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Volumn 391, Issue 2, 2009, Pages 269-274

The RecB Nuclease Domain Binds to RecA-DNA Filaments: Implications for Filament Loading

Author keywords

electron microscopy; helical polymers; recombination

Indexed keywords

EXODEOXYRIBONUCLEASE V; HELICASE; NUCLEASE; RECA PROTEIN; SINGLE STRANDED DNA;

EID: 67650957556     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.06.042     Document Type: Article
Times cited : (10)

References (34)
  • 1
    • 0024443524 scopus 로고
    • Formation of heteroduplex DNA promoted by the combined activities of Escherichia coli recA and recBCD proteins
    • Roman L.J., and Kowalczykowski S.C. Formation of heteroduplex DNA promoted by the combined activities of Escherichia coli recA and recBCD proteins. J. Biol. Chem. 264 (1989) 18340-18348
    • (1989) J. Biol. Chem. , vol.264 , pp. 18340-18348
    • Roman, L.J.1    Kowalczykowski, S.C.2
  • 2
    • 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., and Kowalczykowski S.C. The translocating RecBCD enzyme stimulates recombination by directing RecA protein onto ssDNA in a chi-regulated manner. Cell 90 (1997) 77-86
    • (1997) Cell , vol.90 , pp. 77-86
    • Anderson, D.G.1    Kowalczykowski, S.C.2
  • 3
    • 0034737310 scopus 로고    scopus 로고
    • Identification of the RecA protein-loading domain of RecBCD enzyme
    • Churchill J.J., and Kowalczykowski S.C. 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
  • 4
    • 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., Anderson D.G., and Kowalczykowski S.C. 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
  • 5
    • 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 Kowalczykowski S.C. The RecA binding locus of RecBCD is a general domain for recruitment of DNA strand exchange proteins. Mol. Cell 21 (2006) 573-580
    • (2006) Mol. Cell , vol.21 , pp. 573-580
    • Spies, M.1    Kowalczykowski, S.C.2
  • 6
    • 0026500416 scopus 로고
    • The Structure of the E. coli recA Protein Monomer and Polymer
    • Story R.M., Weber I.T., and Steitz T.A. 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
  • 11
    • 4143068081 scopus 로고    scopus 로고
    • Crystal structure of archaeal recombinase RADA: a snapshot of its extended conformation
    • Wu Y., He Y., Moya I.A., Qian X., and Luo Y. Crystal structure of archaeal recombinase RADA: a snapshot of its extended conformation. Mol. Cell 15 (2004) 423-435
    • (2004) Mol. Cell , vol.15 , pp. 423-435
    • Wu, Y.1    He, Y.2    Moya, I.A.3    Qian, X.4    Luo, Y.5
  • 14
    • 33845305513 scopus 로고    scopus 로고
    • The iterative helical real space reconstruction method: Surmounting the problems posed by real polymers
    • Egelman E.H. The iterative helical real space reconstruction method: Surmounting the problems posed by real polymers. J. Struct. Biol. 157 (2007) 83-94
    • (2007) J. Struct. Biol. , vol.157 , pp. 83-94
    • Egelman, E.H.1
  • 15
    • 0034564239 scopus 로고    scopus 로고
    • A robust algorithm for the reconstruction of helical filaments using single-particle methods
    • Egelman E.H. A robust algorithm for the reconstruction of helical filaments using single-particle methods. Ultramicroscopy 85 (2000) 225-234
    • (2000) Ultramicroscopy , vol.85 , pp. 225-234
    • Egelman, E.H.1
  • 16
    • 33745860367 scopus 로고    scopus 로고
    • Structural Polymorphism in Bacterial EspA Filaments Revealed by Cryo-EM and an Improved Approach to Helical Reconstruction
    • Wang Y.A., Yu X., Yip C., Strynadka N.C., and Egelman E.H. Structural Polymorphism in Bacterial EspA Filaments Revealed by Cryo-EM and an Improved Approach to Helical Reconstruction. Structure 14 (2006) 1189-1196
    • (2006) Structure , vol.14 , pp. 1189-1196
    • Wang, Y.A.1    Yu, X.2    Yip, C.3    Strynadka, N.C.4    Egelman, E.H.5
  • 18
    • 33646182429 scopus 로고    scopus 로고
    • The CH-domain of calponin does not determine the modes of calponin binding to F-actin
    • Galkin V.E., Orlova A., Fattoum A., Walsh M.P., and Egelman E.H. The CH-domain of calponin does not determine the modes of calponin binding to F-actin. J. Mol. Biol. 359 (2006) 478-485
    • (2006) J. Mol. Biol. , vol.359 , pp. 478-485
    • Galkin, V.E.1    Orlova, A.2    Fattoum, A.3    Walsh, M.P.4    Egelman, E.H.5
  • 19
    • 0041620499 scopus 로고    scopus 로고
    • Do the utrophin tandem calponin homology domains bind F-actin in a compact or extended conformation?
    • Galkin V.E., Orlova A., VanLoock M.S., and Egelman E.H. Do the utrophin tandem calponin homology domains bind F-actin in a compact or extended conformation?. J. Mol. Biol. 331 (2003) 967-972
    • (2003) J. Mol. Biol. , vol.331 , pp. 967-972
    • Galkin, V.E.1    Orlova, A.2    VanLoock, M.S.3    Egelman, E.H.4
  • 20
    • 0037092046 scopus 로고    scopus 로고
    • The Utrophin Actin-Binding Domain Binds F-Actin in Two Different Modes: Implications for the Spectrin Superfamily of Proteins
    • Galkin V.E., Orlova A., VanLoock M.S., Rybakova I.N., Ervasti J.M., and Egelman E.H. The Utrophin Actin-Binding Domain Binds F-Actin in Two Different Modes: Implications for the Spectrin Superfamily of Proteins. J. Cell Biol. 157 (2002) 243-251
    • (2002) J. Cell Biol. , vol.157 , pp. 243-251
    • Galkin, V.E.1    Orlova, A.2    VanLoock, M.S.3    Rybakova, I.N.4    Ervasti, J.M.5    Egelman, E.H.6
  • 21
    • 13844297588 scopus 로고    scopus 로고
    • Single particle analysis of relaxed and activated muscle thin filaments
    • Pirani A., Xu C., Hatch V., Craig R., Tobacman L.S., and Lehman W. Single particle analysis of relaxed and activated muscle thin filaments. J. Mol. Biol. 346 (2005) 761-772
    • (2005) J. Mol. Biol. , vol.346 , pp. 761-772
    • Pirani, A.1    Xu, C.2    Hatch, V.3    Craig, R.4    Tobacman, L.S.5    Lehman, W.6
  • 23
    • 44349162159 scopus 로고    scopus 로고
    • Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures
    • Chen Z., Yang H., and Pavletich N.P. Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures. Nature 453 (2008) 448-489
    • (2008) Nature , vol.453 , pp. 448-489
    • Chen, Z.1    Yang, H.2    Pavletich, N.P.3
  • 25
    • 33847745055 scopus 로고    scopus 로고
    • Snapshots of RecA protein involving movement of the C-domain and different conformations of the DNA-binding loops: crystallographic and comparative analysis of 11 structures of Mycobacterium smegmatis RecA
    • Krishna R., Prabu J.R., Manjunath G.P., Datta S., Chandra N.R., Muniyappa K., and Vijayan M. Snapshots of RecA protein involving movement of the C-domain and different conformations of the DNA-binding loops: crystallographic and comparative analysis of 11 structures of Mycobacterium smegmatis RecA. J. Mol. Biol. 367 (2007) 1130-1144
    • (2007) J. Mol. Biol. , vol.367 , pp. 1130-1144
    • Krishna, R.1    Prabu, J.R.2    Manjunath, G.P.3    Datta, S.4    Chandra, N.R.5    Muniyappa, K.6    Vijayan, M.7
  • 26
    • 0035902614 scopus 로고    scopus 로고
    • Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA
    • Yu X., Jacobs S.A., West S.C., Ogawa T., and Egelman E.H. Domain structure and dynamics in the helical filaments formed by RecA and Rad51 on DNA. Proc. Natl Acad. Sci. USA 98 (2001) 8419-8424
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 8419-8424
    • Yu, X.1    Jacobs, S.A.2    West, S.C.3    Ogawa, T.4    Egelman, E.H.5
  • 28
  • 30
    • 0023685553 scopus 로고
    • Increase of the DNA strand assimilation activity of recA protein by removal of the C terminus and structure-function studies of the resulting protein fragment
    • Benedict R.C., and Kowalczykowski S.C. Increase of the DNA strand assimilation activity of recA protein by removal of the C terminus and structure-function studies of the resulting protein fragment. J. Biol. Chem. 263 (1988) 15513-15520
    • (1988) J. Biol. Chem. , vol.263 , pp. 15513-15520
    • Benedict, R.C.1    Kowalczykowski, S.C.2
  • 31
    • 0038276074 scopus 로고    scopus 로고
    • The C Terminus of the Escherichia coli RecA Protein Modulates the DNA Binding Competition with Single-stranded DNA-binding Protein
    • Eggler A.L., Lusetti S.L., and Cox M.M. The C Terminus of the Escherichia coli RecA Protein Modulates the DNA Binding Competition with Single-stranded DNA-binding Protein. J. Biol. Chem. 278 (2003) 16389-16396
    • (2003) J. Biol. Chem. , vol.278 , pp. 16389-16396
    • Eggler, A.L.1    Lusetti, S.L.2    Cox, M.M.3
  • 34
    • 0026527367 scopus 로고
    • C-terminal truncated Escherichia coli RecA protein RecA5327 has enhanced binding affinities to single- and double-stranded DNAs
    • Tateishi S., Horii T., Ogawa T., and Ogawa H. C-terminal truncated Escherichia coli RecA protein RecA5327 has enhanced binding affinities to single- and double-stranded DNAs. J. Mol. Biol. 223 (1992) 115-129
    • (1992) J. Mol. Biol. , vol.223 , pp. 115-129
    • Tateishi, S.1    Horii, T.2    Ogawa, T.3    Ogawa, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.