메뉴 건너뛰기




Volumn 21, Issue 4, 2006, Pages 573-580

The RecA binding locus of RecBCD is a general domain for recruitment of DNA strand exchange proteins

Author keywords

[No Author keywords available]

Indexed keywords

BRCA2 PROTEIN; EXODEOXYRIBONUCLEASE V; RAD51 PROTEIN; RECA PROTEIN;

EID: 32444451553     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2006.01.007     Document Type: Article
Times cited : (89)

References (48)
  • 2
    • 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
    • D.G. Anderson, and S.C. Kowalczykowski The recombination hot spot χ is a regulatory element that switches the polarity of DNA degradation by the RecBCD enzyme Genes Dev. 11 1997 571 581
    • (1997) Genes Dev. , vol.11 , pp. 571-581
    • Anderson, D.G.1    Kowalczykowski, S.C.2
  • 3
    • 0031444642 scopus 로고    scopus 로고
    • The translocating RecBCD enzyme stimulates recombination by directing RecA protein onto ssDNA in a χ-regulated manner
    • D.G. Anderson, and S.C. Kowalczykowski The translocating RecBCD enzyme stimulates recombination by directing RecA protein onto ssDNA in a χ-regulated manner Cell 90 1997 77 86
    • (1997) Cell , vol.90 , pp. 77-86
    • Anderson, D.G.1    Kowalczykowski, S.C.2
  • 4
    • 0031064615 scopus 로고    scopus 로고
    • Chi-activated 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
    • D.G. Anderson, J.J. Churchill, and S.C. Kowalczykowski Chi-activated 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 1997 117 128
    • (1997) Genes Cells , vol.2 , pp. 117-128
    • Anderson, D.G.1    Churchill, J.J.2    Kowalczykowski, S.C.3
  • 6
    • 0001865832 scopus 로고    scopus 로고
    • DNA strand exchange proteins: A biochemical and physical comparison
    • P.R. Bianco, R.B. Tracy, and S.C. Kowalczykowski DNA strand exchange proteins: a biochemical and physical comparison Front. Biosci. 3 1998 D570 D603
    • (1998) Front. Biosci. , vol.3
    • Bianco, P.R.1    Tracy, R.B.2    Kowalczykowski, S.C.3
  • 7
    • 0030949953 scopus 로고    scopus 로고
    • Evolutionary comparisons of RecA-like proteins across all major kingdoms of living organisms
    • V. Brendel, L. Brocchieri, S.J. Sandler, A.J. Clark, and S. Karlin Evolutionary comparisons of RecA-like proteins across all major kingdoms of living organisms J. Mol. Evol. 44 1997 528 541
    • (1997) J. Mol. Evol. , vol.44 , pp. 528-541
    • Brendel, V.1    Brocchieri, L.2    Sandler, S.J.3    Clark, A.J.4    Karlin, S.5
  • 8
    • 0024210803 scopus 로고
    • RecA protein self-assembly: Multiple discrete aggregation states
    • S.L. Brenner, A. Zlotnick, and J.D. Griffith RecA protein self-assembly: multiple discrete aggregation states J. Mol. Biol. 204 1988 959 972
    • (1988) J. Mol. Biol. , vol.204 , pp. 959-972
    • Brenner, S.L.1    Zlotnick, A.2    Griffith, J.D.3
  • 9
    • 0032702679 scopus 로고    scopus 로고
    • Expression of BRC repeats in breast cancer cells disrupts the BRCA2-Rad51 complex and leads to radiation hypersensitivity and loss of G(2)/M checkpoint control
    • C.F. Chen, P.L. Chen, Q. Zhong, Z.D. Sharp, and W.H. Lee Expression of BRC repeats in breast cancer cells disrupts the BRCA2-Rad51 complex and leads to radiation hypersensitivity and loss of G(2)/M checkpoint control J. Biol. Chem. 274 1999 32931 32935
    • (1999) J. Biol. Chem. , vol.274 , pp. 32931-32935
    • Chen, C.F.1    Chen, P.L.2    Zhong, Q.3    Sharp, Z.D.4    Lee, W.H.5
  • 10
    • 0032574733 scopus 로고    scopus 로고
    • The BRC repeats in BRCA2 are critical for RAD51 binding and resistance to methyl methanesulfonate treatment
    • P.L. Chen, C.F. Chen, Y. Chen, J. Xiao, Z.D. Sharp, and W.H. Lee The BRC repeats in BRCA2 are critical for RAD51 binding and resistance to methyl methanesulfonate treatment Proc. Natl. Acad. Sci. USA 95 1998 5287 5292
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5287-5292
    • Chen, P.L.1    Chen, C.F.2    Chen, Y.3    Xiao, J.4    Sharp, Z.D.5    Lee, W.H.6
  • 11
    • 0034737310 scopus 로고    scopus 로고
    • Identification of the RecA protein-loading domain of RecBCD enzyme
    • J.J. Churchill, and S.C. Kowalczykowski Identification of the RecA protein-loading domain of RecBCD enzyme J. Mol. Biol. 297 2000 537 542
    • (2000) J. Mol. Biol. , vol.297 , pp. 537-542
    • Churchill, J.J.1    Kowalczykowski, S.C.2
  • 12
    • 0033119260 scopus 로고    scopus 로고
    • The RecBC enzyme loads RecA protein onto ssDNA asymmetrically and independently of chi, resulting in constitutive recombination activation
    • J.J. Churchill, D.G. Anderson, and S.C. Kowalczykowski The RecBC enzyme loads RecA protein onto ssDNA asymmetrically and independently of chi, resulting in constitutive recombination activation Genes Dev. 13 1999 901 911
    • (1999) Genes Dev. , vol.13 , pp. 901-911
    • Churchill, J.J.1    Anderson, D.G.2    Kowalczykowski, S.C.3
  • 14
    • 0034671684 scopus 로고    scopus 로고
    • Crystal structures of mycobacterium tuberculosis RecA and its complex with ADP-AlF(4): Implications for decreased ATPase activity and molecular aggregation
    • S. Datta, M.M. Prabu, M.B. Vaze, N. Ganesh, N.R. Chandra, K. Muniyappa, and M. Vijayan Crystal structures of mycobacterium tuberculosis RecA and its complex with ADP-AlF(4): implications for decreased ATPase activity and molecular aggregation Nucleic Acids Res. 28 2000 4964 4973
    • (2000) Nucleic Acids Res. , vol.28 , pp. 4964-4973
    • Datta, S.1    Prabu, M.M.2    Vaze, M.B.3    Ganesh, N.4    Chandra, N.R.5    Muniyappa, K.6    Vijayan, M.7
  • 15
    • 0026526718 scopus 로고
    • Recombination and UV resistance of Escherichia coli with the cloned recA and recBCD genes of Serratia marcescens and Proteus mirabilis: Evidence for an advantage of intraspecies combination of P. mirabilis RecA protein and RecBCD enzyme
    • J. de Vries, and W. Wackernagel Recombination and UV resistance of Escherichia coli with the cloned recA and recBCD genes of Serratia marcescens and Proteus mirabilis: evidence for an advantage of intraspecies combination of P. mirabilis RecA protein and RecBCD enzyme J. Gen. Microbiol. 138 1992 31 38
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 31-38
    • De Vries, J.1    Wackernagel, W.2
  • 16
    • 0025902330 scopus 로고
    • Homologous pairing in vitro stimulated by the recombination hotspot, Chi
    • D.A. Dixon, and S.C. Kowalczykowski Homologous pairing in vitro stimulated by the recombination hotspot, Chi Cell 66 1991 361 371
    • (1991) Cell , vol.66 , pp. 361-371
    • Dixon, D.A.1    Kowalczykowski, S.C.2
  • 17
    • 0027511858 scopus 로고
    • The recombination hotspot χ is a regulatory sequence that acts by attenuating the nuclease activity of the E. coli RecBCD enzyme
    • D.A. Dixon, and S.C. Kowalczykowski The recombination hotspot χ is a regulatory sequence that acts by attenuating the nuclease activity of the E. coli RecBCD enzyme Cell 73 1993 87 96
    • (1993) Cell , vol.73 , pp. 87-96
    • Dixon, D.A.1    Kowalczykowski, S.C.2
  • 18
    • 14644412914 scopus 로고    scopus 로고
    • Direct visualization of RecBCD movement reveals cotranslocation of the RecD motor after Chi recognition
    • N. Handa, P.R. Bianco, R.J. Baskin, and S.C. Kowalczykowski Direct visualization of RecBCD movement reveals cotranslocation of the RecD motor after Chi recognition Mol. Cell 17 2005 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
  • 19
    • 0032522789 scopus 로고    scopus 로고
    • RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination
    • F.G. Harmon, and S.C. Kowalczykowski RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination Genes Dev. 12 1998 1134 1144
    • (1998) Genes Dev. , vol.12 , pp. 1134-1144
    • Harmon, F.G.1    Kowalczykowski, S.C.2
  • 20
    • 0028970713 scopus 로고
    • Bacterial classifications derived from recA protein sequence comparisons
    • S. Karlin, G.M. Weinstock, and V. Brendel Bacterial classifications derived from recA protein sequence comparisons J. Bacteriol. 177 1995 6881 6893
    • (1995) J. Bacteriol. , vol.177 , pp. 6881-6893
    • Karlin, S.1    Weinstock, G.M.2    Brendel, V.3
  • 21
    • 0020021789 scopus 로고
    • Induction of E. coli recA protein via recBC and alternate pathways: Quantitation by enzyme-linked immunosorbent assay (ELISA)
    • A.E. Karu, and E.D. Belk Induction of E. coli recA protein via recBC and alternate pathways: quantitation by enzyme-linked immunosorbent assay (ELISA) Mol. Gen. Genet. 185 1982 275 282
    • (1982) Mol. Gen. Genet. , vol.185 , pp. 275-282
    • Karu, A.E.1    Belk, E.D.2
  • 22
    • 0036894879 scopus 로고    scopus 로고
    • Molecular mimicry connects BRCA2 to Rad51 and recombinational DNA repair
    • S.C. Kowalczykowski Molecular mimicry connects BRCA2 to Rad51 and recombinational DNA repair Nat. Struct. Biol. 9 2002 897 899
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 897-899
    • Kowalczykowski, S.C.1
  • 23
    • 14144253362 scopus 로고    scopus 로고
    • Cancer: Catalyst of a catalyst
    • S.C. Kowalczykowski Cancer: catalyst of a catalyst Nature 433 2005 591 592
    • (2005) Nature , vol.433 , pp. 591-592
    • Kowalczykowski, S.C.1
  • 24
    • 0023135142 scopus 로고
    • Effects of the Escherichia coli SSB protein on the single-stranded DNA-dependent ATPase activity of Escherichia coli RecA protein: Evidence that SSB protein facilitates the binding of RecA protein to regions of secondary structure within single-stranded DNA
    • S.C. Kowalczykowski, and R.A. Krupp Effects of the Escherichia coli SSB protein on the single-stranded DNA-dependent ATPase activity of Escherichia coli RecA protein: evidence that SSB protein facilitates the binding of RecA protein to regions of secondary structure within single-stranded DNA J. Mol. Biol. 193 1987 97 113
    • (1987) J. Mol. Biol. , vol.193 , pp. 97-113
    • Kowalczykowski, S.C.1    Krupp, R.A.2
  • 25
    • 0019351776 scopus 로고
    • Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions
    • S.C. Kowalczykowski, N. Lonberg, J.W. Newport, and P.H. von Hippel Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids. I. Characterization of the binding interactions J. Mol. Biol. 145 1981 75 104
    • (1981) J. Mol. Biol. , vol.145 , pp. 75-104
    • Kowalczykowski, S.C.1    Lonberg, N.2    Newport, J.W.3    Von Hippel, P.H.4
  • 27
    • 3142685068 scopus 로고    scopus 로고
    • Specific inhibition of the E.coli RecBCD enzyme by Chi sequences in single-stranded oligodeoxyribonucleotides
    • A. Kulkarni, and D.A. Julin Specific inhibition of the E.coli RecBCD enzyme by Chi sequences in single-stranded oligodeoxyribonucleotides Nucleic Acids Res. 32 2004 3672 3682
    • (2004) Nucleic Acids Res. , vol.32 , pp. 3672-3682
    • Kulkarni, A.1    Julin, D.A.2
  • 28
    • 0016198522 scopus 로고
    • Rec-mediated recombinational hot spot activity in bacteriophage lambda. II. a mutation which causes hot spot activity
    • S.T. Lam, M.M. Stahl, K.D. McMilin, and F.W. Stahl Rec-mediated recombinational hot spot activity in bacteriophage lambda. II. A mutation which causes hot spot activity Genetics 77 1974 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
  • 30
    • 1642463787 scopus 로고    scopus 로고
    • Molecular design and functional organization of the RecA protein
    • D.A. McGrew, and K.L. Knight Molecular design and functional organization of the RecA protein Crit. Rev. Biochem. Mol. Biol. 38 2003 385 432
    • (2003) Crit. Rev. Biochem. Mol. Biol. , vol.38 , pp. 385-432
    • McGrew, D.A.1    Knight, K.L.2
  • 31
    • 0029037763 scopus 로고
    • The recombination hot spot χ activates RecBCD recombination by converting Escherichia coli to a recD mutant phenocopy
    • R.S. Myers, A. Kuzminov, and F.W. Stahl The recombination hot spot χ activates RecBCD recombination by converting Escherichia coli to a recD mutant phenocopy Proc. Natl. Acad. Sci. USA 92 1995 6244 6248
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6244-6248
    • Myers, R.S.1    Kuzminov, A.2    Stahl, F.W.3
  • 32
    • 0032556870 scopus 로고    scopus 로고
    • Stimulation of DNA strand exchange by S. cerevisiae Rad52 protein requires the concerted action of Rad51 protein and RPA
    • J.H. New, T. Sugiyama, and S.C. Kowalczykowski Stimulation of DNA strand exchange by S. cerevisiae Rad52 protein requires the concerted action of Rad51 protein and RPA Nature 391 1998 407 410
    • (1998) Nature , vol.391 , pp. 407-410
    • New, J.H.1    Sugiyama, T.2    Kowalczykowski, S.C.3
  • 34
    • 0034212826 scopus 로고    scopus 로고
    • BiGGER: A new (soft) docking algorithm for predicting protein interactions
    • P.N. Palma, L. Krippahl, J.E. Wampler, and J.J. Moura BiGGER: a new (soft) docking algorithm for predicting protein interactions Proteins 39 2000 372 384
    • (2000) Proteins , vol.39 , pp. 372-384
    • Palma, P.N.1    Krippahl, L.2    Wampler, J.E.3    Moura, J.J.4
  • 36
    • 0029848426 scopus 로고    scopus 로고
    • Interaction of Escherichia coli RecA protein with LexA repressor. I. LexA repressor cleavage is competitive with binding of a secondary DNA molecule
    • W.M. Rehrauer, P.E. Lavery, E.L. Palmer, R.N. Singh, and S.C. Kowalczykowski Interaction of Escherichia coli RecA protein with LexA repressor. I. LexA repressor cleavage is competitive with binding of a secondary DNA molecule J. Biol. Chem. 271 1996 23865 23873
    • (1996) J. Biol. Chem. , vol.271 , pp. 23865-23873
    • Rehrauer, W.M.1    Lavery, P.E.2    Palmer, E.L.3    Singh, R.N.4    Kowalczykowski, S.C.5
  • 39
    • 27744535816 scopus 로고    scopus 로고
    • Homologous recombination by RecBCD and RecF pathways
    • N.P. Higgins ASM Press Washington, D.C.
    • M. Spies, and S.C. Kowalczykowski Homologous recombination by RecBCD and RecF pathways N.P. Higgins The Bacterial Chromosome 2005 ASM Press Washington, D.C. 389 403
    • (2005) The Bacterial Chromosome , pp. 389-403
    • Spies, M.1    Kowalczykowski, S.C.2
  • 40
    • 0141540814 scopus 로고    scopus 로고
    • A molecular throttle: The recombination hotspot, χ, controls DNA translocation by the RecBCD helicase
    • M. Spies, P.R. Bianco, M.S. Dillingham, N. Handa, R.J. Baskin, and S.C. Kowalczykowski A molecular throttle: the recombination hotspot, χ, controls DNA translocation by the RecBCD helicase Cell 114 2003 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
  • 41
    • 0026500416 scopus 로고
    • The structure of the E. coli recA protein monomer and polymer
    • R.M. Story, I.T. Weber, and T.A. Steitz The structure of the E. coli recA protein monomer and polymer Nature 355 1992 318 325
    • (1992) Nature , vol.355 , pp. 318-325
    • Story, R.M.1    Weber, I.T.2    Steitz, T.A.3
  • 42
    • 0027322196 scopus 로고
    • Structural relationship of bacterial RecA proteins to recombination proteins from bacteriophage T4 and yeast
    • R.M. Story, D.K. Bishop, N. Kleckner, and T.A. Steitz Structural relationship of bacterial RecA proteins to recombination proteins from bacteriophage T4 and yeast Science 259 1993 1892 1896
    • (1993) Science , vol.259 , pp. 1892-1896
    • Story, R.M.1    Bishop, D.K.2    Kleckner, N.3    Steitz, T.A.4
  • 43
    • 0033119729 scopus 로고    scopus 로고
    • Regulation of homologous recombination: Chi inactivates RecBCD enzyme by disassembly of the three subunits
    • A.F. Taylor, and G.R. Smith Regulation of homologous recombination: Chi inactivates RecBCD enzyme by disassembly of the three subunits Genes Dev. 13 1999 890 900
    • (1999) Genes Dev. , vol.13 , pp. 890-900
    • Taylor, A.F.1    Smith, G.R.2
  • 44
    • 0021839175 scopus 로고
    • RecBC enzyme nicking at Chi sites during DNA unwinding: Location and orientation-dependence of the cutting
    • A.F. Taylor, D.W. Schultz, A.S. Ponticelli, and G.R. Smith RecBC enzyme nicking at Chi sites during DNA unwinding: location and orientation-dependence of the cutting Cell 41 1985 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
  • 45
    • 0031466027 scopus 로고    scopus 로고
    • RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene brca2
    • A.K.C. Wong, R. Pero, P.A. Ormonde, S.V. Tavtigian, and P.L. Bartel RAD51 interacts with the evolutionarily conserved BRC motifs in the human breast cancer susceptibility gene brca2 J. Biol. Chem. 272 1997 31941 31944
    • (1997) J. Biol. Chem. , vol.272 , pp. 31941-31944
    • Wong, A.K.C.1    Pero, R.2    Ormonde, P.A.3    Tavtigian, S.V.4    Bartel, P.L.5
  • 46
    • 14144253224 scopus 로고    scopus 로고
    • The BRCA2 homologue Brh2 nucleates RAD51 filament formation at a dsDNA-ssDNA junction
    • H. Yang, Q. Li, J. Fan, W.K. Holloman, and N.P. Pavletich The BRCA2 homologue Brh2 nucleates RAD51 filament formation at a dsDNA-ssDNA junction Nature 433 2005 653 657
    • (2005) Nature , vol.433 , pp. 653-657
    • Yang, H.1    Li, Q.2    Fan, J.3    Holloman, W.K.4    Pavletich, N.P.5
  • 47
    • 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
    • M. Yu, J. Souaya, and D.A. Julin 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 1998 981 986
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 981-986
    • Yu, M.1    Souaya, J.2    Julin, D.A.3
  • 48
    • 0345034772 scopus 로고    scopus 로고
    • Isolation and characterization of the C-terminal nuclease domain from the RecB protein of Escherichia coli
    • X.J. Zhang, and D.A. Julin Isolation and characterization of the C-terminal nuclease domain from the RecB protein of Escherichia coli Nucleic Acids Res. 27 1999 4200 4207
    • (1999) Nucleic Acids Res. , vol.27 , pp. 4200-4207
    • Zhang, X.J.1    Julin, D.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.