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Volumn 355, Issue 3, 2006, Pages 473-490

RuvA is a sliding collar that protects holliday junctions from unwinding while promoting branch migration

Author keywords

Branch migration; DNA recombination; DNA replication; Holliday junction; RuvA

Indexed keywords

DNA;

EID: 28944448182     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.10.075     Document Type: Article
Times cited : (7)

References (51)
  • 1
    • 0035997347 scopus 로고    scopus 로고
    • The bacterial RecA protein and the recombinational DNA repair of stalled replication forks
    • S.L. Lusetti, and M.M. Cox The bacterial RecA protein and the recombinational DNA repair of stalled replication forks Annu. Rev. Biochem. 71 2002 71 100
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 71-100
    • Lusetti, S.L.1    Cox, M.M.2
  • 2
    • 0031453378 scopus 로고    scopus 로고
    • Processing of recombination intermediates by the RuvABC proteins
    • S.C. West Processing of recombination intermediates by the RuvABC proteins Annu. Rev. Genet. 31 1997 213 244
    • (1997) Annu. Rev. Genet. , vol.31 , pp. 213-244
    • West, S.C.1
  • 3
    • 0028968305 scopus 로고
    • Structure of a multisubunit complex that promotes DNA branch migration
    • C.A. Parsons, A. Stasiak, R.J. Bennett, and S.C. West Structure of a multisubunit complex that promotes DNA branch migration Nature 374 1995 375 378
    • (1995) Nature , vol.374 , pp. 375-378
    • Parsons, C.A.1    Stasiak, A.2    Bennett, R.J.3    West, S.C.4
  • 4
    • 0031581811 scopus 로고    scopus 로고
    • Structure and subunit composition of the RuvAB-Holliday junction complex
    • X. Yu, S.C. West, and E.H. Egelman Structure and subunit composition of the RuvAB-Holliday junction complex J. Mol. Biol. 266 1997 217 222
    • (1997) J. Mol. Biol. , vol.266 , pp. 217-222
    • Yu, X.1    West, S.C.2    Egelman, E.H.3
  • 5
    • 0026633047 scopus 로고
    • ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E. coli
    • I.R. Tsaneva, B. Muller, and S.C. West ATP-dependent branch migration of Holliday junctions promoted by the RuvA and RuvB proteins of E. coli Cell 69 1992 1171 1180
    • (1992) Cell , vol.69 , pp. 1171-1180
    • Tsaneva, I.R.1    Muller, B.2    West, S.C.3
  • 6
    • 0030727120 scopus 로고    scopus 로고
    • In vitro reconstitution of the late steps of genetic recombination in E. coli
    • A.K. Eggleston, A.H. Mitchell, and S.C. West In vitro reconstitution of the late steps of genetic recombination in E. coli Cell 89 1997 607 617
    • (1997) Cell , vol.89 , pp. 607-617
    • Eggleston, A.K.1    Mitchell, A.H.2    West, S.C.3
  • 7
    • 0034714309 scopus 로고    scopus 로고
    • Cleavage of Holliday junctions by the Escherichia coli RivABC complex
    • A.K. Eggleston, and S.C. West Cleavage of Holliday junctions by the Escherichia coli RivABC complex J. Biol. Chem. 275 2000 26467 26476
    • (2000) J. Biol. Chem. , vol.275 , pp. 26467-26476
    • Eggleston, A.K.1    West, S.C.2
  • 8
    • 0034669196 scopus 로고    scopus 로고
    • The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome
    • S.M. Ingleston, G.J. Sharples, and R.G. Lloyd The acidic pin of RuvA modulates Holliday junction binding and processing by the RuvABC resolvasome EMBO J. 19 2000 6266 6274
    • (2000) EMBO J. , vol.19 , pp. 6266-6274
    • Ingleston, S.M.1    Sharples, G.J.2    Lloyd, R.G.3
  • 11
    • 18644379392 scopus 로고    scopus 로고
    • Crystal structure of the RuvA-RuvB complex: A structural basis for the Holliday junction migrating motor machinery
    • K. Yamada, T. Miyata, D. Tsuchiya, T. Oyama, Y. Fujiwara, and T. Ohnishi Crystal structure of the RuvA-RuvB complex: a structural basis for the Holliday junction migrating motor machinery Mol. Cell 10 2002 671 681
    • (2002) Mol. Cell , vol.10 , pp. 671-681
    • Yamada, K.1    Miyata, T.2    Tsuchiya, D.3    Oyama, T.4    Fujiwara, Y.5    Ohnishi, T.6
  • 12
    • 0035852703 scopus 로고    scopus 로고
    • Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8
    • K. Yamada, N. Kunishima, K. Mayanagi, T. Ohnishi, T. Nishino, and H. Iwasaki Crystal structure of the Holliday junction migration motor protein RuvB from Thermus thermophilus HB8 Proc. Natl Acad. Sci. USA 98 2001 1442 1447
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 1442-1447
    • Yamada, K.1    Kunishima, N.2    Mayanagi, K.3    Ohnishi, T.4    Nishino, T.5    Iwasaki, H.6
  • 14
    • 0026741832 scopus 로고
    • Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions
    • C.A. Parsons, I. Tsaneva, R.G. Lloyd, and S.C. West Interaction of Escherichia coli RuvA and RuvB proteins with synthetic Holliday junctions Proc. Natl Acad. Sci. USA 89 1992 5452 5456
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 5452-5456
    • Parsons, C.A.1    Tsaneva, I.2    Lloyd, R.G.3    West, S.C.4
  • 15
    • 0028965153 scopus 로고
    • Branch migration during homologous recombination: Assembly of a RuvAB Holliday junction complex in vitro
    • K. Hiom, and S.C. West Branch migration during homologous recombination: assembly of a RuvAB Holliday junction complex in vitro Cell 80 1995 787 793
    • (1995) Cell , vol.80 , pp. 787-793
    • Hiom, K.1    West, S.C.2
  • 16
    • 0027184479 scopus 로고
    • Branch migration of Holliday junctions promoted by the Escherichia coli RuvA and RuvB proteins. II. Interaction of RuvB with DNA
    • B. Muller, I.R. Tsaneva, and S.C. West Branch migration of Holliday junctions promoted by the Escherichia coli RuvA and RuvB proteins. II. Interaction of RuvB with DNA J. Biol. Chem. 268 1993 17185 17189
    • (1993) J. Biol. Chem. , vol.268 , pp. 17185-17189
    • Muller, B.1    Tsaneva, I.R.2    West, S.C.3
  • 17
    • 0033786801 scopus 로고    scopus 로고
    • Structure and function of hexameric helicases
    • S.S. Patel, and K.M. Picha Structure and function of hexameric helicases Annu. Rev. Biochem. 69 2000 651 697
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 651-697
    • Patel, S.S.1    Picha, K.M.2
  • 18
    • 0032716810 scopus 로고    scopus 로고
    • Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7
    • M.R. Sawaya, S. Guo, S. Tabor, C.C. Richardson, and T. Ellenberger Crystal structure of the helicase domain from the replicative helicase-primase of bacteriophage T7 Cell 99 1999 167 177
    • (1999) Cell , vol.99 , pp. 167-177
    • Sawaya, M.R.1    Guo, S.2    Tabor, S.3    Richardson, C.C.4    Ellenberger, T.5
  • 19
    • 0034625236 scopus 로고    scopus 로고
    • Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides
    • M.R. Singleton, M.R. Sawaya, T. Ellenberger, and D.B. Wigley Crystal structure of T7 gene 4 ring helicase indicates a mechanism for sequential hydrolysis of nucleotides Cell 101 2000 589 600
    • (2000) Cell , vol.101 , pp. 589-600
    • Singleton, M.R.1    Sawaya, M.R.2    Ellenberger, T.3    Wigley, D.B.4
  • 20
    • 0023046634 scopus 로고
    • Extensive unwinding of the plasmid template during staged enzymatic initiation of DNA replication from the origin of the Escherichia coli chromosome
    • T.A. Baker, K. Sekimizu, B.E. Funnell, and A. Kornberg Extensive unwinding of the plasmid template during staged enzymatic initiation of DNA replication from the origin of the Escherichia coli chromosome Cell 45 1986 53 64
    • (1986) Cell , vol.45 , pp. 53-64
    • Baker, T.A.1    Sekimizu, K.2    Funnell, B.E.3    Kornberg, A.4
  • 21
    • 0028046581 scopus 로고
    • Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein
    • W. Bujalowski, M.M. Klonowska, and M.J. Jezewska Oligomeric structure of Escherichia coli primary replicative helicase DnaB protein J. Biol. Chem. 269 1994 31350 31358
    • (1994) J. Biol. Chem. , vol.269 , pp. 31350-31358
    • Bujalowski, W.1    Klonowska, M.M.2    Jezewska, M.J.3
  • 22
    • 0036385791 scopus 로고    scopus 로고
    • Flexibility of the rings: Structural asymmetry in the DnaB hexameric helicase
    • S. Yang, X. Yu, M. VanLoock, M. Jezewska, W. Bujalowski, and E. Egelman Flexibility of the rings: structural asymmetry in the DnaB hexameric helicase J. Mol. Biol. 321 2002 839 849
    • (2002) J. Mol. Biol. , vol.321 , pp. 839-849
    • Yang, S.1    Yu, X.2    Vanloock, M.3    Jezewska, M.4    Bujalowski, W.5    Egelman, E.6
  • 23
    • 0032562822 scopus 로고    scopus 로고
    • Does single-stranded DNA pass through the inner channel of the protein hexamer in complex with the Escherichia coli DnaB helicase? Fluorescence energy transfer studies
    • M.J. Jezewska, S. Rajendran, D. Bujalowska, and W. Bujalowski Does single-stranded DNA pass through the inner channel of the protein hexamer in complex with the Escherichia coli DnaB helicase? Fluorescence energy transfer studies J. Biol. Chem. 273 1998 10515 10529
    • (1998) J. Biol. Chem. , vol.273 , pp. 10515-10529
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowska, D.3    Bujalowski, W.4
  • 24
    • 0034636979 scopus 로고    scopus 로고
    • The 3′-tail of a forked-duplex sterically determines whether one or two DNA strands pass through the central channel of a replication-fork helicase
    • D.L. Kaplan The 3′-tail of a forked-duplex sterically determines whether one or two DNA strands pass through the central channel of a replication-fork helicase J. Mol. Biol. 301 2000 285 299
    • (2000) J. Mol. Biol. , vol.301 , pp. 285-299
    • Kaplan, D.L.1
  • 25
    • 0032478286 scopus 로고    scopus 로고
    • Complex of Escherichia coli primary replicative helicase DnaB protein with a replication fork: Recognition and structure
    • M.J. Jezewska, S. Rajendran, and W. Bujalowski Complex of Escherichia coli primary replicative helicase DnaB protein with a replication fork: recognition and structure Biochemistry 37 1998 3116 3136
    • (1998) Biochemistry , vol.37 , pp. 3116-3136
    • Jezewska, M.J.1    Rajendran, S.2    Bujalowski, W.3
  • 26
    • 0037294467 scopus 로고    scopus 로고
    • Helicase mechanisms and the coupling of helicases within macromolecular machines. Part II: Integration of helicases into cellular processes
    • E. Delagoutte, and P.H. von Hippel Helicase mechanisms and the coupling of helicases within macromolecular machines. Part II: integration of helicases into cellular processes Quart. Rev. Biophys. 36 2003 1 69
    • (2003) Quart. Rev. Biophys. , vol.36 , pp. 1-69
    • Delagoutte, E.1    Von Hippel, P.H.2
  • 27
    • 0024604814 scopus 로고
    • Characterization of the bacteriophage T4 gene 41 DNA helicase
    • R.W. Richardson, and N.G. Nossal Characterization of the bacteriophage T4 gene 41 DNA helicase J. Biol. Chem. 264 1989 4725 4731
    • (1989) J. Biol. Chem. , vol.264 , pp. 4725-4731
    • Richardson, R.W.1    Nossal, N.G.2
  • 28
    • 13844254122 scopus 로고    scopus 로고
    • Unraveling the early steps of prokaryotic replication
    • E.L. Cunningham, and J.M. Berger Unraveling the early steps of prokaryotic replication Curr. Opin. Struct. Biol. 15 2005 68 76
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 68-76
    • Cunningham, E.L.1    Berger, J.M.2
  • 29
    • 0036753338 scopus 로고    scopus 로고
    • DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands
    • D.L. Kaplan, and M. O'Donnell DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands Mol. Cell 10 2002 647 657
    • (2002) Mol. Cell , vol.10 , pp. 647-657
    • Kaplan, D.L.1    O'Donnell, M.2
  • 30
    • 0034634365 scopus 로고    scopus 로고
    • Multiple-step kinetic mechanism of DNA-independent ATP binding and hydrolysis by Escherichia coli replicative helicase DnaB protein: Quantitative analysis using the rapid quench-flow method
    • S. Rajendran, M.J. Jezewska, and W. Bujalowski Multiple-step kinetic mechanism of DNA-independent ATP binding and hydrolysis by Escherichia coli replicative helicase DnaB protein: quantitative analysis using the rapid quench-flow method J. Mol. Biol. 303 2000 773 795
    • (2000) J. Mol. Biol. , vol.303 , pp. 773-795
    • Rajendran, S.1    Jezewska, M.J.2    Bujalowski, W.3
  • 31
    • 0027476446 scopus 로고
    • RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro
    • I.R. Tsaneva, B. Muller, and S.C. West RuvA and RuvB proteins of Escherichia coli exhibit DNA helicase activity in vitro Proc. Natl Acad. Sci. USA 90 1993 1315 1319
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 1315-1319
    • Tsaneva, I.R.1    Muller, B.2    West, S.C.3
  • 32
    • 0022977660 scopus 로고
    • The Escherichia coli dnaB replication protein is a DNA helicase
    • J.H. LeBowitz, and R. McMacken The Escherichia coli dnaB replication protein is a DNA helicase J. Biol. Chem. 261 1986 4738 4748
    • (1986) J. Biol. Chem. , vol.261 , pp. 4738-4748
    • Lebowitz, J.H.1    McMacken, R.2
  • 33
    • 0032161224 scopus 로고    scopus 로고
    • Migration of a Holliday junction through a nucleosome directed by the E. coli RuvAB motor protein
    • M. Grigoriev, and P. Hsieh Migration of a Holliday junction through a nucleosome directed by the E. coli RuvAB motor protein Mol. Cell 2 1998 373 381
    • (1998) Mol. Cell , vol.2 , pp. 373-381
    • Grigoriev, M.1    Hsieh, P.2
  • 34
    • 0028067935 scopus 로고
    • RuvA and RuvB proteins facilitate the bypass of heterolgous DNA insertions during RecA protein-mediated DNA strand exchange
    • L.E. Iype, E.E. Wood, R.B. Inman, and M.M. Cox RuvA and RuvB proteins facilitate the bypass of heterolgous DNA insertions during RecA protein-mediated DNA strand exchange J. Biol. Chem. 269 1994 24967 24978
    • (1994) J. Biol. Chem. , vol.269 , pp. 24967-24978
    • Iype, L.E.1    Wood, E.E.2    Inman, R.B.3    Cox, M.M.4
  • 35
    • 4143151757 scopus 로고    scopus 로고
    • Twin DNA pumps of a hexameric helicase provide power to simultaneously melt two duplexes
    • D.L. Kaplan, and M. O'Donnell Twin DNA pumps of a hexameric helicase provide power to simultaneously melt two duplexes Mol. Cell 15 2004 453 465
    • (2004) Mol. Cell , vol.15 , pp. 453-465
    • Kaplan, D.L.1    O'Donnell, M.2
  • 36
    • 0030575805 scopus 로고    scopus 로고
    • Bypass of DNA heterologies during RuvAB-mediated three and four-strand branch migration
    • D.E. Adams, and S.C. West Bypass of DNA heterologies during RuvAB-mediated three and four-strand branch migration J. Mol. Biol. 263 1996 582 596
    • (1996) J. Mol. Biol. , vol.263 , pp. 582-596
    • Adams, D.E.1    West, S.C.2
  • 37
    • 0141635255 scopus 로고    scopus 로고
    • Uncoupling of the ATPase activity from the branch migration activity of RuvAB protein complexes containing both wild-type and ATPase-defective RuvB proteins
    • T. Hishida, H. Iwasaki, Y.W. Han, T. Ohnishi, and H. Shinagawa Uncoupling of the ATPase activity from the branch migration activity of RuvAB protein complexes containing both wild-type and ATPase-defective RuvB proteins Genes Cells 8 2003 721 730
    • (2003) Genes Cells , vol.8 , pp. 721-730
    • Hishida, T.1    Iwasaki, H.2    Han, Y.W.3    Ohnishi, T.4    Shinagawa, H.5
  • 38
    • 3242714067 scopus 로고    scopus 로고
    • RuvAB-directed branch migration of individual Holliday junctions is impeded by sequence heterology
    • C. Dennis, A. Fedorov, E. Kas, L. Salome, and M. Grigoriev RuvAB-directed branch migration of individual Holliday junctions is impeded by sequence heterology EMBO J. 23 2004 2413 2422
    • (2004) EMBO J. , vol.23 , pp. 2413-2422
    • Dennis, C.1    Fedorov, A.2    Kas, E.3    Salome, L.4    Grigoriev, M.5
  • 39
    • 0035859954 scopus 로고    scopus 로고
    • Mechanism of termination of DNA replication of Escherichia coli involves helicase-contrahelicase interaction
    • S. Mulugu, A.P.A. Shamsuzzaman, J. Taylor, K. Alexander, and D. Bastia Mechanism of termination of DNA replication of Escherichia coli involves helicase-contrahelicase interaction Proc. Natl Acad. Sci. USA 98 2001 9569 9574
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 9569-9574
    • Mulugu, S.1    Shamsuzzaman, A.P.A.2    Taylor, J.3    Alexander, K.4    Bastia, D.5
  • 41
    • 0025798966 scopus 로고
    • Escherichia coli replication terminator protein impedes simian virus 40 (SV40) DNA replication fork movement and SV40 large tumor antigen helicase activity in vitro at a prokaryotic terminus sequence
    • C.L. Bedrosian, and D. Bastia Escherichia coli replication terminator protein impedes simian virus 40 (SV40) DNA replication fork movement and SV40 large tumor antigen helicase activity in vitro at a prokaryotic terminus sequence Proc. Natl Acad. Sci. USA 88 1991 2618 2622
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2618-2622
    • Bedrosian, C.L.1    Bastia, D.2
  • 42
    • 0029026635 scopus 로고
    • DNA polymerase III holoenzyme: Structure and function of a chromosomal replicating machine
    • Z. Kelman, and M. O'Donnell DNA polymerase III holoenzyme: structure and function of a chromosomal replicating machine Annu. Rev. Biochem. 64 1995 171 200
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 171-200
    • Kelman, Z.1    O'Donnell, M.2
  • 43
    • 0034602163 scopus 로고    scopus 로고
    • The delta subunit of DNA polymerase III holoenzyme serves as a sliding clamp unloader in Escherichia coli
    • F.P. Leu, M.M. Hingorani, J. Turner, and M. O'Donnell The delta subunit of DNA polymerase III holoenzyme serves as a sliding clamp unloader in Escherichia coli J. Biol. Chem. 275 2000 34609 34618
    • (2000) J. Biol. Chem. , vol.275 , pp. 34609-34618
    • Leu, F.P.1    Hingorani, M.M.2    Turner, J.3    O'Donnell, M.4
  • 44
    • 0026717535 scopus 로고
    • Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme is a sliding DNA clamp
    • X.P. Kong, R.O. Onrust, M. O'Donnell, and J. Kuriyan Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme is a sliding DNA clamp Cell 69 1992 425 437
    • (1992) Cell , vol.69 , pp. 425-437
    • Kong, X.P.1    Onrust, R.O.2    O'Donnell, M.3    Kuriyan, J.4
  • 45
    • 0025809742 scopus 로고
    • Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme
    • P.T. Stukenberg, P.S. Studwell-Vaughan, and M. O'Donnell Mechanism of the sliding beta-clamp of DNA polymerase III holoenzyme J. Biol. Chem. 266 1991 11328 11334
    • (1991) J. Biol. Chem. , vol.266 , pp. 11328-11334
    • Stukenberg, P.T.1    Studwell-Vaughan, P.S.2    O'Donnell, M.3
  • 47
    • 0142106381 scopus 로고    scopus 로고
    • A tetramer-octamer equilibrium in Mycobacterium leprae and Escherichia coli RuvA by analytical ultracentrifugation
    • Y.C. Lee, R. Flora, J.A. McCafferty, J. Gor, I.R. Tsaneva, and S.J. Perkins A tetramer-octamer equilibrium in Mycobacterium leprae and Escherichia coli RuvA by analytical ultracentrifugation J. Mol. Biol. 333 2003 677 682
    • (2003) J. Mol. Biol. , vol.333 , pp. 677-682
    • Lee, Y.C.1    Flora, R.2    McCafferty, J.A.3    Gor, J.4    Tsaneva, I.R.5    Perkins, S.J.6
  • 48
    • 0033634983 scopus 로고    scopus 로고
    • Structure of BamHI bound to nonspecific DNA: A model for DNA sliding
    • H. Viadiu, and A.K. Aggarwal Structure of BamHI bound to nonspecific DNA: a model for DNA sliding Mol. Cell 5 2000 889 895
    • (2000) Mol. Cell , vol.5 , pp. 889-895
    • Viadiu, H.1    Aggarwal, A.K.2
  • 49
    • 4644265622 scopus 로고    scopus 로고
    • Obstacle bypass in protein motion along DNA by two-dimensional rather than one-dimensional sliding
    • M. Kampmann Obstacle bypass in protein motion along DNA by two-dimensional rather than one-dimensional sliding J. Biol. Chem. 279 2004 38715 38720
    • (2004) J. Biol. Chem. , vol.279 , pp. 38715-38720
    • Kampmann, M.1
  • 50
    • 0026444104 scopus 로고
    • Purification and properties of the RuvA and RuvB proteins of Escherichia coli
    • I. Tsaneva, G. Illing, R. Lloyd, and S. West Purification and properties of the RuvA and RuvB proteins of Escherichia coli Mol. Gen Genet. 235 1992 1 10
    • (1992) Mol. Gen Genet. , vol.235 , pp. 1-10
    • Tsaneva, I.1    Illing, G.2    Lloyd, R.3    West, S.4
  • 51
    • 0030595331 scopus 로고    scopus 로고
    • Replisome assembly reveals the basis for asymmetric function in leading and lagging strand replication
    • A. Yuzhakov, J. Turner, and M. O'Donnell Replisome assembly reveals the basis for asymmetric function in leading and lagging strand replication Cell 86 1996 877 886
    • (1996) Cell , vol.86 , pp. 877-886
    • Yuzhakov, A.1    Turner, J.2    O'Donnell, M.3


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