different bacterial genomes
    • El Karoui, M., V. Biaudet, S. Schbath, and A. Gruss. 1999. Characteristics of Chi distribution on different bacterial genomes. Res. Microbiol. 150:579-587.
    • (1999) Res. Microbiol , vol.150 , pp. 579-587
    • El Karoui, M.1    Biaudet, V.2    Schbath, S.3    Gruss, A.4
  • 101
    • 0031929601 scopus 로고    scopus 로고
    • Identification of the lactococcal exonuclease/recombinase and its modulation by the putative Chi sequence
    • El Karoui, M., D. Ehrlich, and A. Gruss. 1998. Identification of the lactococcal exonuclease/recombinase and its modulation by the putative Chi sequence. Proc. Natl. Acad. Sci. USA 95:626-631.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 626-631
    • El Karoui, M.1    Ehrlich, D.2    Gruss, A.3
  • 102
    • 0014326203 scopus 로고
    • Recombination deficient mutants of Escherichia coli K12 that map between thyA and argA
    • Emmerson, P. T. 1968. Recombination deficient mutants of Escherichia coli K12 that map between thyA and argA. Genetics 60:19-30.
    • (1968) Genetics , vol.60 , pp. 19-30
    • Emmerson, P.T.1
  • 103
    • 0031563796 scopus 로고    scopus 로고
    • The RecBCD enzyme initiation complex for DNA unwinding: Enzyme positioning and DNA opening
    • Farah, J. A., and G. R. Smith. 1997. The RecBCD enzyme initiation complex for DNA unwinding: enzyme positioning and DNA opening. J. Mol. Biol. 272:699-715.
    • (1997) J. Mol. Biol , vol.272 , pp. 699-715
    • Farah, J.A.1    Smith, G.R.2
  • 104
    • 0031802164 scopus 로고    scopus 로고
    • Genetic recombination in Bacillus subtilis 168: Effects of recU and recS mutations on DNA repair and homologous recombination
    • Fernandez, S., A. Sorokin, and J. C. Alonso. 1998. Genetic recombination in Bacillus subtilis 168: effects of recU and recS mutations on DNA repair and homologous recombination. J. Bacteriol. 180:3405-3409.
    • (1998) J. Bacteriol , vol.180 , pp. 3405-3409
    • Fernandez, S.1    Sorokin, A.2    Alonso, J.C.3
  • 105
    • 0023047180 scopus 로고
    • Complete nucleotide sequence of recD, the structural gene for the alpha subunit of exonuclease V of Escherichia coli
    • Finch, P. W., A. Storey, K. Brown, I. D. Hickson, and P. T. Emmerson. 1986. Complete nucleotide sequence of recD, the structural gene for the alpha subunit of exonuclease V of Escherichia coli. Nucleic Acids Res. 14:8583-8594.
    • (1986) Nucleic Acids Res , vol.14 , pp. 8583-8594
    • Finch, P.W.1    Storey, A.2    Brown, K.3    Hickson, I.D.4    Emmerson, P.T.5
  • 106
    • 9244235535 scopus 로고    scopus 로고
    • Mechanism of ATP-dependent translocation of E. coli UvrD monomers along single-stranded DNA
    • Fischer, C. J., N. K. Maluf, and T. M. Lohman. 2004. Mechanism of ATP-dependent translocation of E. coli UvrD monomers along single-stranded DNA. J. Mol. Biol. 344:1287-1309.
    • (2004) J. Mol. Biol , vol.344 , pp. 1287-1309
    • Fischer, C.J.1    Maluf, N.K.2    Lohman, T.M.3
  • 107
    • 0031819593 scopus 로고    scopus 로고
    • Salt-stable complexes of the Escherichia coli RecBCD enzyme bound to double-stranded DNA
    • Gabbidon, M. R., V. E. Rampersaud, and D. A. Julin. 1998. Salt-stable complexes of the Escherichia coli RecBCD enzyme bound to double-stranded DNA. Arch. Biochem. Biophys. 350:266-272.
    • (1998) Arch. Biochem. Biophys , vol.350 , pp. 266-272
    • Gabbidon, M.R.1    Rampersaud, V.E.2    Julin, D.A.3
  • 108
    • 33750296934 scopus 로고    scopus 로고
    • Direct observation of individual RecA filaments assembling on single DNA molecules
    • Galletto, R., I. Amitani, R. J. Baskin, and S. C. Kowalczykowski. 2006. Direct observation of individual RecA filaments assembling on single DNA molecules. Nature 443:875-878.
    • (2006) Nature , vol.443 , pp. 875-878
    • Galletto, R.1    Amitani, I.2    Baskin, R.J.3    Kowalczykowski, S.C.4
  • 110
    • 0016168106 scopus 로고
    • Persistence of pyrimidine dimers during post-replication repair in ultraviolet light-irradiated Escherichia coli K12
    • Ganesan, A. K. 1974. Persistence of pyrimidine dimers during post-replication repair in ultraviolet light-irradiated Escherichia coli K12. J. Mol. Biol. 87:103-119.
    • (1974) J. Mol. Biol , vol.87 , pp. 103-119
    • Ganesan, A.K.1
  • 111
    • 0027455769 scopus 로고
    • Strand-specific binding to duplex DNA ends by the subunits of the Escherichia coli RecBCD enzyme
    • Ganesan, S., and G. R. Smith. 1993. Strand-specific binding to duplex DNA ends by the subunits of the Escherichia coli RecBCD enzyme. J. Mol. Biol. 229:67-78.
    • (1993) J. Mol. Biol , vol.229 , pp. 67-78
    • Ganesan, S.1    Smith, G.R.2
  • 112
    • 33746912768 scopus 로고    scopus 로고
    • Kinetics of ATP-stimulated nuclease activity of the Escherichia coli RecBCD enzyme
    • Ghatak, A., and D. A. Julin. 2006. Kinetics of ATP-stimulated nuclease activity of the Escherichia coli RecBCD enzyme. J. Mol. Biol. 361:954-968.
    • (2006) J. Mol. Biol , vol.361 , pp. 954-968
    • Ghatak, A.1    Julin, D.A.2
  • 113
    • 0026551842 scopus 로고
    • Identification of sbcD mutations as cosuppressors of recBC that allow propagation of DNA palindromes in Escherichia coli K-12
    • Gibson, F. P., D. R. Leach, and R. G. Lloyd. 1992. Identification of sbcD mutations as cosuppressors of recBC that allow propagation of DNA palindromes in Escherichia coli K-12. J. Bacteriol. 174:1222-1228.
    • (1992) J. Bacteriol , vol.174 , pp. 1222-1228
    • Gibson, F.P.1    Leach, D.R.2    Lloyd, R.G.3
  • 115
    • 0015522679 scopus 로고
    • Purification and properties of the recBC DNase of Escherichia coli K-12
    • Goldmark, P. J., and S. Linn. 1972. Purification and properties of the recBC DNase of Escherichia coli K-12. J. Biol. Chem. 247:1849-1860.
    • (1972) J. Biol. Chem , vol.247 , pp. 1849-1860
    • Goldmark, P.J.1    Linn, S.2
  • 116
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya, A. E., and E. V. Koonin. 1993. Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol. 3:419-429.
    • (1993) Curr. Opin. Struct. Biol , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 117
    • 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
  • 118
    • 0032571396 scopus 로고    scopus 로고
    • Site-directed mutations in motif VI of Escherichia coli DNA helicase II result in multiple biochemical defects: Evidence for the involvement of motif VI in the coupling of ATPase and DNA binding activities via conformational changes
    • Hall, M. C., A. Z. Ozsoy, and S. W. Matson. 1998. Site-directed mutations in motif VI of Escherichia coli DNA helicase II result in multiple biochemical defects: evidence for the involvement of motif VI in the coupling of ATPase and DNA binding activities via conformational changes. J. Mol. Biol. 277:257-271.
    • (1998) J. Mol. Biol , vol.277 , pp. 257-271
    • Hall, M.C.1    Ozsoy, A.Z.2    Matson, S.W.3
  • 120
    • 0013858652 scopus 로고
    • The U.V. sensitivity of bacteria: Its relation to the DNA replication cycle
    • Hanawalt, P. C. 1966. The U.V. sensitivity of bacteria: its relation to the DNA replication cycle. Photochem. Photobiol. 5:1-12.
    • (1966) Photochem. Photobiol , vol.5 , pp. 1-12
    • Hanawalt, P.C.1
  • 121
    • 14644412914 scopus 로고    scopus 로고
    • Direct visualization of RecBCD movement reveals cotranslocation of the RecD motor after χ recognition
    • Handa, N., P. R. Bianco, R. J. Baskin, and S. C. Kowalczykowski. 2005. Direct visualization of RecBCD movement reveals cotranslocation of the RecD motor after χ recognition. Mol. Cell 17:745-750.
    • (2005) Mol. Cell , vol.17 , pp. 745-750
    • Handa, N.1    Bianco, P.R.2    Baskin, R.J.3    Kowalczykowski, S.C.4
  • 122
    • 0034034023 scopus 로고    scopus 로고
    • Cellular responses to postsegregational killing by restriction-modification genes
    • Handa, N., A. Ichige, K. Kusano, and I. Kobayashi. 2000. Cellular responses to postsegregational killing by restriction-modification genes. J. Bacteriol. 182:2218-2229.
    • (2000) J. Bacteriol , vol.182 , pp. 2218-2229
    • Handa, N.1    Ichige, A.2    Kusano, K.3    Kobayashi, I.4
  • 123
    • 33845966684 scopus 로고    scopus 로고
    • A RecA mutant, RecA(730), suppresses the recombination deficiency of the RecBC(1004)D- chi* interaction in vitro and in vivo
    • Handa, N., and S. C. Kowalczykowski. 2007. A RecA mutant, RecA(730), suppresses the recombination deficiency of the RecBC(1004)D- chi* interaction in vitro and in vivo. J. Mol. Biol. 365:1314-1325.
    • (2007) J. Mol. Biol , vol.365 , pp. 1314-1325
    • Handa, N.1    Kowalczykowski, S.C.2
  • 124
    • 0031300459 scopus 로고    scopus 로고
    • Clustering of chi sequence in Escherichia coli genome
    • Handa, N., S. Ohashi, and I. Kobayashi. 1997. Clustering of chi sequence in Escherichia coli genome. Microb. Comp. Genomics 2:287-298.
    • (1997) Microb. Comp. Genomics , vol.2 , pp. 287-298
    • Handa, N.1    Ohashi, S.2    Kobayashi, I.3
  • 125
    • 0031196741 scopus 로고    scopus 로고
    • Chi-star, a chi-related 11-mer sequence partially active in an E. coli recC1004 strain
    • Handa, N., S. Ohashi, K. Kusano, and I. Kobayashi. 1997. Chi-star, a chi-related 11-mer sequence partially active in an E. coli recC1004 strain. Genes Cells 2:525-536.
    • (1997) Genes Cells , vol.2 , pp. 525-536
    • Handa, N.1    Ohashi, S.2    Kusano, K.3    Kobayashi, I.4
  • 126
    • 0032522789 scopus 로고    scopus 로고
    • RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination
    • Harmon, F. G., and S. C. Kowalczykowski. 1998. RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination. Genes Dev. 12:1134-1144.
    • (1998) Genes Dev , vol.12 , pp. 1134-1144
    • Harmon, F.G.1    Kowalczykowski, S.C.2
  • 127
    • 31844456472 scopus 로고    scopus 로고
    • Replication fork reactivation downstream of a blocked nascent leading strand
    • Heller, R. C., and K. J. Marians. 2006. Replication fork reactivation downstream of a blocked nascent leading strand. Nature 439:557-562.
    • (2006) Nature , vol.439 , pp. 557-562
    • Heller, R.C.1    Marians, K.J.2
  • 128
    • 33845330910 scopus 로고    scopus 로고
    • Replisome assembly and the direct restart of stalled replication forks
    • Heller, R. C., and K. J. Marians. 2006. Replisome assembly and the direct restart of stalled replication forks. Nat. Rev. Mol. Cell Biol. 7:932-943.
    • (2006) Nat. Rev. Mol. Cell Biol , vol.7 , pp. 932-943
    • Heller, R.C.1    Marians, K.J.2
  • 129
    • 0016810915 scopus 로고
    • The nature and origin of a class of essential gene substitutions in bacteriophage lambda
    • Henderson, D., and J. Weil. 1975. The nature and origin of a class of essential gene substitutions in bacteriophage lambda. Virology 67:124-135.
    • (1975) Virology , vol.67 , pp. 124-135
    • Henderson, D.1    Weil, J.2
  • 130
    • 0021970716 scopus 로고
    • Reconstitution of RecBC DNase activity from purified Escherichia coli RecB and RecC proteins
    • Hickson, I. D., C. N. Robson, K. E. Atkinson, L. Hutton, and P. T. Emmerson. 1985. Reconstitution of RecBC DNase activity from purified Escherichia coli RecB and RecC proteins. J. Biol. Chem. 260:1224-1229.
    • (1985) J. Biol. Chem , vol.260 , pp. 1224-1229
    • Hickson, I.D.1    Robson, C.N.2    Atkinson, K.E.3    Hutton, L.4    Emmerson, P.T.5
  • 131
    • 0015817690 scopus 로고
    • Genetic analysis of the recF pathway to genetic recombination in Escherichia coli K12: Isolation and characterization of mutants
    • Horii, Z.-I., and A. J. Clark. 1973. Genetic analysis of the recF pathway to genetic recombination in Escherichia coli K12: isolation and characterization of mutants. J. Mol. Biol. 80:327-344.
    • (1973) J. Mol. Biol , vol.80 , pp. 327-344
    • Horii, Z.-I.1    Clark, A.J.2
  • 132
    • 0015897380 scopus 로고
    • DNA repair and recombination
    • Howard-Flanders, P. 1973. DNA repair and recombination. Br. Med. Bull. 29:226-235.
    • (1973) Br. Med. Bull , vol.29 , pp. 226-235
    • Howard-Flanders, P.1
  • 133
    • 0013914280 scopus 로고
    • Mutants of Escherichia coli K-12 defective in DNA repair and in genetic recombination
    • Howard-Flanders, P., and L. Theriot. 1966. Mutants of Escherichia coli K-12 defective in DNA repair and in genetic recombination. Genetics 53:1137-1150.
    • (1966) Genetics , vol.53 , pp. 1137-1150
    • Howard-Flanders, P.1    Theriot, L.2
  • 134
    • 0026462853 scopus 로고
    • Alteration by site-directed mutagenesis of the conserved lysine residue in the consensus ATP-binding sequence of the RecB protein of Escherichia coli
    • Hsieh, S., and D. A. Julin. 1992. Alteration by site-directed mutagenesis of the conserved lysine residue in the consensus ATP-binding sequence of the RecB protein of Escherichia coli. Nucleic Acids Res. 20:5647-5653.
    • (1992) Nucleic Acids Res , vol.20 , pp. 5647-5653
    • Hsieh, S.1    Julin, D.A.2
  • 135
    • 0031686571 scopus 로고    scopus 로고
    • The premature ageing syndrome protein, WRN, is a 3′→5′ exonuclease
    • Huang, S., B. Li, M. D. Gray, J. Oshima, I. S. Mian, and J. Campisi. 1998. The premature ageing syndrome protein, WRN, is a 3′→5′ exonuclease. Nat. Genet. 20:114-116.
    • (1998) Nat. Genet , vol.20 , pp. 114-116
    • Huang, S.1    Li, B.2    Gray, M.D.3    Oshima, J.4    Mian, I.S.5    Campisi, J.6
  • 136
    • 0035371889 scopus 로고    scopus 로고
    • Single molecule nanomanipulation of biomolecules
    • Ishii, Y., A. Ishijima, and T. Yanagida. 2001. Single molecule nanomanipulation of biomolecules. Trends Biotechnol. 19:211-216.
    • (2001) Trends Biotechnol , vol.19 , pp. 211-216
    • Ishii, Y.1    Ishijima, A.2    Yanagida, T.3
  • 137
    • 0037295442 scopus 로고    scopus 로고
    • RecFOR function is required for DNA repair and recombination in a RecA loading-deficient recB mutant of Escherichia coli
    • Ivancic-Bace, I., P. Peharec, S. Moslavac, N. Skrobot, E. Salaj-Smic, and K. Brcic-Kostic. 2003. RecFOR function is required for DNA repair and recombination in a RecA loading-deficient recB mutant of Escherichia coli. Genetics 163:485-494.
    • (2003) Genetics , vol.163 , pp. 485-494
    • Ivancic-Bace, I.1    Peharec, P.2    Moslavac, S.3    Skrobot, N.4    Salaj-Smic, E.5    Brcic-Kostic, K.6
  • 138
    • 14544272738 scopus 로고    scopus 로고
    • Effects of recJ, recQ, and recFOR mutations on recombination in nuclease-deficient recB recD double mutants of Escherichia coli
    • Ivancic-Bace, I., E. Salaj-Smic, and K. Brcic-Kostic. 2005. Effects of recJ, recQ, and recFOR mutations on recombination in nuclease-deficient recB recD double mutants of Escherichia coli. J. Bacteriol. 187:1350-1356.
    • (2005) J. Bacteriol , vol.187 , pp. 1350-1356
    • Ivancic-Bace, I.1    Salaj-Smic, E.2    Brcic-Kostic, K.3
  • 139
    • 0014982055 scopus 로고
    • Usefulness of benzoylated naphthoylated DEAE-cellulose to distinguish and fractionate double-stranded DNA bearing different extents of single-stranded regions
    • Iyer, V. N., and W. D. Rupp. 1971. Usefulness of benzoylated naphthoylated DEAE-cellulose to distinguish and fractionate double-stranded DNA bearing different extents of single-stranded regions. Biochim. Biophys. Acta 228:117-126.
    • (1971) Biochim. Biophys. Acta , vol.228 , pp. 117-126
    • Iyer, V.N.1    Rupp, W.D.2
  • 140
    • 2442513338 scopus 로고    scopus 로고
    • The DNA-unwinding mechanism of the ring helicase of bacteriophage T7
    • Jeong, Y. J., M. K. Levin, and S. S. Patel. 2004. The DNA-unwinding mechanism of the ring helicase of bacteriophage T7. Proc. Natl. Acad. Sci. USA 101:7264-7269.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 7264-7269
    • Jeong, Y.J.1    Levin, M.K.2    Patel, S.S.3
  • 141
    • 0023645109 scopus 로고
    • Photoaffinity labeling of the recBCD enzyme of Escherichia coli with 8-azidoadenosine 5′- triphosphate
    • Julin, D. A., and I. R. Lehman. 1987. Photoaffinity labeling of the recBCD enzyme of Escherichia coli with 8-azidoadenosine 5′- triphosphate. J. Biol. Chem. 262:9044-9051.
    • (1987) J. Biol. Chem , vol.262 , pp. 9044-9051
    • Julin, D.A.1    Lehman, I.R.2
  • 142
    • 0036021357 scopus 로고    scopus 로고
    • Enhancement of Saccharomyces cerevisiae end-joining efficiency by cell growth stage but not by impairment of recombination
    • Karathanasis, E., and T. E. Wilson. 2002. Enhancement of Saccharomyces cerevisiae end-joining efficiency by cell growth stage but not by impairment of recombination. Genetics 161:1015-1027.
    • (2002) Genetics , vol.161 , pp. 1015-1027
    • Karathanasis, E.1    Wilson, T.E.2
  • 143
    • 0015406320 scopus 로고
    • Uncoupling of the recBC ATPase from DNase by DNA crosslinked with psoralen
    • Karu, A. E., and S. Linn. 1972. Uncoupling of the recBC ATPase from DNase by DNA crosslinked with psoralen. Proc. Natl. Acad. Sci. USA 69:2855-2859.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 2855-2859
    • Karu, A.E.1    Linn, S.2
  • 144
    • 0015839529 scopus 로고
    • The recBC deoxyribonuclease of Escherichia coli K-12. Substrate specificity and reaction intermediates
    • Karu, A. E., V. Mackay, P. J. Goldmark, and S. Linn. 1973. The recBC deoxyribonuclease of Escherichia coli K-12. Substrate specificity and reaction intermediates. J. Biol. Chem. 248:4874-4884.
    • (1973) J. Biol. Chem , vol.248 , pp. 4874-4884
    • Karu, A.E.1    Mackay, V.2    Goldmark, P.J.3    Linn, S.4
  • 145
    • 0021992965 scopus 로고
    • Mechanism of transient inhibition of DNA synthesis in ultraviolet-irradiated E. coli: Inhibition is independent of recA whilst recovery requires recA protein itself and an additional, inducible SOS function
    • Khidhir, M. A., S. Casaregola, and I. B. Holland. 1985. Mechanism of transient inhibition of DNA synthesis in ultraviolet-irradiated E. coli: inhibition is independent of recA whilst recovery requires recA protein itself and an additional, inducible SOS function. Mol. Gen. Genet. 199:133-140.
    • (1985) Mol. Gen. Genet , vol.199 , pp. 133-140
    • Khidhir, M.A.1    Casaregola, S.2    Holland, I.B.3
  • 146
    • 23744446306 scopus 로고    scopus 로고
    • Dynamic formation of RecA filaments at DNA double strand break repair centers in live cells
    • Kidane, D., and P. L. Graumann. 2005. Dynamic formation of RecA filaments at DNA double strand break repair centers in live cells. J. Cell Biol. 170:357-366.
    • (2005) J. Cell Biol , vol.170 , pp. 357-366
    • Kidane, D.1    Graumann, P.L.2
  • 147
    • 21344435463 scopus 로고    scopus 로고
    • Identification of novel restriction endonuclease-like fold families among hypothetical proteins
    • Kinch, L. N., K. Ginalski, L. Rychlewski, and N. V. Grishin. 2005. Identification of novel restriction endonuclease-like fold families among hypothetical proteins. Nucleic Acids Res. 33:3598-3605.
    • (2005) Nucleic Acids Res , vol.33 , pp. 3598-3605
    • Kinch, L.N.1    Ginalski, K.2    Rychlewski, L.3    Grishin, N.V.4
  • 148
    • 0030008328 scopus 로고    scopus 로고
    • Recombination by replication
    • Kogoma, T. 1996. Recombination by replication. Cell 85:625-627.
    • (1996) Cell , vol.85 , pp. 625-627
    • Kogoma, T.1
  • 149
    • 0030737725 scopus 로고    scopus 로고
    • Stable DNA replication: Interplay between DNA replication, homologous recombination, and transcription
    • Kogoma, T. 1997. Stable DNA replication: interplay between DNA replication, homologous recombination, and transcription. Microbiol. Mol. Biol. Rev. 61:212-238.
    • (1997) Microbiol. Mol. Biol. Rev , vol.61 , pp. 212-238
    • Kogoma, T.1
  • 150
    • 0027522361 scopus 로고
    • The Bacillus subtilis addAB genes are fully functional in Escherichia coli
    • Kooistra, J., B. J. Haijema, and G. Venema. 1993. The Bacillus subtilis addAB genes are fully functional in Escherichia coli. Mol. Microbiol. 7:915-923.
    • (1993) Mol. Microbiol , vol.7 , pp. 915-923
    • Kooistra, J.1    Haijema, B.J.2    Venema, G.3
  • 151
    • 0029079521 scopus 로고
    • Interaction with the recombination hot spot χ in vivo converts the RecBCD enzyme of Escherichia coli into a χ-independent recombinase by inactivation of the RecD subunit
    • Koppen, A., S. Krobitsch, B. Thoms, and W. Wackernagel. 1995. Interaction with the recombination hot spot χ in vivo converts the RecBCD enzyme of Escherichia coli into a χ-independent recombinase by inactivation of the RecD subunit. Proc. Natl. Acad. Sci. USA 92:6249-6253.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6249-6253
    • Koppen, A.1    Krobitsch, S.2    Thoms, B.3    Wackernagel, W.4
  • 152
    • 0026567882 scopus 로고
    • Alteration by site-directed mutagenesis of the conserved lysine residue in the ATP-binding consensus sequence of the RecD subunit of the Escherichia coli RecBCD enzyme
    • Korangy, F., and D. A. Julin. 1992. Alteration by site-directed mutagenesis of the conserved lysine residue in the ATP-binding consensus sequence of the RecD subunit of the Escherichia coli RecBCD enzyme. J. Biol. Chem. 267:1727-1732.
    • (1992) J. Biol. Chem , vol.267 , pp. 1727-1732
    • Korangy, F.1    Julin, D.A.2
  • 153
    • 0028100641 scopus 로고
    • Efficiency of ATP hydrolysis and DNA unwinding by the RecBC enzyme from Escherichia coli
    • Korangy, F., and D. A. Julin. 1994. Efficiency of ATP hydrolysis and DNA unwinding by the RecBC enzyme from Escherichia coli. Biochemistry 33:9552-9560.
    • (1994) Biochemistry , vol.33 , pp. 9552-9560
    • Korangy, F.1    Julin, D.A.2
  • 154
    • 0026564608 scopus 로고
    • Enzymatic effects of a lysine-to-glutamine mutation in the ATP-binding consensus sequence in the RecD subunit of the RecBCD enzyme from Escherichia coli
    • Korangy, F., and D. A. Julin. 1992. Enzymatic effects of a lysine-to-glutamine mutation in the ATP-binding consensus sequence in the RecD subunit of the RecBCD enzyme from Escherichia coli. J. Biol. Chem. 267:1733-1740.
    • (1992) J. Biol. Chem , vol.267 , pp. 1733-1740
    • Korangy, F.1    Julin, D.A.2
  • 155
    • 0027288130 scopus 로고
    • Kinetics and processivity of ATP hydrolysis and DNA unwinding by the RecBC enzyme from Escherichia coli
    • Korangy, F., and D. A. Julin. 1993. Kinetics and processivity of ATP hydrolysis and DNA unwinding by the RecBC enzyme from Escherichia coli. Biochemistry 32:4873-4880.
    • (1993) Biochemistry , vol.32 , pp. 4873-4880
    • Korangy, F.1    Julin, D.A.2
  • 156
    • 0026723028 scopus 로고
    • A mutation in the consensus ATP-binding sequence of the RecD subunit reduces the processivity of the RecBCD enzyme from Escherichia coli
    • Korangy, F., and D. A. Julin. 1992. A mutation in the consensus ATP-binding sequence of the RecD subunit reduces the processivity of the RecBCD enzyme from Escherichia coli. J. Biol. Chem. 267:3088-3095.
    • (1992) J. Biol. Chem , vol.267 , pp. 3088-3095
    • Korangy, F.1    Julin, D.A.2
  • 157
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • Korolev, S., J. Hsieh, G. H. Gauss, T. M. Lohman, and G. Waksman. 1997. Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP. Cell 90:635-647.
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 158
    • 0025848721 scopus 로고
    • Biochemical and biological function of Escherichia coli RecA protein: Behavior of mutant RecA proteins
    • Kowalczykowski, S. C. 1991. Biochemical and biological function of Escherichia coli RecA protein: behavior of mutant RecA proteins. Biochimie 73:289-304.
    • (1991) Biochimie , vol.73 , pp. 289-304
    • Kowalczykowski, S.C.1
  • 159
    • 0025891414 scopus 로고
    • Biochemistry of genetic recombination: Energetics and mechanism of DNA strand exchange
    • Kowalczykowski, S. C. 1991. Biochemistry of genetic recombination: energetics and mechanism of DNA strand exchange. Annu. Rev. Biophys. Biophys. Chem. 20:539-575.
    • (1991) Annu. Rev. Biophys. Biophys. Chem , vol.20 , pp. 539-575
    • Kowalczykowski, S.C.1
  • 160
    • 0034176335 scopus 로고    scopus 로고
    • Initiation of genetic recombination and recombination-dependent replication
    • Kowalczykowski, S. C. 2000. Initiation of genetic recombination and recombination-dependent replication. Trends Biochem. Sci. 25:156-165.
    • (2000) Trends Biochem. Sci , vol.25 , pp. 156-165
    • Kowalczykowski, S.C.1
  • 161
    • 0036894879 scopus 로고    scopus 로고
    • Molecular mimicry connects BRCA2 to Rad51 and recombinational DNA repair
    • Kowalczykowski, S. C. 2002. Molecular mimicry connects BRCA2 to Rad51 and recombinational DNA repair. Nat. Struct. Biol. 9:897-899.
    • (2002) Nat. Struct. Biol , vol.9 , pp. 897-899
    • Kowalczykowski, S.C.1
  • 163
    • 0016371628 scopus 로고
    • In vivo studies of temperature-sensitive recB and recC mutants
    • Kushner, S. R. 1974. In vivo studies of temperature-sensitive recB and recC mutants. J. Bacteriol. 120:1213-1218.
    • (1974) J. Bacteriol , vol.120 , pp. 1213-1218
    • Kushner, S.R.1
  • 165
    • 0028998597 scopus 로고
    • Collapse and repair of replication forks in Escherichia coli
    • Kuzminov, A. 1995. Collapse and repair of replication forks in Escherichia coli. Mol. Microbiol. 16:373-384.
    • (1995) Mol. Microbiol , vol.16 , pp. 373-384
    • Kuzminov, A.1
  • 166
    • 0035902579 scopus 로고    scopus 로고
    • DNA replication meets genetic exchange: Chromosomal damage and its repair by homologous recombination
    • Kuzminov, A. 2001. DNA replication meets genetic exchange: chromosomal damage and its repair by homologous recombination. Proc. Natl. Acad. Sci. USA 98:8461-8468.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 8461-8468
    • Kuzminov, A.1
  • 167
    • 0029347083 scopus 로고
    • Instability of inhibited replication forks in E. coli
    • Kuzminov, A. 1995. Instability of inhibited replication forks in E. coli. Bioessays 17:733-741.
    • (1995) Bioessays , vol.17 , pp. 733-741
    • Kuzminov, A.1
  • 169
    • 0032715175 scopus 로고    scopus 로고
    • Recombinational repair of DNA damage in Escherichia coli and bacteriophage λ
    • Kuzminov, A. 1999. Recombinational repair of DNA damage in Escherichia coli and bacteriophage λ. Microbiol. Mol. Biol. Rev. 63:751-813.
    • (1999) Microbiol. Mol. Biol. Rev , vol.63 , pp. 751-813
    • Kuzminov, A.1
  • 170
    • 0028176499 scopus 로고
    • Chi sites in combination with RecA protein increase the survival of linear DNA in Escherichia coli by inactivating exoV activity of RecBCD nuclease
    • Kuzminov, A., E. Schabtach, and F. W. Stahl. 1994. Chi sites in combination with RecA protein increase the survival of linear DNA in Escherichia coli by inactivating exoV activity of RecBCD nuclease. EMBO J. 13:2764-2776.
    • (1994) EMBO J , vol.13 , pp. 2764-2776
    • Kuzminov, A.1    Schabtach, E.2    Stahl, F.W.3
  • 171
    • 0031019463 scopus 로고    scopus 로고
    • Stability of linear DNA in recA mutant Escherichia coli cells reflects ongoing chromosomal DNA degradation
    • Kuzminov, A., and F. W. Stahl. 1997. Stability of linear DNA in recA mutant Escherichia coli cells reflects ongoing chromosomal DNA degradation. J. Bacteriol. 179:880-888.
    • (1997) J. Bacteriol , vol.179 , pp. 880-888
    • Kuzminov, A.1    Stahl, F.W.2
  • 172
    • 0018882511 scopus 로고
    • Assay for type II restriction endonucleases using the Escherichia coli recBC DNase and duplex circular DNA
    • Lackey, D., and S. Linn. 1980. Assay for type II restriction endonucleases using the Escherichia coli recBC DNase and duplex circular DNA. Methods Enzymol. 65:26-28.
    • (1980) Methods Enzymol , vol.65 , pp. 26-28
    • Lackey, D.1    Linn, S.2
  • 173
    • 0016198522 scopus 로고
    • Rec-mediated recombinational hot spot activity in bacteriophage lambda. II. A mutation which causes hot spot activity
    • Lam, S. T., M. M. Stahl, K. D. McMilin, and F. W. Stahl. 1974. Rec-mediated recombinational hot spot activity in bacteriophage lambda. II. A mutation which causes hot spot activity. Genetics 77:425-433.
    • (1974) Genetics , vol.77 , pp. 425-433
    • Lam, S.T.1    Stahl, M.M.2    McMilin, K.D.3    Stahl, F.W.4
  • 174
    • 0033983656 scopus 로고    scopus 로고
    • Crossover hot-spot instigator (Chi) sequences in Escherichia coli occupy distinct recombination/transcription islands
    • Lao, P. J., and D. R. Forsdyke. 2000. Crossover hot-spot instigator (Chi) sequences in Escherichia coli occupy distinct recombination/transcription islands. Gene 243:47-57.
    • (2000) Gene , vol.243 , pp. 47-57
    • Lao, P.J.1    Forsdyke, D.R.2
  • 175
    • 33845657428 scopus 로고    scopus 로고
    • UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke
    • Lee, J. Y., and W. Yang. 2006. UvrD helicase unwinds DNA one base pair at a time by a two-part power stroke. Cell 127:1349-1360.
    • (2006) Cell , vol.127 , pp. 1349-1360
    • Lee, J.Y.1    Yang, W.2
  • 176
    • 20444440763 scopus 로고    scopus 로고
    • A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase
    • Levin, M. K., M. Gurjar, and S. S. Patel. 2005. A Brownian motor mechanism of translocation and strand separation by hepatitis C virus helicase. Nat. Struct. Mol. Biol. 12:429-435.
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 429-435
    • Levin, M.K.1    Gurjar, M.2    Patel, S.S.3
  • 177
    • 0015839221 scopus 로고
    • Postreplication repair in an excision-defective mutant of Escherichia coli: Ultraviolet light-induced incorporation of bromodeoxyuridine into parental DNA
    • Ley, R. D. 1973. Postreplication repair in an excision-defective mutant of Escherichia coli: ultraviolet light-induced incorporation of bromodeoxyuridine into parental DNA. Photochem. Photobiol. 18:87-95.
    • (1973) Photochem. Photobiol , vol.18 , pp. 87-95
    • Ley, R.D.1
  • 178
    • 0015812076 scopus 로고
    • Formation of the recB-recC DNase by in vitro complementation and evidence concerning its subunit nature
    • Lieberman, R. P., and M. Oishi. 1973. Formation of the recB-recC DNase by in vitro complementation and evidence concerning its subunit nature. Nat. New Biol. 243:75-77.
    • (1973) Nat. New Biol , vol.243 , pp. 75-77
    • Lieberman, R.P.1    Oishi, M.2
  • 179
    • 0016368944 scopus 로고
    • The recBC deoxyribonuclease of Escherichia coli: Isolation and characterization of the subunit proteins and reconstitution of the enzyme
    • Lieberman, R. P., and M. Oishi. 1974. The recBC deoxyribonuclease of Escherichia coli: isolation and characterization of the subunit proteins and reconstitution of the enzyme. Proc. Natl. Acad. Sci. USA 71:4816-4820.
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 4816-4820
    • Lieberman, R.P.1    Oishi, M.2
  • 180
    • 0035956977 scopus 로고    scopus 로고
    • Comparative genomics of the restriction-modification systems in Helicobacter pylori
    • Lin, L. F., J. Posfai, R. J. Roberts, and H. Kong. 2001. Comparative genomics of the restriction-modification systems in Helicobacter pylori. Proc. Natl. Acad. Sci. USA 98:2740-2745.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2740-2745
    • Lin, L.F.1    Posfai, J.2    Roberts, R.J.3    Kong, H.4
  • 181
    • 0036434993 scopus 로고    scopus 로고
    • Subcellular localization of the Bacillus subtilis structural maintenance of chromosomes (SMC) protein
    • Lindow, J. C., M. Kuwano, S. Moriya, and A. D. Grossman. 2002. Subcellular localization of the Bacillus subtilis structural maintenance of chromosomes (SMC) protein. Mol. Microbiol. 46:997-1009.
    • (2002) Mol. Microbiol , vol.46 , pp. 997-1009
    • Lindow, J.C.1    Kuwano, M.2    Moriya, S.3    Grossman, A.D.4
  • 182
    • 0016653702 scopus 로고
    • The degradation of duplex DNA by the recBC DNase of Escherichia coli
    • Linn, S., and V. MacKay. 1975. The degradation of duplex DNA by the recBC DNase of Escherichia coli. Basic Life Sci. 5A:293-299.
    • (1975) Basic Life Sci , vol.5 A , pp. 293-299
    • Linn, S.1    MacKay, V.2
  • 183
    • 0022345185 scopus 로고
    • Identification and genetic analysis of sbcC mutations in commonly used recBC sbcB strains of Escherichia coli K-12
    • Lloyd, R. G., and C. Buckman. 1985. Identification and genetic analysis of sbcC mutations in commonly used recBC sbcB strains of Escherichia coli K-12. J. Bacteriol. 164:836-844.
    • (1985) J. Bacteriol , vol.164 , pp. 836-844
    • Lloyd, R.G.1    Buckman, C.2
  • 184
    • 0025921507 scopus 로고
    • Overlapping functions of recD, recJ and recN provide evidence of three epistatic groups of genes in Escherichia coli recombination and DNA repair
    • Lloyd, R. G., and C. Buckman. 1991. Overlapping functions of recD, recJ and recN provide evidence of three epistatic groups of genes in Escherichia coli recombination and DNA repair. Biochimie 73:313-320.
    • (1991) Biochimie , vol.73 , pp. 313-320
    • Lloyd, R.G.1    Buckman, C.2
  • 185
    • 0023915211 scopus 로고    scopus 로고
    • Lloyd, R. G., M. C. Porton, and C. Buckman. 1988. Effect of recF, recJ, recN, recO and ruv mutations on ultraviolet survival and genetic recombination in a recD strain of Escherichia coli K12. Mol. Gen. Genet. 212:317-324.
    • Lloyd, R. G., M. C. Porton, and C. Buckman. 1988. Effect of recF, recJ, recN, recO and ruv mutations on ultraviolet survival and genetic recombination in a recD strain of Escherichia coli K12. Mol. Gen. Genet. 212:317-324.
  • 186
    • 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
  • 187
    • 0021334513 scopus 로고
    • Genetic analysis of the recJ gene of Escherichia coli K-12
    • Lovett, S. T., and A. J. Clark. 1984. Genetic analysis of the recJ gene of Escherichia coli K-12. J. Bacteriol. 157:190-196.
    • (1984) J. Bacteriol , vol.157 , pp. 190-196
    • Lovett, S.T.1    Clark, A.J.2
  • 188
    • 0023790378 scopus 로고
    • The genetic dependence of recombination in recD mutants of Escherichia coli
    • Lovett, S. T., C. Luisi-DeLuca, and R. D. Kolodner. 1988. The genetic dependence of recombination in recD mutants of Escherichia coli. Genetics 120:37-45.
    • (1988) Genetics , vol.120 , pp. 37-45
    • Lovett, S.T.1    Luisi-DeLuca, C.2    Kolodner, R.D.3
  • 189
    • 2542430217 scopus 로고    scopus 로고
    • Fluorescence stopped-flow studies of single turnover kinetics of E. coli RecBCD helicase-catalyzed DNA unwinding
    • Lucius, A. L., C. J. Wong, and T. M. Lohman. 2004. Fluorescence stopped-flow studies of single turnover kinetics of E. coli RecBCD helicase-catalyzed DNA unwinding. J. Mol. Biol. 339:731-750.
    • (2004) J. Mol. Biol , vol.339 , pp. 731-750
    • Lucius, A.L.1    Wong, C.J.2    Lohman, T.M.3
  • 190
    • 2542475076 scopus 로고    scopus 로고
    • Effects of temperature and ATP on the kinetic mechanism and kinetic step-size for E.coli RecBCD helicase-catalyzed DNA unwinding
    • Lucius, A. L., and T. M. Lohman. 2004. Effects of temperature and ATP on the kinetic mechanism and kinetic step-size for E.coli RecBCD helicase-catalyzed DNA unwinding. J. Mol. Biol. 339:751-771.
    • (2004) J. Mol. Biol , vol.339 , pp. 751-771
    • Lucius, A.L.1    Lohman, T.M.2
  • 191
    • 0141865611 scopus 로고    scopus 로고
    • General methods for analysis of sequential "n-step" kinetic mechanisms: Application to single turnover kinetics of helicase-catalyzed DNA unwinding
    • Lucius, A. L., N. K. Maluf, C. J. Fischer, and T. M. Lohman. 2003. General methods for analysis of sequential "n-step" kinetic mechanisms: application to single turnover kinetics of helicase-catalyzed DNA unwinding. Biophys. J. 85:2224-2239.
    • (2003) Biophys. J , vol.85 , pp. 2224-2239
    • Lucius, A.L.1    Maluf, N.K.2    Fischer, C.J.3    Lohman, T.M.4
  • 192
    • 0021336548 scopus 로고
    • Unusual alleles of recB and recC stimulate excision of inverted repeat transposons Tn10 and Tn5
    • Lundblad, V., A. F. Taylor, G. R. Smith, and N. Kleckner. 1984. Unusual alleles of recB and recC stimulate excision of inverted repeat transposons Tn10 and Tn5. Proc. Natl. Acad. Sci. USA 81:824-828.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 824-828
    • Lundblad, V.1    Taylor, A.F.2    Smith, G.R.3    Kleckner, N.4
  • 193
    • 0035997347 scopus 로고    scopus 로고
    • The bacterial RecA protein and the recombinational DNA repair of stalled replication forks
    • Lusetti, S. L., and M. M. Cox. 2002. The bacterial RecA protein and the recombinational DNA repair of stalled replication forks. Annu. Rev. Biochem. 71:71-100.
    • (2002) Annu. Rev. Biochem , vol.71 , pp. 71-100
    • Lusetti, S.L.1    Cox, M.M.2
  • 194
    • 0016186413 scopus 로고
    • The mechanism of degradation of duplex deoxyribonucleic acid by the recBC enzyme of Escherichia coli K-12
    • MacKay, V., and S. Linn. 1974. The mechanism of degradation of duplex deoxyribonucleic acid by the recBC enzyme of Escherichia coli K-12. J. Biol. Chem. 249:4286-4294.
    • (1974) J. Biol. Chem , vol.249 , pp. 4286-4294
    • MacKay, V.1    Linn, S.2
  • 195
    • 0348225084 scopus 로고    scopus 로고
    • Is modification sufficient to protect a bacterial chromosome from a resident restriction endonuclease?
    • Makovets, S., L. M. Powell, A. J. Titheradge, G. W. Blakely, and N. E. Murray. 2004. Is modification sufficient to protect a bacterial chromosome from a resident restriction endonuclease? Mol. Microbiol. 51:135-147.
    • (2004) Mol. Microbiol , vol.51 , pp. 135-147
    • Makovets, S.1    Powell, L.M.2    Titheradge, A.J.3    Blakely, G.W.4    Murray, N.E.5
  • 196
    • 1642443168 scopus 로고    scopus 로고
    • Mechanisms of replication fork restart in Escherichia coli
    • Marians, K. J. 2004. Mechanisms of replication fork restart in Escherichia coli. Philos. Trans. R. Soc. Lond. B Biol. Sci. 359:71-77.
    • (2004) Philos. Trans. R. Soc. Lond. B Biol. Sci , vol.359 , pp. 71-77
    • Marians, K.J.1
  • 197
    • 1842317984 scopus 로고
    • Generalized transduction
    • F. Scaife, D. Leach, and A. Galizzi ed, Academic Press, London, United Kingdom
    • Masters, M. 1985. Generalized transduction, p. 197-215. In F. Scaife, D. Leach, and A. Galizzi (ed.), Genetics of bacteria. Academic Press, London, United Kingdom.
    • (1985) Genetics of bacteria , pp. 197-215
    • Masters, M.1
  • 198
    • 0026628341 scopus 로고
    • Reconstitution of the activities of the RecBCD holoenzyme of Escherichia coli from the purified subunits
    • Masterson, C., P. E. Boehmer, F. McDonald, S. Chaudhuri, I. D. Hickson, and P. T. Emmerson. 1992. Reconstitution of the activities of the RecBCD holoenzyme of Escherichia coli from the purified subunits. J. Biol. Chem. 267:13564-13572.
    • (1992) J. Biol. Chem , vol.267 , pp. 13564-13572
    • Masterson, C.1    Boehmer, P.E.2    McDonald, F.3    Chaudhuri, S.4    Hickson, I.D.5    Emmerson, P.T.6
  • 199
    • 0021071027 scopus 로고
    • The gene 4 protein of bacteriophage T7. Characterization of helicase activity
    • Matson, S. W., S. Tabor, and C. C. Richardson. 1983. The gene 4 protein of bacteriophage T7. Characterization of helicase activity. J. Biol. Chem. 258:14017-14024.
    • (1983) J. Biol. Chem , vol.258 , pp. 14017-14024
    • Matson, S.W.1    Tabor, S.2    Richardson, C.C.3
  • 200
    • 4544262040 scopus 로고    scopus 로고
    • The type I and III restriction endonucleases: Structural elements in molecular motors that process DNA
    • A. Pingoud ed, Springer, Berlin, Germany
    • McClelland, S. E., and M. D. Szczelkun. 2004. The type I and III restriction endonucleases: structural elements in molecular motors that process DNA, p. 111-132. In A. Pingoud (ed.), Restriction endonucleases. Springer, Berlin, Germany.
    • (2004) Restriction endonucleases , pp. 111-132
    • McClelland, S.E.1    Szczelkun, M.D.2
  • 201
    • 0036683338 scopus 로고    scopus 로고
    • Genome stability and the processing of damaged replication forks by RecG
    • McGlynn, P., and R. G. Lloyd. 2002. Genome stability and the processing of damaged replication forks by RecG. Trends Genet. 18:413-419.
    • (2002) Trends Genet , vol.18 , pp. 413-419
    • McGlynn, P.1    Lloyd, R.G.2
  • 202
    • 0034737294 scopus 로고    scopus 로고
    • Modulation of RNA polymerase by (p)ppGpp reveals a RecG-dependent mechanism for replication fork progression
    • McGlynn, P., and R. G. Lloyd. 2000. Modulation of RNA polymerase by (p)ppGpp reveals a RecG-dependent mechanism for replication fork progression. Cell 101:35-45.
    • (2000) Cell , vol.101 , pp. 35-45
    • McGlynn, P.1    Lloyd, R.G.2
  • 203
    • 0036844340 scopus 로고    scopus 로고
    • Recombinational repair and restart of damaged replication forks
    • McGlynn, P., and R. G. Lloyd. 2002. Recombinational repair and restart of damaged replication forks. Nat. Rev. Mol. Cell Biol. 3:859-870.
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 859-870
    • McGlynn, P.1    Lloyd, R.G.2
  • 204
    • 50049090597 scopus 로고    scopus 로고
    • Constitutive SOS expression and damage-inducible AddAB-mediated recombinational repair systems for Coxiella burnetii as potential adaptations for survival within macrophages
    • Mertens, K., L. Lantsheer, D. G. Ennis, and J. E. Samuel. 2008. Constitutive SOS expression and damage-inducible AddAB-mediated recombinational repair systems for Coxiella burnetii as potential adaptations for survival within macrophages. Mol. Microbiol. 69:1411-1426.
    • (2008) Mol. Microbiol , vol.69 , pp. 1411-1426
    • Mertens, K.1    Lantsheer, L.2    Ennis, D.G.3    Samuel, J.E.4
  • 208
    • 0037398332 scopus 로고    scopus 로고
    • Chromosomal lesion suppression and removal in Escherichia coli via linear DNA degradation
    • Miranda, A., and A. Kuzminov. 2003. Chromosomal lesion suppression and removal in Escherichia coli via linear DNA degradation. Genetics 163:1255-1271.
    • (2003) Genetics , vol.163 , pp. 1255-1271
    • Miranda, A.1    Kuzminov, A.2
  • 209
    • 0025300179 scopus 로고
    • Interconversion of replication and recombination structures: Implications for terminal repeats and concatemers
    • Morgan, A. R., and A. Severini. 1990. Interconversion of replication and recombination structures: implications for terminal repeats and concatemers. J. Theor. Biol. 144:195-202.
    • (1990) J. Theor. Biol , vol.144 , pp. 195-202
    • Morgan, A.R.1    Severini, A.2
  • 210
    • 0034681305 scopus 로고    scopus 로고
    • Bacteriophage P22 Abc2 protein binds to RecC increases the 5′ strand nicking activity of RecBCD and together with lambda bet, promotes Chi-independent recombination
    • Murphy, K. C. 2000. Bacteriophage P22 Abc2 protein binds to RecC increases the 5′ strand nicking activity of RecBCD and together with lambda bet, promotes Chi-independent recombination. J. Mol. Biol. 296:385-401.
    • (2000) J. Mol. Biol , vol.296 , pp. 385-401
    • Murphy, K.C.1
  • 211
    • 0025925181 scopus 로고
    • Lambda Gam protein inhibits the helicase and Chi-stimulated recombination activities of Escherichia coli RecBCD enzyme
    • Murphy, K. C. 1991. Lambda Gam protein inhibits the helicase and Chi-stimulated recombination activities of Escherichia coli RecBCD enzyme. J. Bacteriol. 173:5808-5821.
    • (1991) J. Bacteriol , vol.173 , pp. 5808-5821
    • Murphy, K.C.1
  • 212
    • 0029037763 scopus 로고
    • The recombination hot spot χ activates RecBCD recombination by converting Escherichia coli to a recD mutant phenocopy
    • Myers, R. S., A. Kuzminov, and F. W. Stahl. 1995. The recombination hot spot χ activates RecBCD recombination by converting Escherichia coli to a recD mutant phenocopy. Proc. Natl. Acad. Sci. USA 92:6244-6248.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6244-6248
    • Myers, R.S.1    Kuzminov, A.2    Stahl, F.W.3
  • 213
    • 0028566106 scopus 로고
    • Chi and the RecBC D enzyme of Escherichia coli
    • Myers, R. S., and F. W. Stahl. 1994. Chi and the RecBC D enzyme of Escherichia coli. Annu. Rev. Genet. 28:49-70.
    • (1994) Annu. Rev. Genet , vol.28 , pp. 49-70
    • Myers, R.S.1    Stahl, F.W.2
  • 214
    • 0028971616 scopus 로고
    • Chi recombination activity in phage lambda decays as a function of genetic distance
    • Myers, R. S., M. M. Stahl, and F. W. Stahl. 1995. Chi recombination activity in phage lambda decays as a function of genetic distance. Genetics 141:805-812.
    • (1995) Genetics , vol.141 , pp. 805-812
    • Myers, R.S.1    Stahl, M.M.2    Stahl, F.W.3
  • 215
    • 0021185614 scopus 로고
    • Isolation and genetic characterization of a thymineless death-resistant mutant of Escherichia coli K-12: Identification of a new mutation (recQ1) that blocks the recF recombination pathway
    • Nakayama, H., K. Nakayama, R. Nakayama, N. Irino, Y. Nakayama, and P. C. Hanawalt. 1984. Isolation and genetic characterization of a thymineless death-resistant mutant of Escherichia coli K-12: identification of a new mutation (recQ1) that blocks the recF recombination pathway. Mol. Gen. Genet. 195:474-480.
    • (1984) Mol. Gen. Genet , vol.195 , pp. 474-480
    • Nakayama, H.1    Nakayama, K.2    Nakayama, R.3    Irino, N.4    Nakayama, Y.5    Hanawalt, P.C.6
  • 216
    • 0015266288 scopus 로고
    • Adenosine triphosphatase associated with adenosine triphosphate-dependent deoxyribonuclease (recB-recC enzyme-E. coli-ATP to phosphodiester hydrolysis ratio-DNA-dependent ATPase activity)
    • Nobrega, F. G., F. H. Rola, M. Pasetto-Nobrega, and M. Oishi. 1972. Adenosine triphosphatase associated with adenosine triphosphate-dependent deoxyribonuclease (recB-recC enzyme-E. coli-ATP to phosphodiester hydrolysis ratio-DNA-dependent ATPase activity). Proc. Natl. Acad. Sci. USA 69:15-19.
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 15-19
    • Nobrega, F.G.1    Rola, F.H.2    Pasetto-Nobrega, M.3    Oishi, M.4
  • 217
    • 0014649255 scopus 로고
    • An ATP-dependent deoxyribonuclease from E. coli with a possible role in genetic recombination
    • Oishi, M. 1969. An ATP-dependent deoxyribonuclease from E. coli with a possible role in genetic recombination. Proc. Natl. Acad. Sci. USA 64:1292-1299.
    • (1969) Proc. Natl. Acad. Sci. USA , vol.64 , pp. 1292-1299
    • Oishi, M.1
  • 218
    • 2942637828 scopus 로고    scopus 로고
    • The Werner syndrome helicase and exonuclease cooperate to resolve telomeric D-loops in a manner regulated by TRF1 and TRF2
    • Opresko, P. L., M. Otterlei, J. Graakjaer, P. Bruheim, L. Dawut, S. Kolvraa, A. May, M. M. Seidman, and V. A. Bohr. 2004. The Werner syndrome helicase and exonuclease cooperate to resolve telomeric D-loops in a manner regulated by TRF1 and TRF2. Mol. Cell 14:763-774.
    • (2004) Mol. Cell , vol.14 , pp. 763-774
    • Opresko, P.L.1    Otterlei, M.2    Graakjaer, J.3    Bruheim, P.4    Dawut, L.5    Kolvraa, S.6    May, A.7    Seidman, M.M.8    Bohr, V.A.9
  • 219
    • 0025231804 scopus 로고
    • Biochemical and physical characterization of exonuclease V from Escherichia coli. Comparison of the catalytic activities of the RecBC and RecBCD enzymes
    • Palas, K. M., and S. R. Kushner. 1990. Biochemical and physical characterization of exonuclease V from Escherichia coli. Comparison of the catalytic activities of the RecBC and RecBCD enzymes. J. Biol. Chem. 265:3447-3454.
    • (1990) J. Biol. Chem , vol.265 , pp. 3447-3454
    • Palas, K.M.1    Kushner, S.R.2
  • 220
    • 0038799991 scopus 로고    scopus 로고
    • Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae
    • Pâques, F., and J. E. Haber. 1999. Multiple pathways of recombination induced by double-strand breaks in Saccharomyces cerevisiae. Microbiol. Mol. Biol. Rev. 63:349-404.
    • (1999) Microbiol. Mol. Biol. Rev , vol.63 , pp. 349-404
    • Pâques, F.1    Haber, J.E.2
  • 221
    • 34548359230 scopus 로고    scopus 로고
    • Single-molecule fluorescence to study molecular motors
    • Park, H., E. Toprak, and P. R. Selvin. 2007. Single-molecule fluorescence to study molecular motors. Q. Rev. Biophys. 40:87-111.
    • (2007) Q. Rev. Biophys , vol.40 , pp. 87-111
    • Park, H.1    Toprak, E.2    Selvin, P.R.3
  • 223
    • 1542375262 scopus 로고    scopus 로고
    • Forward and reverse motion of single RecBCD molecules on DNA
    • Perkins, T. T., H. W. Li, R. V. Dalal, J. Gelles, and S. M. Block. 2004. Forward and reverse motion of single RecBCD molecules on DNA. Biophys. J. 86:1640-1648.
    • (2004) Biophys. J , vol.86 , pp. 1640-1648
    • Perkins, T.T.1    Li, H.W.2    Dalal, R.V.3    Gelles, J.4    Block, S.M.5
  • 224
    • 0030977227 scopus 로고    scopus 로고
    • The RecB protein of Escherichia coli translocates along single-stranded DNA in the 3′ to 5′ direction: A proposed ratchet mechanism
    • Phillips, R. J., D. C. Hickleton, P. E. Boehmer, and P. T. Emmerson. 1997. The RecB protein of Escherichia coli translocates along single-stranded DNA in the 3′ to 5′ direction: a proposed ratchet mechanism. Mol. Gen. Genet. 254:319-329.
    • (1997) Mol. Gen. Genet , vol.254 , pp. 319-329
    • Phillips, R.J.1    Hickleton, D.C.2    Boehmer, P.E.3    Emmerson, P.T.4
  • 225
    • 0021807208 scopus 로고
    • Chi-dependent DNA strand cleavage by RecBC enzyme
    • Ponticelli, A. S., D. W. Schultz, A. F. Taylor, and G. R. Smith. 1985. Chi-dependent DNA strand cleavage by RecBC enzyme. Cell 41:145-151.
    • (1985) Cell , vol.41 , pp. 145-151
    • Ponticelli, A.S.1    Schultz, D.W.2    Taylor, A.F.3    Smith, G.R.4
  • 227
    • 0034971260 scopus 로고    scopus 로고
    • In vivo evidence for two active nuclease motifs in the double-strand break repair enzyme RexAB of Lactococcus lactis
    • Quiberoni, A., I. Biswas, M. El Karoui, L. Rezaiki, P. Tailliez, and A. Gruss. 2001. In vivo evidence for two active nuclease motifs in the double-strand break repair enzyme RexAB of Lactococcus lactis. J. Bacteriol. 183:4071-4078.
    • (2001) J. Bacteriol , vol.183 , pp. 4071-4078
    • Quiberoni, A.1    Biswas, I.2    El Karoui, M.3    Rezaiki, L.4    Tailliez, P.5    Gruss, A.6
  • 228
    • 0035103540 scopus 로고    scopus 로고
    • Distinctive features of homologous recombination in an 'old' microorganism, Lactococcus lactis
    • Quiberoni, A., L. Rezaiki, M. El Karoui, I. Biswas, P. Tailliez, and A. Gruss. 2001. Distinctive features of homologous recombination in an 'old' microorganism, Lactococcus lactis. Res. Microbiol. 152:131-139.
    • (2001) Res. Microbiol , vol.152 , pp. 131-139
    • Quiberoni, A.1    Rezaiki, L.2    El Karoui, M.3    Biswas, I.4    Tailliez, P.5    Gruss, A.6
  • 230
    • 25444473121 scopus 로고    scopus 로고
    • RecD plays an essential function during growth at low temperature in the Antarctic bacterium Pseudomonas syringae Lz4W
    • Regha, K., A. K. Satapathy, and M. K. Ray. 2005. RecD plays an essential function during growth at low temperature in the Antarctic bacterium Pseudomonas syringae Lz4W. Genetics 170:1473-1484.
    • (2005) Genetics , vol.170 , pp. 1473-1484
    • Regha, K.1    Satapathy, A.K.2    Ray, M.K.3
  • 231
    • 0022360935 scopus 로고    scopus 로고
    • Register, J. C., III, and J. Griffith. 1985. The direction of RecA protein assembly onto single strand DNA is the same as the direction of strand assimilation during strand exchange. J. Biol. Chem. 260:12308-12312.
    • Register, J. C., III, and J. Griffith. 1985. The direction of RecA protein assembly onto single strand DNA is the same as the direction of strand assimilation during strand exchange. J. Biol. Chem. 260:12308-12312.
  • 232
    • 23944518444 scopus 로고    scopus 로고
    • An inactivated nuclease-like domain in RecC with novel function: Implications for evolution
    • Rigden, D. J. 2005. An inactivated nuclease-like domain in RecC with novel function: implications for evolution. BMC Struct. Biol. 5:9.
    • (2005) BMC Struct. Biol , vol.5 , pp. 9
    • Rigden, D.J.1
  • 233
    • 0026516821 scopus 로고
    • Inhibition of the recBCD-dependent activation of Chi recombinational hot spots in SOS-induced cells of Escherichia coli
    • Rinken, R., and W. Wackernagel. 1992. Inhibition of the recBCD-dependent activation of Chi recombinational hot spots in SOS-induced cells of Escherichia coli. J. Bacteriol. 174:1172- 1178.
    • (1992) J. Bacteriol , vol.174 , pp. 1172-1178
    • Rinken, R.1    Wackernagel, W.2
  • 234
    • 0030633568 scopus 로고    scopus 로고
    • RecA protein: Structure, function, and role in recombinational DNA repair
    • Roca, A. I., and M. M. Cox. 1997. RecA protein: structure, function, and role in recombinational DNA repair. Prog. Nucleic Acid Res. Mol. Biol. 56:129-223.
    • (1997) Prog. Nucleic Acid Res. Mol. Biol , vol.56 , pp. 129-223
    • Roca, A.I.1    Cox, M.M.2
  • 235
    • 55449115425 scopus 로고    scopus 로고
    • Comparative and evolutionary analysis of the bacterial homologous recombination systems
    • Rocha, E. P., E. Cornet, and B. Michel. 2005. Comparative and evolutionary analysis of the bacterial homologous recombination systems. PLoS Genet. 1:e15.
    • (2005) PLoS Genet , vol.1
    • Rocha, E.P.1    Cornet, E.2    Michel, B.3
  • 236
    • 0026351806 scopus 로고
    • RecBCD-dependent joint molecule formation promoted by the Escherichia coli RecA and SSB proteins
    • Roman, L. J., D. A. Dixon, and S. C. Kowalczykowski. 1991. RecBCD-dependent joint molecule formation promoted by the Escherichia coli RecA and SSB proteins. Proc. Natl. Acad. Sci. USA 88:3367-3371.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3367-3371
    • Roman, L.J.1    Dixon, D.A.2    Kowalczykowski, S.C.3
  • 237
    • 0026673415 scopus 로고
    • Processivity of the DNA helicase activity of Escherichia coli recBCD enzyme
    • Roman, L. J., A. K. Eggleston, and S. C. Kowalczykowski. 1992. Processivity of the DNA helicase activity of Escherichia coli recBCD enzyme. J. Biol. Chem. 267:4207-4214.
    • (1992) J. Biol. Chem , vol.267 , pp. 4207-4214
    • Roman, L.J.1    Eggleston, A.K.2    Kowalczykowski, S.C.3
  • 238
    • 0024565799 scopus 로고
    • Characterization of the adenosinetriphosphatase activity of the Escherichia coli RecBCD enzyme: Relationship of ATP hydrolysis to the unwinding of duplex DNA
    • Roman, L. J., and S. C. Kowalczykowski. 1989. Characterization of the adenosinetriphosphatase activity of the Escherichia coli RecBCD enzyme: relationship of ATP hydrolysis to the unwinding of duplex DNA. Biochemistry 28:2873-2881.
    • (1989) Biochemistry , vol.28 , pp. 2873-2881
    • Roman, L.J.1    Kowalczykowski, S.C.2
  • 239
    • 0024512057 scopus 로고
    • Characterization of the helicase activity of the Escherichia coli RecBCD enzyme using a novel helicase assay
    • Roman, L. J., and S. C. Kowalczykowski. 1989. Characterization of the helicase activity of the Escherichia coli RecBCD enzyme using a novel helicase assay. Biochemistry 28:2863-2873.
    • (1989) Biochemistry , vol.28 , pp. 2863-2873
    • Roman, L.J.1    Kowalczykowski, S.C.2
  • 240
    • 0024443524 scopus 로고
    • Formation of heteroduplex DNA promoted by the combined activities of Escherichia coli RecA and RecBCD proteins
    • Roman, L. J., and S. C. Kowalczykowski. 1989. Formation of heteroduplex DNA promoted by the combined activities of Escherichia coli RecA and RecBCD proteins. J. Biol. Chem. 264:18340-18348.
    • (1989) J. Biol. Chem , vol.264 , pp. 18340-18348
    • Roman, L.J.1    Kowalczykowski, S.C.2
  • 241
    • 0018357909 scopus 로고
    • Mechanisms of action of the type-I restriction endonuclease EcoB and the RecBC DNase from E. coli
    • Rosamond, J., B. Endlich, K. M. Telander, and S. Linn. 1979. Mechanisms of action of the type-I restriction endonuclease EcoB and the RecBC DNase from E. coli. Cold Spring Harb. Symp. Quant. Biol. 43:1049-1057.
    • (1979) Cold Spring Harb. Symp. Quant. Biol , vol.43 , pp. 1049-1057
    • Rosamond, J.1    Endlich, B.2    Telander, K.M.3    Linn, S.4
  • 243
    • 0017650847 scopus 로고
    • Defective excision and postreplication repair of UV-damaged DNA in a recL mutant strain of E. coli K-12
    • Rothman, R. H., and A. J. Clark. 1977. Defective excision and postreplication repair of UV-damaged DNA in a recL mutant strain of E. coli K-12. Mol. Gen. Genet. 155:267-277.
    • (1977) Mol. Gen. Genet , vol.155 , pp. 267-277
    • Rothman, R.H.1    Clark, A.J.2
  • 244
    • 0017689807 scopus 로고
    • The dependence of postreplication repair on uvrB in a recF mutant of Escherichia coli K-12
    • Rothman, R. H., and A. J. Clark. 1977. The dependence of postreplication repair on uvrB in a recF mutant of Escherichia coli K-12. Mol. Gen. Genet. 155:279-286.
    • (1977) Mol. Gen. Genet , vol.155 , pp. 279-286
    • Rothman, R.H.1    Clark, A.J.2
  • 245
    • 0016604384 scopus 로고
    • The beginning of an investigation of the role of recF in the pathways of metabolism of ultraviolet-irradiated DNA in Escherichia coli
    • Rothman, R. H., T. Kato, and A. J. Clark. 1975. The beginning of an investigation of the role of recF in the pathways of metabolism of ultraviolet-irradiated DNA in Escherichia coli. Basic Life Sci. 5A:283-291.
    • (1975) Basic Life Sci , vol.5 A , pp. 283-291
    • Rothman, R.H.1    Kato, T.2    Clark, A.J.3
  • 246
    • 0014432520 scopus 로고
    • Discontinuities in the DNA synthesized in an excision-defective strain of Escherichia coli following ultraviolet irradiation
    • Rupp, W. D., and P. Howard-Flanders. 1968. Discontinuities in the DNA synthesized in an excision-defective strain of Escherichia coli following ultraviolet irradiation. J. Mol. Biol. 31:291-304.
    • (1968) J. Mol. Biol , vol.31 , pp. 291-304
    • Rupp, W.D.1    Howard-Flanders, P.2
  • 248
    • 0034123356 scopus 로고    scopus 로고
    • Multiple genetic pathways for restarting DNA replication forks in Escherichia coli K-12
    • Sandler, S. J. 2000. Multiple genetic pathways for restarting DNA replication forks in Escherichia coli K-12. Genetics 155:487-497.
    • (2000) Genetics , vol.155 , pp. 487-497
    • Sandler, S.J.1
  • 249
    • 0020599039 scopus 로고
    • Escherichia coli RecBC pseudorevertants lacking Chi recombinational hotspot activity
    • Schultz, D. W., A. F. Taylor, and G. R. Smith. 1983. Escherichia coli RecBC pseudorevertants lacking Chi recombinational hotspot activity. J. Bacteriol. 155:664-680.
    • (1983) J. Bacteriol , vol.155 , pp. 664-680
    • Schultz, D.W.1    Taylor, A.F.2    Smith, G.R.3
  • 250
    • 0032582794 scopus 로고    scopus 로고
    • RuvAB acts at arrested replication forks
    • Seigneur, M., V. Bidnenko, S. D. Ehrlich, and B. Michel. 1998. RuvAB acts at arrested replication forks. Cell 95:419-430.
    • (1998) Cell , vol.95 , pp. 419-430
    • Seigneur, M.1    Bidnenko, V.2    Ehrlich, S.D.3    Michel, B.4
  • 251
    • 34447520500 scopus 로고    scopus 로고
    • Effect of a recD mutation on DNA damage resistance and transformation in Deinococcus radiodurans
    • Servinsky, M. D., and D. A. Julin. 2007. Effect of a recD mutation on DNA damage resistance and transformation in Deinococcus radiodurans. J. Bacteriol. 189:5101-5107.
    • (2007) J. Bacteriol , vol.189 , pp. 5101-5107
    • Servinsky, M.D.1    Julin, D.A.2
  • 252
    • 0028269715 scopus 로고
    • Study of the structure of replicative intermediates of HSV-1 DNA by pulsed-field gel electrophoresis
    • Severini, A., A. R. Morgan, D. R. Tovell, and D. L. Tyrrell. 1994. Study of the structure of replicative intermediates of HSV-1 DNA by pulsed-field gel electrophoresis. Virology 200:428-435.
    • (1994) Virology , vol.200 , pp. 428-435
    • Severini, A.1    Morgan, A.R.2    Tovell, D.R.3    Tyrrell, D.L.4
  • 253
    • 0000133316 scopus 로고
    • Purified Escherichia coli recA protein catalyzes homologous pairing of superhelical DNA and single-stranded fragments
    • Shibata, T., C. DasGupta, R. P. Cunningham, and C. M. Radding. 1979. Purified Escherichia coli recA protein catalyzes homologous pairing of superhelical DNA and single-stranded fragments. Proc. Natl. Acad. Sci. USA 76:1638-1642.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 1638-1642
    • Shibata, T.1    DasGupta, C.2    Cunningham, R.P.3    Radding, C.M.4
  • 254
    • 35348890199 scopus 로고    scopus 로고
    • Bacterial DNA repair by nonhomologous end joining
    • Shuman, S., and M. S. Glickman. 2007. Bacterial DNA repair by nonhomologous end joining. Nat. Rev. Microbiol. 5:852-861.
    • (2007) Nat. Rev. Microbiol , vol.5 , pp. 852-861
    • Shuman, S.1    Glickman, M.S.2
  • 255
    • 0017133690 scopus 로고
    • T4 DNA injection. II. Protection of entering DNA from host exonuclease V
    • Silverstein, J. L., and E. B. Goldberg. 1976. T4 DNA injection. II. Protection of entering DNA from host exonuclease V. Virology 72:212-223.
    • (1976) Virology , vol.72 , pp. 212-223
    • Silverstein, J.L.1    Goldberg, E.B.2
  • 256
    • 0015419143 scopus 로고
    • Degradation of bacteriophage lambda deoxyribonucleic acid after restriction by Escherichia coli K-12
    • Simmon, V. F., and S. Lederberg. 1972. Degradation of bacteriophage lambda deoxyribonucleic acid after restriction by Escherichia coli K-12. J. Bacteriol. 112:161-169.
    • (1972) J. Bacteriol , vol.112 , pp. 161-169
    • Simmon, V.F.1    Lederberg, S.2
  • 257
  • 258
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton, M. R., M. S. Dillingham, and D. B. Wigley. 2007. Structure and mechanism of helicases and nucleic acid translocases. Annu. Rev. Biochem. 76:23-50.
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 259
    • 0035812836 scopus 로고    scopus 로고
    • Structural analysis of DNA replication fork reversal by RecG
    • Singleton, M. R., S. Scaife, and D. B. Wigley. 2001. Structural analysis of DNA replication fork reversal by RecG. Cell 107:79-89.
    • (2001) Cell , vol.107 , pp. 79-89
    • Singleton, M.R.1    Scaife, S.2    Wigley, D.B.3
  • 260
    • 0036211179 scopus 로고    scopus 로고
    • Modularity and specialization in superfamily 1 and 2 helicases
    • Singleton, M. R., and D. B. Wigley. 2002. Modularity and specialization in superfamily 1 and 2 helicases. J. Bacteriol. 184:1819-1826.
    • (2002) J. Bacteriol , vol.184 , pp. 1819-1826
    • Singleton, M.R.1    Wigley, D.B.2
  • 261
    • 0002050661 scopus 로고
    • A replicator's view of recombination (and repair)
    • R. F. Grell ed, Plenum Press, New York, NY
    • Skalka, A. 1974. A replicator's view of recombination (and repair), p. 421-432. In R. F. Grell (ed.), Mechanisms in recombination. Plenum Press, New York, NY.
    • (1974) Mechanisms in recombination , pp. 421-432
    • Skalka, A.1
  • 262
    • 0025967320 scopus 로고
    • Conjugational recombination in Escherichia coli: Myths and mechanisms
    • Smith, G. R. 1991. Conjugational recombination in Escherichia coli: myths and mechanisms. Cell 64:19-27.
    • (1991) Cell , vol.64 , pp. 19-27
    • Smith, G.R.1
  • 263
    • 0035671854 scopus 로고    scopus 로고
    • Homologous recombination near and far from DNA breaks: Alternative roles and contrasting views
    • Smith, G. R. 2001. Homologous recombination near and far from DNA breaks: alternative roles and contrasting views. Annu. Rev. Genet. 35:243-274.
    • (2001) Annu. Rev. Genet , vol.35 , pp. 243-274
    • Smith, G.R.1
  • 264
    • 0019457036 scopus 로고
    • Structure of Chi hotspots of generalized recombination
    • Smith, G. R., S. M. Kunes, D. W. Schultz, A. Taylor, and K. L. Triman. 1981. Structure of Chi hotspots of generalized recombination. Cell 24:429-436.
    • (1981) Cell , vol.24 , pp. 429-436
    • Smith, G.R.1    Kunes, S.M.2    Schultz, D.W.3    Taylor, A.4    Triman, K.L.5
  • 265
    • 0033516596 scopus 로고    scopus 로고
    • DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase
    • Soultanas, P., M. S. Dillingham, S. S. Velankar, and D. B. Wigley. 1999. DNA binding mediates conformational changes and metal ion coordination in the active site of PcrA helicase. J. Mol. Biol. 290:137-148.
    • (1999) J. Mol. Biol , vol.290 , pp. 137-148
    • Soultanas, P.1    Dillingham, M.S.2    Velankar, S.S.3    Wigley, D.B.4
  • 267
    • 36049052525 scopus 로고    scopus 로고
    • RecBCD enzyme switches lead motor subunits in response to χ recognition
    • Spies, M., I. Amitani, R. J. Baskin, and S. C. Kowalczykowski. 2007. RecBCD enzyme switches lead motor subunits in response to χ recognition. Cell 131:694-705.
    • (2007) Cell , vol.131 , pp. 694-705
    • Spies, M.1    Amitani, I.2    Baskin, R.J.3    Kowalczykowski, S.C.4
  • 268
    • 0141540814 scopus 로고    scopus 로고
    • A molecular throttle: The recombination hotspot χ controls DNA translocation by the RecBCD helicase
    • Spies, M., P. R. Bianco, M. S. Dillingham, N. Handa, R. J. Baskin, and S. C. Kowalczykowski. 2003. A molecular throttle: the recombination hotspot χ controls DNA translocation by the RecBCD helicase. Cell 114:647-654.
    • (2003) Cell , vol.114 , pp. 647-654
    • Spies, M.1    Bianco, P.R.2    Dillingham, M.S.3    Handa, N.4    Baskin, R.J.5    Kowalczykowski, S.C.6
  • 269
    • 27744497422 scopus 로고    scopus 로고
    • Translocation by the RecB motor is an absolute requirement for χ-recognition and RecA protein loading by RecBCD enzyme
    • Spies, M., M. S. Dillingham, and S. C. Kowalczykowski. 2005. Translocation by the RecB motor is an absolute requirement for χ-recognition and RecA protein loading by RecBCD enzyme. J. Biol. Chem. 280:37078- 37087.
    • (2005) J. Biol. Chem , vol.280 , pp. 37078-37087
    • Spies, M.1    Dillingham, M.S.2    Kowalczykowski, S.C.3
  • 270
    • 27744535816 scopus 로고    scopus 로고
    • Homologous recombination by RecBCD and RecF pathways
    • N. P. Higgins ed, ASM Press, Washington, DC
    • Spies, M., and S. C. Kowalczykowski. 2005. Homologous recombination by RecBCD and RecF pathways, p. 389-403. In N. P. Higgins (ed.), The bacterial chromosome. ASM Press, Washington, DC.
    • (2005) The bacterial chromosome , pp. 389-403
    • Spies, M.1    Kowalczykowski, S.C.2
  • 271
    • 32444451553 scopus 로고    scopus 로고
    • The RecA binding locus of RecBCD is a general domain for recruitment of DNA strand exchange proteins
    • Spies, M., and S. C. Kowalczykowski. 2006. The RecA binding locus of RecBCD is a general domain for recruitment of DNA strand exchange proteins. Mol. Cell 21:573-580.
    • (2006) Mol. Cell , vol.21 , pp. 573-580
    • Spies, M.1    Kowalczykowski, S.C.2
  • 272
    • 0018230936 scopus 로고
    • A single base-pair change creates a Chi recombinational hotspot in bacteriophage lambda
    • Sprague, K. U., D. H. Faulds, and G. R. Smith. 1978. A single base-pair change creates a Chi recombinational hotspot in bacteriophage lambda. Proc. Natl. Acad. Sci. USA 75:6182-6186.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 6182-6186
    • Sprague, K.U.1    Faulds, D.H.2    Smith, G.R.3
  • 273
    • 22144474444 scopus 로고    scopus 로고
    • Chi: A little sequence controls a big enzyme
    • Stahl, F. W. 2005. Chi: a little sequence controls a big enzyme. Genetics 170:487-493.
    • (2005) Genetics , vol.170 , pp. 487-493
    • Stahl, F.W.1
  • 274
    • 0016809728 scopus 로고
    • Rec-mediated recombinational hot spot activity in bacteriophage lambda. IV. Effect of heterology on Chi-stimulated crossing over
    • Stahl, F. W., and M. M. Stahl. 1975. Rec-mediated recombinational hot spot activity in bacteriophage lambda. IV. Effect of heterology on Chi-stimulated crossing over. Mol. Gen. Genet. 140:29-37.
    • (1975) Mol. Gen. Genet , vol.140 , pp. 29-37
    • Stahl, F.W.1    Stahl, M.M.2
  • 275
    • 0016200336 scopus 로고
    • A role for recBC nuclease in the distribution of crossovers along unreplicated chromosomes of phage lambda
    • Stahl, F. W., and M. M. Stahl. 1974. A role for recBC nuclease in the distribution of crossovers along unreplicated chromosomes of phage lambda. Mol. Gen. Genet. 131:27-30.
    • (1974) Mol. Gen. Genet , vol.131 , pp. 27-30
    • Stahl, F.W.1    Stahl, M.M.2
  • 276
    • 0018980111 scopus 로고
    • Directionality and nonreciprocality of Chi-stimulated recombination in phage lambda
    • Stahl, F. W., M. M. Stahl, R. E. Malone, and J. M. Crasemann. 1980. Directionality and nonreciprocality of Chi-stimulated recombination in phage lambda. Genetics 94:235-248.
    • (1980) Genetics , vol.94 , pp. 235-248
    • Stahl, F.W.1    Stahl, M.M.2    Malone, R.E.3    Crasemann, J.M.4
  • 277
    • 0025009867 scopus 로고
    • Further tests of a recombination model in which Chi removes the RecD subunit from the RecBCD enzyme of Escherichia coli
    • Stahl, F. W., L. C. Thomason, I. Siddiqi, and M. M. Stahl. 1990. Further tests of a recombination model in which Chi removes the RecD subunit from the RecBCD enzyme of Escherichia coli. Genetics 126:519-533.
    • (1990) Genetics , vol.126 , pp. 519-533
    • Stahl, F.W.1    Thomason, L.C.2    Siddiqi, I.3    Stahl, M.M.4
  • 278
    • 27744540194 scopus 로고    scopus 로고
    • Coupling of two motor proteins: A new motor can move faster
    • Stukalin, E. B., H. Phillips III, and A. B. Kolomeisky. 2005. Coupling of two motor proteins: a new motor can move faster. Phys. Rev. Lett. 94:238101.
    • (2005) Phys. Rev. Lett , vol.94 , pp. 238101
    • Stukalin, E.B.1    Phillips III, H.2    Kolomeisky, A.B.3
  • 279
    • 30144432572 scopus 로고    scopus 로고
    • The nuclease domain of the Escherichia coli RecBCD enzyme catalyzes degradation of linear and circular single-stranded and double-stranded DNA
    • Sun, J. Z., D. A. Julin, and J. S. Hu. 2006. The nuclease domain of the Escherichia coli RecBCD enzyme catalyzes degradation of linear and circular single-stranded and double-stranded DNA. Biochemistry 45:131-140.
    • (2006) Biochemistry , vol.45 , pp. 131-140
    • Sun, J.Z.1    Julin, D.A.2    Hu, J.S.3
  • 280
    • 0036900120 scopus 로고    scopus 로고
    • Role of RAD52 epistasis group genes in homologous recombination and double-strand break repair
    • Symington, L. S. 2002. Role of RAD52 epistasis group genes in homologous recombination and double-strand break repair. Microbiol. Mol. Biol. Rev. 66:630-670.
    • (2002) Microbiol. Mol. Biol. Rev , vol.66 , pp. 630-670
    • Symington, L.S.1
  • 281
    • 0037065729 scopus 로고    scopus 로고
    • Kinetic models of translocation, head-on collision, and DNA cleavage by type I restriction endonucleases
    • Szczelkun, M. D. 2002. Kinetic models of translocation, head-on collision, and DNA cleavage by type I restriction endonucleases. Biochemistry 41:2067-2074.
    • (2002) Biochemistry , vol.41 , pp. 2067-2074
    • Szczelkun, M.D.1
  • 282
    • 0020541955 scopus 로고
    • The double-strand-break repair model for recombination
    • Szostak, J. W., T. L. Orr-Weaver, R. J. Rothstein, and F. W. Stahl. 1983. The double-strand-break repair model for recombination. Cell 33:25-35.
    • (1983) Cell , vol.33 , pp. 25-35
    • Szostak, J.W.1    Orr-Weaver, T.L.2    Rothstein, R.J.3    Stahl, F.W.4
  • 283
    • 0015527124 scopus 로고
    • 5′-oligonucleotides as the acid-soluble products of the ATP-dependent DNase form Escherichia coli
    • Tanner, D., F. G. Nobrega, and M. Oishi. 1972. 5′-oligonucleotides as the acid-soluble products of the ATP-dependent DNase form Escherichia coli. J. Mol. Biol. 67:513-516.
    • (1972) J. Mol. Biol , vol.67 , pp. 513-516
    • Tanner, D.1    Nobrega, F.G.2    Oishi, M.3
  • 284
    • 0344985828 scopus 로고
    • Unwinding and rewinding of DNA by exonuclease V
    • B. Alberts and C. F. Fox ed, Academic Press, New York, NY
    • Taylor, A., and G. R. Smith. 1980. Unwinding and rewinding of DNA by exonuclease V, p. 909-919. In B. Alberts and C. F. Fox (ed.), Mechanistic studies of DNA replication and genetic recombination, vol. 19. Academic Press, New York, NY.
    • (1980) Mechanistic studies of DNA replication and genetic recombination , vol.19 , pp. 909-919
    • Taylor, A.1    Smith, G.R.2
  • 285
    • 0019158176 scopus 로고
    • Unwinding and rewinding of DNA by the RecBC enzyme
    • Taylor, A., and G. R. Smith. 1980. Unwinding and rewinding of DNA by the RecBC enzyme. Cell 22:447-457.
    • (1980) Cell , vol.22 , pp. 447-457
    • Taylor, A.1    Smith, G.R.2
  • 286
    • 0002098916 scopus 로고
    • The RecBCD enzyme of Escherichia coli
    • R. Kucherlapati and G. R. Smith ed, American Society for Microbiology, Washington, DC
    • Taylor, A. F. 1988. The RecBCD enzyme of Escherichia coli, p. 231-263. In R. Kucherlapati and G. R. Smith (ed.), Genetic recombination. American Society for Microbiology, Washington, DC.
    • (1988) Genetic recombination , pp. 231-263
    • Taylor, A.F.1
  • 287
    • 0021839175 scopus 로고
    • RecBC enzyme nicking at Chi sites during DNA unwinding: Location and orientation-dependence of the cutting
    • Taylor, A. F., D. W. Schultz, A. S. Ponticelli, and G. R. Smith. 1985. RecBC enzyme nicking at Chi sites during DNA unwinding: location and orientation-dependence of the cutting. Cell 41:153-163.
    • (1985) Cell , vol.41 , pp. 153-163
    • Taylor, A.F.1    Schultz, D.W.2    Ponticelli, A.S.3    Smith, G.R.4
  • 288
    • 0028810980 scopus 로고
    • Monomeric RecBCD enzyme binds and unwinds DNA
    • Taylor, A. F., and G. R. Smith. 1995. Monomeric RecBCD enzyme binds and unwinds DNA. J. Biol. Chem. 270:24451-24458.
    • (1995) J. Biol. Chem , vol.270 , pp. 24451-24458
    • Taylor, A.F.1    Smith, G.R.2
  • 289
    • 0037698985 scopus 로고    scopus 로고
    • RecBCD enzyme is a DNA helicase with fast and slow motors of opposite polarity
    • Taylor, A. F., and G. R. Smith. 2003. RecBCD enzyme is a DNA helicase with fast and slow motors of opposite polarity. Nature 423:889-893.
    • (2003) Nature , vol.423 , pp. 889-893
    • Taylor, A.F.1    Smith, G.R.2
  • 290
    • 0026720049 scopus 로고
    • RecBCD enzyme is altered upon cutting DNA at a Chi recombination hotspot
    • Taylor, A. F., and G. R. Smith. 1992. RecBCD enzyme is altered upon cutting DNA at a Chi recombination hotspot. Proc. Natl. Acad. Sci. USA 89:5226-5230.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5226-5230
    • Taylor, A.F.1    Smith, G.R.2
  • 291
    • 0033119729 scopus 로고    scopus 로고
    • Regulation of homologous recombination: Chi inactivates RecBCD enzyme by disassembly of the three subunits
    • Taylor, A. F., and G. R. Smith. 1999. Regulation of homologous recombination: Chi inactivates RecBCD enzyme by disassembly of the three subunits. Genes Dev. 13:890-900.
    • (1999) Genes Dev , vol.13 , pp. 890-900
    • Taylor, A.F.1    Smith, G.R.2
  • 292
    • 0028802635 scopus 로고
    • Strand specificity of nicking of DNA at Chi sites by RecBCD enzyme: Modulation by ATP and magnesium levels
    • Taylor, A. F., and G. R. Smith. 1995. Strand specificity of nicking of DNA at Chi sites by RecBCD enzyme: modulation by ATP and magnesium levels. J. Biol. Chem. 270:24459-24467.
    • (1995) J. Biol. Chem , vol.270 , pp. 24459-24467
    • Taylor, A.F.1    Smith, G.R.2
  • 293
    • 0022181381 scopus 로고
    • Substrate specificity of the DNA unwinding activity of the RecBC enzyme of Escherichia coli
    • Taylor, A. F., and G. R. Smith. 1985. Substrate specificity of the DNA unwinding activity of the RecBC enzyme of Escherichia coli. J. Mol. Biol. 185:431-443.
    • (1985) J. Mol. Biol , vol.185 , pp. 431-443
    • Taylor, A.F.1    Smith, G.R.2
  • 294
    • 57349198529 scopus 로고    scopus 로고
    • Telander-Muskavitch, K. M., and S. Linn. 1980. Electron microscopy of E. coli recBC enzyme reaction intermediates, p. 901-918. In B. Alberts (ed.), Mechanistic studies of DNA replication and genetic recombination, 19. Academic Press, New York, NY.
    • Telander-Muskavitch, K. M., and S. Linn. 1980. Electron microscopy of E. coli recBC enzyme reaction intermediates, p. 901-918. In B. Alberts (ed.), Mechanistic studies of DNA replication and genetic recombination, vol. 19. Academic Press, New York, NY.
  • 295
    • 0020048680 scopus 로고
    • A unified mechanism for the nuclease and unwinding activities of the recBC enzyme of Escherichia coli
    • Telander-Muskavitch, K. M., and S. Linn. 1982. A unified mechanism for the nuclease and unwinding activities of the recBC enzyme of Escherichia coli. J. Biol. Chem. 257:2641-2648.
    • (1982) J. Biol. Chem , vol.257 , pp. 2641-2648
    • Telander-Muskavitch, K.M.1    Linn, S.2
  • 296
    • 0001457105 scopus 로고
    • A hypothesis: Chi-activation of recBCD enzyme involves removal of the recD subunit
    • E. C. Friedberg and P. C. Hanawalt ed, Alan R. Liss, Inc, New York, NY
    • Thaler, D. S., E. Sampson, I. Siddiqi, S. M. Rosenberg, F. W. Stahl, and M. Stahl. 1988. A hypothesis: Chi-activation of recBCD enzyme involves removal of the recD subunit, p. 413-422. In E. C. Friedberg and P. C. Hanawalt (ed.), Mechanisms and consequences of DNA damage processing. Alan R. Liss, Inc., New York, NY.
    • (1988) Mechanisms and consequences of DNA damage processing , pp. 413-422
    • Thaler, D.S.1    Sampson, E.2    Siddiqi, I.3    Rosenberg, S.M.4    Stahl, F.W.5    Stahl, M.6
  • 298
    • 37549057335 scopus 로고    scopus 로고
    • + strains of Escherichia coli and roles of SbcB15 and XonA2 ExoI mutant enzymes. J. Bacteriol. 190:179-192.
    • + strains of Escherichia coli and roles of SbcB15 and XonA2 ExoI mutant enzymes. J. Bacteriol. 190:179-192.
  • 299
    • 0031794968 scopus 로고    scopus 로고
    • Interaction of RecBCD enzyme with DNA at double-strand breaks produced in UV-irradiated Escherichia coli: Requirement for DNA end processing
    • Thoms, B., and W. Wackernagel. 1998. Interaction of RecBCD enzyme with DNA at double-strand breaks produced in UV-irradiated Escherichia coli: requirement for DNA end processing. J. Bacteriol. 180:5639- 5645.
    • (1998) J. Bacteriol , vol.180 , pp. 5639-5645
    • Thoms, B.1    Wackernagel, W.2
  • 300
    • 0033935187 scopus 로고    scopus 로고
    • The contributions of replication orientation, gene direction, and signal sequences to base-composition asymmetries in bacterial genomes
    • Tillier, E. R., and R. A. Collins. 2000. The contributions of replication orientation, gene direction, and signal sequences to base-composition asymmetries in bacterial genomes. J. Mol. Evol. 50:249-257.
    • (2000) J. Mol. Evol , vol.50 , pp. 249-257
    • Tillier, E.R.1    Collins, R.A.2
  • 301
    • 0015496023 scopus 로고
    • Structural genes of ATP-dependent deoxyribonuclease of Escherichia coli
    • Tomizawa, J., and H. Ogawa. 1972. Structural genes of ATP-dependent deoxyribonuclease of Escherichia coli. Nat. New Biol. 239:14-16.
    • (1972) Nat. New Biol , vol.239 , pp. 14-16
    • Tomizawa, J.1    Ogawa, H.2
  • 302
    • 34247602963 scopus 로고    scopus 로고
    • A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA
    • Tomko, E. J., C. J. Fischer, A. Niedziela-Majka, and T. M. Lohman. 2007. A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA. Mol. Cell 26:335-347.
    • (2007) Mol. Cell , vol.26 , pp. 335-347
    • Tomko, E.J.1    Fischer, C.J.2    Niedziela-Majka, A.3    Lohman, T.M.4
  • 303
    • 0031586127 scopus 로고    scopus 로고
    • The recombination hot spot Chi is embedded within islands of preferred DNA pairing sequences in the E. coli genome
    • Tracy, R. B., F. Chédin, and S. C. Kowalczykowski. 1997. The recombination hot spot Chi is embedded within islands of preferred DNA pairing sequences in the E. coli genome. Cell 90:205-206.
    • (1997) Cell , vol.90 , pp. 205-206
    • Tracy, R.B.1    Chédin, F.2    Kowalczykowski, S.C.3
  • 304
    • 0034707195 scopus 로고    scopus 로고
    • The orientation bias of Chi sequences is a general tendency of G-rich oligomers
    • Uno, R., Y. Nakayama, K. Arakawa, and M. Tomita. 2000. The orientation bias of Chi sequences is a general tendency of G-rich oligomers. Gene 259:207-215.
    • (2000) Gene , vol.259 , pp. 207-215
    • Uno, R.1    Nakayama, Y.2    Arakawa, K.3    Tomita, M.4
  • 305
    • 33747884625 scopus 로고    scopus 로고
    • Over-representation of Chi sequences caused by di-codon increase in Escherichia coli K-12
    • Uno, R., Y. Nakayama, and M. Tomita. 2006. Over-representation of Chi sequences caused by di-codon increase in Escherichia coli K-12. Gene 380:30-37.
    • (2006) Gene , vol.380 , pp. 30-37
    • Uno, R.1    Nakayama, Y.2    Tomita, M.3
  • 306
    • 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
  • 307
    • 0034703487 scopus 로고    scopus 로고
    • A novel mutational hotspot in a natural quasipalindrome in Escherichia coli
    • Viswanathan, M., J. J. Lacirignola, R. L. Hurley, and S. T. Lovett. 2000. A novel mutational hotspot in a natural quasipalindrome in Escherichia coli. J. Mol. Biol. 302:553-564.
    • (2000) J. Mol. Biol , vol.302 , pp. 553-564
    • Viswanathan, M.1    Lacirignola, J.J.2    Hurley, R.L.3    Lovett, S.T.4
  • 308
    • 0015928150 scopus 로고
    • Genetic transformation in E. coli: The inhibitory role of the recBC DNase
    • Wackernagel, W. 1973. Genetic transformation in E. coli: the inhibitory role of the recBC DNase. Biochem. Biophys. Res. Commun. 51:306-311.
    • (1973) Biochem. Biophys. Res. Commun , vol.51 , pp. 306-311
    • Wackernagel, W.1
  • 309
    • 0034614654 scopus 로고    scopus 로고
    • A single nuclease active site of the Escherichia coli RecBCD enzyme catalyzes single-stranded DNA degradation in both directions
    • Wang, J., R. Chen, and D. A. Julin. 2000. A single nuclease active site of the Escherichia coli RecBCD enzyme catalyzes single-stranded DNA degradation in both directions. J. Biol. Chem. 275:507-513.
    • (2000) J. Biol. Chem , vol.275 , pp. 507-513
    • Wang, J.1    Chen, R.2    Julin, D.A.3
  • 310
    • 10644241539 scopus 로고    scopus 로고
    • DNA helicase activity of the RecD protein from Deinococcus radiodurans
    • Wang, J., and D. A. Julin. 2004. DNA helicase activity of the RecD protein from Deinococcus radiodurans. J. Biol. Chem. 279:52024-52032.
    • (2004) J. Biol. Chem , vol.279 , pp. 52024-52032
    • Wang, J.1    Julin, D.A.2
  • 311
    • 0021364455 scopus 로고
    • recF-dependent and recF recB-independent DNA gap-filling repair processes transfer dimer-containing parental strands to daughter strands in Escherichia coli K-12 uvrB
    • Wang, T.-C. V., and K. C. Smith. 1984. recF-dependent and recF recB-independent DNA gap-filling repair processes transfer dimer-containing parental strands to daughter strands in Escherichia coli K-12 uvrB. J. Bacteriol. 158:727-729.
    • (1984) J. Bacteriol , vol.158 , pp. 727-729
    • Wang, T.-C.V.1    Smith, K.C.2
  • 313
    • 0017130522 scopus 로고
    • Mechanism of DNA degradation by the ATP-dependent DNase from Hemophilus influenzae Rd
    • Wilcox, K. W., and H. O. Smith. 1976. Mechanism of DNA degradation by the ATP-dependent DNase from Hemophilus influenzae Rd. J. Biol. Chem. 251:6127-6134.
    • (1976) J. Biol. Chem , vol.251 , pp. 6127-6134
    • Wilcox, K.W.1    Smith, H.O.2
  • 314
    • 0014512023 scopus 로고
    • + strains of Escherichia coli K-12 mutant at recA, recB, or recC
    • + strains of Escherichia coli K-12 mutant at recA, recB, or recC. J. Bacteriol. 98:599-604.
    • (1969) J. Bacteriol , vol.98 , pp. 599-604
    • Wilkins, B.M.1
  • 315
    • 0014347219 scopus 로고
    • The genetic properties of DNA transferred from ultraviolet-irradiated Hfr cells of Escherichia coli K-12 during mating
    • Wilkins, B. M., and P. Howard-Flanders. 1968. The genetic properties of DNA transferred from ultraviolet-irradiated Hfr cells of Escherichia coli K-12 during mating. Genetics 60:243-255.
    • (1968) Genetics , vol.60 , pp. 243-255
    • Wilkins, B.M.1    Howard-Flanders, P.2
  • 316
    • 0014599009 scopus 로고
    • Genetic analysis of recombination-deficient mutants of Escherichia coli K-12 carrying rec mutations cotransducible with thyA
    • Willetts, N. S., and D. W. Mount. 1969. Genetic analysis of recombination-deficient mutants of Escherichia coli K-12 carrying rec mutations cotransducible with thyA. J. Bacteriol. 100:923-934.
    • (1969) J. Bacteriol , vol.100 , pp. 923-934
    • Willetts, N.S.1    Mount, D.W.2
  • 317
    • 0019410048 scopus 로고
    • Partial purification and properties of an exonuclease inhibitor induced by bacteriophage Mu-1
    • Williams, J. G., and C. M. Radding. 1981. Partial purification and properties of an exonuclease inhibitor induced by bacteriophage Mu-1. J. Virol. 39:548-558.
    • (1981) J. Virol , vol.39 , pp. 548-558
    • Williams, J.G.1    Radding, C.M.2
  • 318
    • 0037308590 scopus 로고    scopus 로고
    • Non-homologous end-joining: Bacteria join the chromosome breakdance
    • Wilson, T. E., L. M. Topper, and P. L. Palmbos. 2003. Non-homologous end-joining: bacteria join the chromosome breakdance. Trends Biochem. Sci. 28:62-66.
    • (2003) Trends Biochem. Sci , vol.28 , pp. 62-66
    • Wilson, T.E.1    Topper, L.M.2    Palmbos, P.L.3
  • 319
    • 0023428773 scopus 로고
    • Recovery from ultraviolet light-induced inhibition of DNA synthesis requires umuDC gene products in recA718 mutant strains but not in recA+ strains of Escherichia coli
    • Witkin, E. M., V. Roegner-Maniscalco, J. B. Sweasy, and J. O. McCall. 1987. Recovery from ultraviolet light-induced inhibition of DNA synthesis requires umuDC gene products in recA718 mutant strains but not in recA+ strains of Escherichia coli. Proc. Natl. Acad. Sci. USA 84:6805-6809.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6805-6809
    • Witkin, E.M.1    Roegner-Maniscalco, V.2    Sweasy, J.B.3    McCall, J.O.4
  • 320
    • 24644435846 scopus 로고    scopus 로고
    • Energetics of DNA end binding by E. coli RecBC and RecBCD helicases indicate loop formation in the 3′-single-stranded DNA tail
    • Wong, C. J., A. L. Lucius, and T. M. Lohman. 2005. Energetics of DNA end binding by E. coli RecBC and RecBCD helicases indicate loop formation in the 3′-single-stranded DNA tail. J. Mol. Biol. 352:765-782.
    • (2005) J. Mol. Biol , vol.352 , pp. 765-782
    • Wong, C.J.1    Lucius, A.L.2    Lohman, T.M.3
  • 321
    • 18244428198 scopus 로고
    • Mechanisms of enzyme degradation of bacterial chromosomes and their regulation
    • In French
    • Wright, M., and G. Buttin. 1969. Mechanisms of enzyme degradation of bacterial chromosomes and their regulation. Bull. Soc. Chim. Biol. (Paris) 51:1373-1383. (In French.)
    • (1969) Bull. Soc. Chim. Biol. (Paris) , vol.51 , pp. 1373-1383
    • Wright, M.1    Buttin, G.2
  • 322
    • 0015149052 scopus 로고
    • The isolation and characterization from Escherichia coli of an adenosine triphosphate-dependent deoxyribonuclease directed by recB,C genes
    • Wright, M., G. Buttin, and J. Hurwitz. 1971. The isolation and characterization from Escherichia coli of an adenosine triphosphate-dependent deoxyribonuclease directed by recB,C genes. J. Biol. Chem. 246:6543-6555.
    • (1971) J. Biol. Chem , vol.246 , pp. 6543-6555
    • Wright, M.1    Buttin, G.2    Hurwitz, J.3
  • 323
    • 0037134454 scopus 로고    scopus 로고
    • A dynamic RecA filament permits DNA polymerase-catalyzed extension of the invading strand in recombination intermediates
    • Xu, L., and K. J. Marians. 2002. A dynamic RecA filament permits DNA polymerase-catalyzed extension of the invading strand in recombination intermediates. J. Biol. Chem. 277:14321-14328.
    • (2002) J. Biol. Chem , vol.277 , pp. 14321-14328
    • Xu, L.1    Marians, K.J.2
  • 324
    • 34447095032 scopus 로고    scopus 로고
    • A dual-nuclease mechanism for DNA break processing by AddAB-type helicase-nucleases
    • Yeeles, J. T., and M. S. Dillingham. 2007. A dual-nuclease mechanism for DNA break processing by AddAB-type helicase-nucleases. J. Mol. Biol. 371:66-78.
    • (2007) J. Mol. Biol , vol.371 , pp. 66-78
    • Yeeles, J.T.1    Dillingham, M.S.2
  • 325
    • 0032477911 scopus 로고    scopus 로고
    • The 30-kDa C-terminal domain of the RecB protein is critical for the nuclease activity, but not the helicase activity, of the RecBCD enzyme from Escherichia coli
    • Yu, M., J. Souaya, and D. A. Julin. 1998. The 30-kDa C-terminal domain of the RecB protein is critical for the nuclease activity, but not the helicase activity, of the RecBCD enzyme from Escherichia coli. Proc. Natl. Acad. Sci. USA 95:981-986.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 981-986
    • Yu, M.1    Souaya, J.2    Julin, D.A.3
  • 326
    • 0032491378 scopus 로고    scopus 로고
    • Identification of the nuclease active site in the multifunctional RecBCD enzyme by creation of a chimeric enzyme
    • Yu, M., J. Souaya, and D. A. Julin. 1998. Identification of the nuclease active site in the multifunctional RecBCD enzyme by creation of a chimeric enzyme. J. Mol. Biol. 283:797-808.
    • (1998) J. Mol. Biol , vol.283 , pp. 797-808
    • Yu, M.1    Souaya, J.2    Julin, D.A.3
  • 327
    • 0345034772 scopus 로고    scopus 로고
    • Isolation and characterization of the C-terminal nuclease domain from the RecB protein of Escherichia coli
    • Zhang, X. J., and D. A. Julin. 1999. Isolation and characterization of the C-terminal nuclease domain from the RecB protein of Escherichia coli. Nucleic Acids Res. 27:4200-4207.
    • (1999) Nucleic Acids Res , vol.27 , pp. 4200-4207
    • Zhang, X.J.1    Julin, D.A.2
  • 328
    • 34247844641 scopus 로고    scopus 로고
    • A new role of Deinococcus radiodurans RecD in antioxidant pathway
    • Zhou, Q., X. Zhang, H. Xu, B. Xu, and Y. Hua. 2007. A new role of Deinococcus radiodurans RecD in antioxidant pathway. FEMS Microbiol. Lett. 271:118-125.
    • (2007) FEMS Microbiol. Lett , vol.271 , pp. 118-125
    • Zhou, Q.1    Zhang, X.2    Xu, H.3    Xu, B.4    Hua, Y.5
  • 329
    • 9244236007 scopus 로고    scopus 로고
    • The recombination genes addAB are not restricted to gram-positive bacteria: Genetic analysis of the recombination initiation enzymes RecF and AddAB in Rhizobium etli
    • Zuniga-Castillo, J., D. Romero, and J. M. Martinez-Salazar. 2004. The recombination genes addAB are not restricted to gram-positive bacteria: genetic analysis of the recombination initiation enzymes RecF and AddAB in Rhizobium etli. J. Bacteriol. 186:7905-7913.
    • (2004) J. Bacteriol , vol.186 , pp. 7905-7913
    • Zuniga-Castillo, J.1    Romero, D.2    Martinez-Salazar, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.