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Volumn 432, Issue 7014, 2004, Pages 187-193

Crystal structure of RecBCD enzyme reveals a machine for processing DNA breaks

Author keywords

[No Author keywords available]

Indexed keywords

CRYSTAL STRUCTURE; DNA; SUBSTRATES;

EID: 9144271294     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/nature02988     Document Type: Article
Times cited : (351)

References (50)
  • 1
    • 0034176335 scopus 로고    scopus 로고
    • Initiation of genetic recombination and recombination-dependent replication
    • Kowalczykowski, S. C. Initiation of genetic recombination and recombination-dependent replication. Trends. Biochem. Sci. 25, 156-165 (2000).
    • (2000) Trends. Biochem. Sci. , vol.25 , pp. 156-165
    • Kowalczykowski, S.C.1
  • 2
    • 0021807208 scopus 로고
    • Chi-dependent DNA strand cleavage by the RecBC enzyme
    • Ponticelli, A. S., Schultz, D. W., Taylor, A. F. & Smith, G. R. Chi-dependent DNA strand cleavage by the RecBC enzyme. Cell 41, 145-151 (1985).
    • (1985) Cell , vol.41 , pp. 145-151
    • Ponticelli, A.S.1    Schultz, D.W.2    Taylor, A.F.3    Smith, G.R.4
  • 3
    • 0021839175 scopus 로고
    • RecBC enzyme nicking at Chi sites during DNA unwinding: Location and orientation-dependence of the cutting
    • Taylor, A. F., Schultz, D. W., Ponticelli, A. S. & Smith, G. R. RecBC enzyme nicking at Chi sites during DNA unwinding: location and orientation-dependence of the cutting, Cell 41, 153-163 (1985).
    • (1985) Cell , vol.41 , pp. 153-163
    • Taylor, A.F.1    Schultz, D.W.2    Ponticelli, A.S.3    Smith, G.R.4
  • 4
    • 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. B. & Kowalczykowski, S. C. 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).
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6706-6711
    • Bianco, P.B.1    Kowalczykowski, S.C.2
  • 5
    • 0141540814 scopus 로고    scopus 로고
    • A molecular throttle: The recombination hotspot Chi controls DNA translocation by the RecBCD helicase
    • Spies, M. et al. A molecular throttle: the recombination hotspot Chi controls DNA translocation by the RecBCD helicase. Cell 114, 647-654 (2003).
    • (2003) Cell , vol.114 , pp. 647-654
    • Spies, M.1
  • 6
    • 0027511858 scopus 로고
    • The recombination hotspot Chi is a regulatory sequence that acts by attenuating the nuclease activity of the E. coli RecBCD enzyme
    • Dixon, D. A. & Kowalczykowski, S. C. The recombination hotspot Chi is a regulatory sequence that acts by attenuating the nuclease activity of the E. coli RecBCD enzyme. Cell 73, 87-96 (1993).
    • (1993) Cell , vol.73 , pp. 87-96
    • Dixon, D.A.1    Kowalczykowski, S.C.2
  • 7
    • 0030969429 scopus 로고    scopus 로고
    • The recombination hot spot Chi is a regulatory element that switches the polarity of DNA degradation by the RecBCD enzyme
    • Anderson, D. G. & Kowalczykowski, S. C. The recombination hot spot Chi is a regulatory element that switches the polarity of DNA degradation by the RecBCD enzyme. Genes Dev. 11, 571-581 (1997a).
    • (1997) Genes Dev. , vol.11 , pp. 571-581
    • Anderson, D.G.1    Kowalczykowski, S.C.2
  • 8
    • 0028802635 scopus 로고
    • Strand specificity of nicking of DNA at Chi sites by RecBCD enzyme
    • Taylor, A. F. & Smith, G. R. Strand specificity of nicking of DNA at Chi sites by RecBCD enzyme. J. Biol. Chem. 270, 24459-24467 (1995b).
    • (1995) J. Biol. Chem. , vol.270 , pp. 24459-24467
    • Taylor, A.F.1    Smith, G.R.2
  • 9
    • 0031444642 scopus 로고    scopus 로고
    • The translocating RecBCD enzyme stimulates recombination by directing RecA protein onto ssDNA in a Chi-regulated manner
    • Anderson, D. G. & Kowalczykowski, S. C. The translocating RecBCD enzyme stimulates recombination by directing RecA protein onto ssDNA in a Chi-regulated manner. Cell 90, 77-86 (1997b).
    • (1997) Cell , vol.90 , pp. 77-86
    • Anderson, D.G.1    Kowalczykowski, S.C.2
  • 10
    • 0028810980 scopus 로고
    • Monomeric RecBCD enzyme binds and unwinds DNA
    • Taylor, A. F. & Smith, G. R. Monomeric RecBCD enzyme binds and unwinds DNA. J. Biol. Chem. 270, 24451-24458 (1995a).
    • (1995) J. Biol. Chem. , vol.270 , pp. 24451-24458
    • Taylor, A.F.1    Smith, G.R.2
  • 11
    • 0025864481 scopus 로고
    • Escherichia coli RecBCD enzyme: Inducible overproduction and reconstitution of the ATP-dependent deoxyribonuclease from purified subunits
    • Boehmer, P. E. & Emmerson, P. T. Escherichia coli RecBCD enzyme: inducible overproduction and reconstitution of the ATP-dependent deoxyribonuclease from purified subunits. Gene 102, 1-6 (1991).
    • (1991) Gene , vol.102 , pp. 1-6
    • Boehmer, P.E.1    Emmerson, P.T.2
  • 12
    • 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., Souaya, J. & Julin, D. A. 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).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 981-986
    • Yu, M.1    Souaya, J.2    Julin, D.A.3
  • 13
    • 0031196741 scopus 로고    scopus 로고
    • Chi*, a chi-related 11-mer sequence partially active in an E. coli recC 1004 strain
    • Handa, N., Ohashi, S., Kusano, K. & Kobayashi, I. Chi*, a chi-related 11-mer sequence partially active in an E. coli recC1004 strain. Genes Cells 2, 525-536 (1997).
    • (1997) Genes Cells , vol.2 , pp. 525-536
    • Handa, N.1    Ohashi, S.2    Kusano, K.3    Kobayashi, I.4
  • 14
  • 15
    • 0037698985 scopus 로고    scopus 로고
    • RecBCD enzyme is a DNA helicase with fast and slow motors of opposite polarity
    • Taylor, A. F. & Smith, G. R. RecBCD enzyme is a DNA helicase with fast and slow motors of opposite polarity. Nature 423, 889-893 (2003).
    • (2003) Nature , vol.423 , pp. 889-893
    • Taylor, A.F.1    Smith, G.R.2
  • 16
    • 0024565799 scopus 로고
    • Characterisation of the adenosinetriphosphatase activity of the Escherichia coli RecBCD enzyme: Relationship of ATP hydrolysis to the unwinding of duplex DNA
    • Roman, L. J. & Kowakzykowski, S. C. Characterisation 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).
    • (1989) Biochemistry , vol.28 , pp. 2873-2881
    • Roman, L.J.1    Kowakzykowski, S.C.2
  • 17
    • 0027455769 scopus 로고
    • Strand-specific binding to duplex DNA ends by the subunits of the Escherichia coli RecBCD enzyme
    • Ganesan, S. & Smith, G. R. Strand-specific binding to duplex DNA ends by the subunits of the Escherichia coli RecBCD enzyme. J. Mol. Biol. 229, 67-78 (1993).
    • (1993) J. Mol. Biol. , vol.229 , pp. 67-78
    • Ganesan, S.1    Smith, G.R.2
  • 18
    • 0031563796 scopus 로고    scopus 로고
    • The RecBCD enzyme initiation complex for DNA unwinding: Enzyme positioning and DNA opening
    • Farah, J. A. & Smith, G. R. The RecBCD enzyme initiation complex for DNA unwinding: enzyme positioning and DNA opening. J. Mol. Biol. 272, 699-715 (1997).
    • (1997) J. Mol. Biol. , vol.272 , pp. 699-715
    • Farah, J.A.1    Smith, G.R.2
  • 19
    • 0026646152 scopus 로고
    • The RecB subunit of the Escherichia coli RecBCD enzyme couples ATP hydrolysis to DNA unwinding
    • Boehmer, P. E. & Emmerson, P. T. The RecB subunit of the Escherichia coli RecBCD enzyme couples ATP hydrolysis to DNA unwinding. J. Biol. Chem. 267, 4981-4987 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 4981-4987
    • Boehmer, P.E.1    Emmerson, P.T.2
  • 20
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya, A. E. & Koonin, E. V. Helicases: amino acid sequence comparisons and structure-function relationships. Curr. Opin. Struct. Biol. 3, 419-429 (1993).
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 22
    • 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., Hsieh, J., Gauss, G. H., Lohman, T. M. & Waksman, G. 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).
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 23
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA helicase with a DNA substrate indicate an inchworm mechanism
    • Velankar, S. S., Soultanas, P., Dillingham, M. S., Subramanya, H. S. & Wigley, D. B. Crystal structures of complexes of PcrA helicase with a DNA substrate indicate an inchworm mechanism. Cell 97, 75-84 (1999).
    • (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
  • 24
    • 0034635172 scopus 로고    scopus 로고
    • Unidirectional single-stranded DNA translocation by PcrA helicase: Measurement of step size and translocation speed
    • Dillingham, M. S., Wigley, D. B. & Webb, M. R. Unidirectional single-stranded DNA translocation by PcrA helicase: measurement of step size and translocation speed. Biochemistry 39, 205-212 (2000).
    • (2000) Biochemistry , vol.39 , pp. 205-212
    • Dillingham, M.S.1    Wigley, D.B.2    Webb, M.R.3
  • 25
    • 0034679815 scopus 로고    scopus 로고
    • Uncoupling DNA translocation and helicase activity in PcrA: Direct evidence for an active mechanism
    • Soultanas, P., Dillingham, M. S., Wiley, P., Webb, M. R. & Wigley, D. B. Uncoupling DNA translocation and helicase activity in PcrA: direct evidence for an active mechanism. EMBO J. 19, 3799-3810 (2000).
    • (2000) EMBO J. , vol.19 , pp. 3799-3810
    • Soultanas, P.1    Dillingham, M.S.2    Wiley, P.3    Webb, M.R.4    Wigley, D.B.5
  • 26
    • 0036211179 scopus 로고    scopus 로고
    • Modularity and specialisation in Superfamily 1 and 2 helicases
    • Singleton, M. R. & Wigley, D. B. Modularity and specialisation in Superfamily 1 and 2 helicases. J. Bacteriol. 184, 1819-1826 (2002).
    • (2002) J. Bacteriol. , vol.184 , pp. 1819-1826
    • Singleton, M.R.1    Wigley, D.B.2
  • 27
    • 0034664813 scopus 로고    scopus 로고
    • Holliday junction resolvases and related nucleases: Identification of new families, phyletic distribution and evolutionary trajectories
    • Aravind, L., Makarova, K. S. & Koonin, E. V. Holliday junction resolvases and related nucleases: identification of new families, phyletic distribution and evolutionary trajectories. Nucleic Acids Res. 28, 3417-3432 (2000).
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3417-3432
    • Aravind, L.1    Makarova, K.S.2    Koonin, E.V.3
  • 28
    • 0030881051 scopus 로고    scopus 로고
    • Toroidal structure of λ-exonuclease
    • Kovall, R. & Matthews, B. W. Toroidal structure of λ-exonuclease. Science 277, 1824-1827 (1997).
    • (1997) Science , vol.277 , pp. 1824-1827
    • Kovall, R.1    Matthews, B.W.2
  • 29
    • 0032491378 scopus 로고    scopus 로고
    • Identification of the nuclease active site in the multifunctional RecBCD enzyme by creation of a chimeric enzyme
    • Yu, M., Souaya, J. & Julin, D. A. Identification of the nuclease active site in the multifunctional RecBCD enzyme by creation of a chimeric enzyme. J. Mol. Biol. 283, 797-808 (1998).
    • (1998) J. Mol. Biol. , vol.283 , pp. 797-808
    • Yu, M.1    Souaya, J.2    Julin, D.A.3
  • 31
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138 (1993).
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 32
    • 0035989351 scopus 로고    scopus 로고
    • Domain of RecC required for assembly of the regulatory RecD subunit into the Escherichia coli RecBCD holoenzyme
    • Amundsen, S. K., Taylor, A. F. & Smith, G. R. Domain of RecC required for assembly of the regulatory RecD subunit into the Escherichia coli RecBCD holoenzyme. Genetics 161, 483-492 (2002).
    • (2002) Genetics , vol.161 , pp. 483-492
    • Amundsen, S.K.1    Taylor, A.F.2    Smith, G.R.3
  • 33
    • 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., Ruan, B., Yu, M., Wang, J. & Julin, D. A. The RecD subunit of the RecBCD enzyme from Escherichia coli is a single-stranded DNA dependent ATPase. J. Biol. Chem. 272, 10072-10079 (1997).
    • (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
  • 34
    • 0018801570 scopus 로고
    • Evidence for two mechanisms for DNA unwinding catalyzed by DNA helicases
    • Kuhn, B., Abdel-Monem, M., Krell, H. & Hoffmann-Berling, H. Evidence for two mechanisms for DNA unwinding catalyzed by DNA helicases. J. Biol. Chem. 254, 11343-11350 (1979).
    • (1979) J. Biol. Chem. , vol.254 , pp. 11343-11350
    • Kuhn, B.1    Abdel-Monem, M.2    Krell, H.3    Hoffmann-Berling, H.4
  • 35
    • 0035902592 scopus 로고    scopus 로고
    • Defining the roles of individual residues in the single-stranded DNA binding site of PcrA helicase
    • Dillingham, M. S., Soultanas, P., Wiley, P., Webb, M. R. & Wigley, D. B. 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).
    • (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
  • 36
    • 0034682407 scopus 로고    scopus 로고
    • Translocation step size and mechanism of the RecBC DNA helicase
    • Bianco, P. R. & Kowalczykowski, S. C. Translocation step size and mechanism of the RecBC DNA helicase. Nature 405, 368-372 (2000).
    • (2000) Nature , vol.405 , pp. 368-372
    • Bianco, P.R.1    Kowalczykowski, S.C.2
  • 37
    • 0028100641 scopus 로고
    • Efficiency of ATP hydrolysis and DNA unwinding by the RecBC enzyme from Escherichia coli
    • Korangy, F. & Julin, D. A. Efficiency of ATP hydrolysis and DNA unwinding by the RecBC enzyme from Escherichia coli. Biochemistry 33, 9552-9560 (1994).
    • (1994) Biochemistry , vol.33 , pp. 9552-9560
    • Korangy, F.1    Julin, D.A.2
  • 38
    • 0020599039 scopus 로고
    • Escherichia coli RecBC pseudorevertants lacking Chi recombinational hotspot activity
    • Schultz, D. W., Taylor, A. F. & Smith, G. R. Escherichia coli RecBC pseudorevertants lacking Chi recombinational hotspot activity. J. Bacteriol. 155, 664-680 (1983).
    • (1983) J. Bacteriol. , vol.155 , pp. 664-680
    • Schultz, D.W.1    Taylor, A.F.2    Smith, G.R.3
  • 40
    • 0034647421 scopus 로고    scopus 로고
    • A novel, 11 nucleotide variant of Chi, Chi*: One of a class of sequences defining the Escherichia coli recombination hotspot Chi
    • Arnold, D. A., Handa, N., Kobayashi, I. & Kowalczykowski, S. C. A novel, 11 nucleotide variant of Chi, Chi*: One of a class of sequences defining the Escherichia coli recombination hotspot Chi. J. Mol. Biol. 300, 469-479 (2000).
    • (2000) J. Mol. Biol. , vol.300 , pp. 469-479
    • Arnold, D.A.1    Handa, N.2    Kobayashi, I.3    Kowalczykowski, S.C.4
  • 41
    • 3142685068 scopus 로고    scopus 로고
    • Specific inhibition of the E. coli RecBCD enzyme by Chi sequences in single-stranded oligodeoxynucleotides
    • Kulkarni, A. & Julin, D. A. Specific inhibition of the E. coli RecBCD enzyme by Chi sequences in single-stranded oligodeoxynucleotides. Nucleic Acids Res. 32, 3672-3682 (2004).
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3672-3682
    • Kulkarni, A.1    Julin, D.A.2
  • 42
    • 0025231804 scopus 로고
    • Biochemical and physical properties of exonuclease V from Escherichia coli
    • Palas, K. M. & Kushner, S. R. Biochemical and physical properties of exonuclease V from Escherichia coli. J. Biol. Chem. 265, 3447-3454 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 3447-3454
    • Palas, K.M.1    Kushner, S.R.2
  • 43
    • 0034737310 scopus 로고    scopus 로고
    • Identification of the RecA protein-loading domain of RecBCD enzyme
    • Churchill, J. J. & Kowalczykowski, S. C. Identification of the RecA protein-loading domain of RecBCD enzyme. J. Mol. Biol. 297, 537-542 (2000).
    • (2000) J. Mol. Biol. , vol.297 , pp. 537-542
    • Churchill, J.J.1    Kowalczykowski, S.C.2
  • 44
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800 (1993).
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 45
    • 0033082065 scopus 로고    scopus 로고
    • Optimising Shake-and-bake for proteins
    • Weeks, C. M. & Miller, R. Optimising Shake-and-bake for proteins. Acta Crystallogr. D 55, 492-500 (1999).
    • (1999) Acta Crystallogr. D , vol.55 , pp. 492-500
    • Weeks, C.M.1    Miller, R.2
  • 46
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • de La Fortelle, E. & Bricogne, G. Maximum-likelihood heavy-atom parameter refinement for the multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 472-494
    • De La Fortelle, E.1    Bricogne, G.2
  • 47
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computing Project No. 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 48
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 904-925 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 904-925
    • Brunger, A.T.1
  • 49
    • 0030040323 scopus 로고    scopus 로고
    • Reduced surface: An efficient way to compute molecular surfaces
    • Sanner, M. F., Spehner, J. C. & Olson, A. J. Reduced surface: an efficient way to compute molecular surfaces. Biopolymers 38, 305-320 (1996).
    • (1996) Biopolymers , vol.38 , pp. 305-320
    • Sanner, M.F.1    Spehner, J.C.2    Olson, A.J.3
  • 50
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealistic molecular graphics
    • Merritt, E. A. & Bacon, D. J. Raster3D: Photorealistic molecular graphics. Methods Enzymol. 277, 505-524 (1997).
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


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