메뉴 건너뛰기




Volumn 508, Issue 7496, 2014, Pages 416-419

Structural basis for translocation by AddAB helicase-nuclease and its arrest at χ sites

Author keywords

[No Author keywords available]

Indexed keywords

ADDA PROTEIN; ADDB PROTEIN; ADENOSINE TRIPHOSPHATE; DOUBLE STRANDED DNA; HELICASE; NUCLEASE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 84898995018     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature13037     Document Type: Article
Times cited : (42)

References (33)
  • 1
    • 0016198522 scopus 로고
    • Rec-mediated recombinational hot spot activity in bacteriophage lambda ii a mutation which causes hot spot activity
    • Lam, S. T., Stahl, M. M., McMilin, K. D. & Stahl, F. W. Rec-mediated recombinational hot spot activity in bacteriophage lambda. II. A mutation which causes hot spot activity. Genetics 77, 425-433 (1974
    • (1974) Genetics , vol.77 , pp. 425-433
    • Lam, S.T.1    Stahl, M.M.2    McMilin, K.D.3    Stahl, F.W.4
  • 2
    • 0031713244 scopus 로고    scopus 로고
    • Afive-nucleotidesequence protects dna fromexonucleolytic degradation by addab, the recbcd analogue of bacillus subtilis
    • Chédin, F.,Noirot, P., Biaudet, V.& Ehrlich, S. D.Afive-nucleotidesequence protects DNA fromexonucleolytic degradation by AddAB, the RecBCD analogue of Bacillus subtilis. Mol. Microbiol. 29, 1369-1377 (1998
    • (1998) Mol. Microbiol , vol.29 , pp. 1369-1377
    • Chédin, F.1    Noirot, P.2    Biaudet, V.3    Ehrlich, S.D.4
  • 3
    • 57349157777 scopus 로고    scopus 로고
    • Recbcd enzyme and the repair of double-stranded dna breaks
    • Dillingham, M. S. & Kowalczykowski, S. C. RecBCD enzyme and the repair of double-stranded DNA breaks. Microbiol. Mol. Biol. Rev. 72, 642-671 (2008
    • (2008) Microbiol. Mol. Biol. Rev , vol.72 , pp. 642-671
    • Dillingham, M.S.1    Kowalczykowski, S.C.2
  • 4
    • 84871340015 scopus 로고    scopus 로고
    • Bacterial dnarepair: Recent insights into the mechanismof recbcd addab and adnab
    • Wigley, D. B. Bacterial DNArepair: Recent insights into the mechanismof RecBCD, AddAB and AdnAB. Nature Rev. Microbiol. 11, 9-13 (2013
    • (2013) Nature Rev. Microbiol , vol.11 , pp. 9-13
    • Wigley, D.B.1
  • 5
    • 0021807208 scopus 로고
    • Chi-dependent dna strand cleavage by recbc enzyme
    • Ponticelli, A. S., Schultz, D. W., Taylor, A. F. & Smith, G. R. Chi-dependent DNA strand cleavage by 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
  • 6
    • 0031444642 scopus 로고    scopus 로고
    • The translocating recbcd enzyme stimulates recombination by directing reca protein onto ssdnain a chi-regulated manner
    • Anderson, D. G. & Kowalczykowski, S. C. The translocating RecBCD enzyme stimulates recombination by directing RecA protein onto ssDNAin a chi-regulated manner. Cell 90, 77-86 (1997
    • (1997) Cell , vol.90 , pp. 77-86
    • Anderson, D.G.1    Kowalczykowski, S.C.2
  • 7
    • 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
  • 8
    • 36049052525 scopus 로고    scopus 로고
    • Recbcd enzyme switches lead motor subunits in response to chi recognition
    • Spies, M., Amitani, I., Baskin, R. J. & Kowalczykowski, S. C. RecBCD enzyme switches lead motor subunits in response to chi recognition. Cell 131, 694-705 (2007
    • (2007) Cell , vol.131 , pp. 694-705
    • Spies, M.1    Amitani, I.2    Baskin, R.J.3    Kowalczykowski, S.C.4
  • 9
  • 10
    • 84858796420 scopus 로고    scopus 로고
    • Insights into chi recognition from the structure of an addab-Type helicase-nuclease complex
    • Saikrishnan, K. et al. Insights into Chi recognition from the structure of an AddAB-Type helicase-nuclease complex. EMBO J. 31, 1568-1578 (2012
    • (2012) EMBO J. , vol.31 , pp. 1568-1578
    • Saikrishnan, K.1
  • 11
  • 12
    • 79953177394 scopus 로고    scopus 로고
    • The addab helicase-nuclease catalyses rapid and processive dna unwinding using a single superfamily 1a motor domain
    • Yeeles, J. T., Gwynn, E. J., Webb, M. R. & Dillingham, M. S. The AddAB helicase-nuclease catalyses rapid and processive DNA unwinding using a single Superfamily 1A motor domain. Nucleic Acids Res. 39, 2271-2285 (2011
    • (2011) Nucleic Acids Res , vol.39 , pp. 2271-2285
    • Yeeles, J.T.1    Gwynn, E.J.2    Webb, M.R.3    Dillingham, M.S.4
  • 13
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton, M. R., Dillingham, M. S. & Wigley, D. B. Structure and mechanism of helicases and nucleic acid translocases. Annu. Rev. Biochem. 76, 23-50 (2007
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 14
    • 77449156020 scopus 로고    scopus 로고
    • Characterization of the mycobacterial adnab dna motor provides insights into the evolution of bacterial motor-nuclease machines
    • Unciuleac, M. C. & Shuman, S. Characterization of the mycobacterial AdnAB DNA motor provides insights into the evolution of bacterial motor-nuclease machines. J. Biol. Chem. 285, 2632-2641 (2010
    • (2010) J. Biol. Chem , vol.285 , pp. 2632-2641
    • Unciuleac, M.C.1    Shuman, S.2
  • 15
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of pcra dna 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 DNA 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
  • 16
    • 77957785417 scopus 로고    scopus 로고
    • Escherichia coli recbc helicase has two translocase activities controlled by a single atpase motor
    • Wu, C. G., Bradford, C. & Lohman, T. M. Escherichia coli RecBC helicase has two translocase activities controlled by a single ATPase motor. Nature Struct. Mol. Biol. 17, 1210-1217 (2010
    • (2010) Nature Struct. Mol. Biol , vol.17 , pp. 1210-1217
    • Wu, C.G.1    Bradford, C.2    Lohman, T.M.3
  • 17
    • 84861889126 scopus 로고    scopus 로고
    • Molecular determinants responsible for recognition of the singlestranded dna regulatory sequence, x, by recbcd enzyme
    • Handa, N. et al. Molecular determinants responsible for recognition of the singlestranded DNA regulatory sequence, x, by RecBCD enzyme. Proc. Natl Acad. Sci. USA 109, 8901-8906 (2012
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 8901-8906
    • Handa, N.1
  • 18
    • 84861860703 scopus 로고    scopus 로고
    • Mutation of x-recognition by recbcd reveals a regulated molecular latch and suggests a channel-bypass mechanismfor biological control
    • Yang, L. et al. Mutation of x-recognition by RecBCD reveals a regulated molecular latch and suggests a channel-bypass mechanismfor biological control. Proc. Natl Acad. Sci. USA 109, 8907-8912 (2012
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 8907-8912
    • Yang, L.1
  • 19
    • 0030881051 scopus 로고    scopus 로고
    • Toroidal structure of l-exonuclease
    • Kovall, R. & Matthews, B. W. Toroidal structure of l-exonuclease. Science 277, 1824-1827 (1997
    • (1997) Science , vol.277 , pp. 1824-1827
    • Kovall, R.1    Matthews, B.W.2
  • 20
    • 79961050090 scopus 로고    scopus 로고
    • Crystal structures of l exonuclease in complex with dna suggest an electrostatic ratchet mechanism for processivity
    • Zhang, J., McCabe, K. A. & Bell, C. E. Crystal structures of l exonuclease in complex with DNA suggest an electrostatic ratchet mechanism for processivity. Proc. Natl Acad. Sci. USA 108, 11872-11877 (2011
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 11872-11877
    • Zhang, J.1    McCabe, K.A.2    Bell, C.E.3
  • 21
    • 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
  • 22
    • 0024406221 scopus 로고
    • Recombination of bacteriophage l in recdmutants of escherichia coli
    • Thaler, D. S. et al. Recombination of bacteriophage l in recDmutants of Escherichia coli. Genome 31, 53-67 (1989
    • (1989) Genome , vol.31 , pp. 53-67
    • Thaler, D.S.1
  • 23
    • 0035905807 scopus 로고    scopus 로고
    • X-sequence recognition and dna translocation by single recbcd helicase/nuclease molecules
    • Dohoney, K. M. & Gelles, J. x-sequence recognition and DNA translocation by single RecBCD helicase/nuclease molecules. Nature 409, 370-374 (2001
    • (2001) Nature , vol.409 , pp. 370-374
    • Dohoney, K.M.1    Gelles, J.2
  • 24
    • 14644412914 scopus 로고    scopus 로고
    • Direct visualization of recbcd movement reveals cotranslocation of the recd motor after x recognition
    • Handa, N., Bianco, P. R., Baskin, R. J.& Kowalczykowski, S. C. Direct visualization of RecBCD movement reveals cotranslocation of the RecD motor after x recognition. Mol. Cell 17, 745-750 (2005
    • (2005) Mol. Cell , vol.17 , pp. 745-750
    • Handa, N.1    Bianco, P.R.2    Baskin, R.J.3    Kowalczykowski, S.C.4
  • 25
    • 33747375815 scopus 로고    scopus 로고
    • Probing 39-ssdna loop formation in e coli recbcd/recbc-dna complexes using non-natural dna: A model for ''chi'' recognition complexes
    • Wong, C. J., Rice, R. L., Baker, N. A., Ju, T. & Lohman, T. M. Probing 39-ssDNA loop formation in E. coli RecBCD/RecBC-DNA complexes using non-natural DNA: A model for ''Chi'' recognition complexes. J. Mol. Biol. 362, 26-43 (2006
    • (2006) J. Mol. Biol , vol.362 , pp. 26-43
    • Wong, C.J.1    Rice, R.L.2    Baker, N.A.3    Ju, T.4    Lohman, T.M.5
  • 26
    • 0033578824 scopus 로고    scopus 로고
    • A single mutation recbd1080a eliminates reca protein loading but not chi recognition by recbcd enzyme
    • Anderson, D. G., Churchill, J. J. & Kowalczykowski, S. C. A single mutation, RecBD1080A eliminates RecA protein loading but not Chi recognition by RecBCD enzyme. J. Biol. Chem. 274, 27139-27144 (1999
    • (1999) J. Biol. Chem , vol.274 , pp. 27139-27144
    • Anderson, D.G.1    Churchill, J.J.2    Kowalczykowski, S.C.3
  • 27
    • 65549136266 scopus 로고    scopus 로고
    • An iron-sulfur cluster is essential for the binding of brokendna byaddab-Type helicase-nucleases
    • Yeeles, J. T., Cammack, R.& Dillingham, M. S.An iron-sulfur cluster is essential for the binding of brokenDNA byAddAB-Type helicase-nucleases. J. Biol. Chem. 284, 7746-7755 (2009
    • (2009) J. Biol. Chem , vol.284 , pp. 7746-7755
    • Yeeles, J.T.1    Cammack, R.2    Dillingham, M.S.3
  • 29
    • 0028103275 scopus 로고
    • Collaborative Computational Project Number 4. The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994
    • (1994) Acta Crystallogr , vol.D50 , pp. 760-763
  • 30
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007
    • (2007) J. Appl. Crystallogr , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 32
    • 76449098262 scopus 로고    scopus 로고
    • Phenix: A comprehensive python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010
    • (2010) Acta Crystallogr , vol.D66 , pp. 213-221
    • Adams, P.D.1
  • 33
    • 34547592557 scopus 로고    scopus 로고
    • Molprobity: All-Atom contacts and structure validation for proteins and nucleic acids
    • Davis, I. W. et al. MolProbity: All-Atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35, W375-W383 (2007
    • (2007) Nucleic Acids Res , vol.35
    • Davis, I.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.