메뉴 건너뛰기




Volumn 51, Issue 13, 2012, Pages 2921-2929

Translocation of E. coli RecQ helicase on single-stranded DNA

Author keywords

[No Author keywords available]

Indexed keywords

ATP HYDROLYSIS; ATP-HYDROLYSIS ACTIVITY; DNA LENGTH; DOUBLE-STRANDED DNA BREAKS; E. COLI; GAP SIZE; HELICASES; HILL COEFFICIENT; KINETIC MODELS; LATTICE OCCUPANCY; PROCESSIVITY; RECQ HELICASES; SINGLE-STRANDED DNA; SINGLE-STRANDED DNA (SS-DNA); SPECIFIC ACTIVITY; UNWINDING ACTIVITY;

EID: 84859397679     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3000676     Document Type: Article
Times cited : (15)

References (48)
  • 1
    • 0035951425 scopus 로고    scopus 로고
    • A general model for nucleic acid helicases and their "coupling" within macromolecular machines
    • von Hippel, P. H. and Delagoutte, E. (2001) A general model for nucleic acid helicases and their "coupling" within macromolecular machines Cell 104, 177-190
    • (2001) Cell , vol.104 , pp. 177-190
    • Von Hippel, P.H.1    Delagoutte, E.2
  • 2
    • 34548638261 scopus 로고    scopus 로고
    • Structure and mechanism of helicases and nucleic acid translocases
    • Singleton, M. R., Dillingham, M. S., and Wigley, D. B. (2007) Structure and mechanism of helicases and nucleic acid translocases Annu. Rev. Biochem. 76, 23-50
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 23-50
    • Singleton, M.R.1    Dillingham, M.S.2    Wigley, D.B.3
  • 3
    • 0037673943 scopus 로고    scopus 로고
    • The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments
    • Veaute, X., Jeusset, J., Soustelle, C., Kowalczykowski, S. C., Le Cam, E., and Fabre, F. (2003) The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments Nature 423, 309-312
    • (2003) Nature , vol.423 , pp. 309-312
    • Veaute, X.1    Jeusset, J.2    Soustelle, C.3    Kowalczykowski, S.C.4    Le Cam, E.5    Fabre, F.6
  • 4
    • 67649637509 scopus 로고    scopus 로고
    • Srs2 disassembles Rad51 filaments by a protein-protein interaction triggering ATP turnover and dissociation of Rad51 from DNA
    • Antony, E., Tomko, E. J., Xiao, Q., Krejci, L., Lohman, T. M., and Ellenberger, T. (2009) Srs2 disassembles Rad51 filaments by a protein-protein interaction triggering ATP turnover and dissociation of Rad51 from DNA Mol. Cell 35, 105-115
    • (2009) Mol. Cell , vol.35 , pp. 105-115
    • Antony, E.1    Tomko, E.J.2    Xiao, Q.3    Krejci, L.4    Lohman, T.M.5    Ellenberger, T.6
  • 6
    • 0037115947 scopus 로고    scopus 로고
    • RecQ family helicases: Roles as tumor suppressor proteins
    • Nakayama, H. (2002) RecQ family helicases: roles as tumor suppressor proteins Oncogene 21, 9008-9021
    • (2002) Oncogene , vol.21 , pp. 9008-9021
    • Nakayama, H.1
  • 7
    • 24044549679 scopus 로고    scopus 로고
    • Escherichia coli RecQ helicase: A player in thymineless death
    • Nakayama, H. (2005) Escherichia coli RecQ helicase: a player in thymineless death Mutat. Res. 577, 228-236
    • (2005) Mutat. Res. , vol.577 , pp. 228-236
    • Nakayama, H.1
  • 8
    • 0021185614 scopus 로고
    • Isolation and genetic characterization of a thymineless death-resistant mutant of Escherichia coli K-12: Identification of a new mutation (recQ1) that blocks the recF recombination pathway
    • Nakayama, H., Nakayama, K., Nakayama, R., Irino, N., Nakayama, Y., and Hanawalt, P. C. (1984) Isolation and genetic characterization of a thymineless death-resistant mutant of Escherichia coli K-12: Identification of a new mutation (recQ1) that blocks the recF recombination pathway Mol. Gen. Genet. 195, 474-480
    • (1984) Mol. Gen. Genet. , vol.195 , pp. 474-480
    • Nakayama, H.1    Nakayama, K.2    Nakayama, R.3    Irino, N.4    Nakayama, Y.5    Hanawalt, P.C.6
  • 9
    • 0032740855 scopus 로고    scopus 로고
    • RecQ and RecJ process blocked replication forks prior to the resumption of replication in UV-irradiated Escherichia coli
    • Courcelle, J. and Hanawalt, P. C. (1999) RecQ and RecJ process blocked replication forks prior to the resumption of replication in UV-irradiated Escherichia coli Mol. Gen. Genet. 262, 543-551
    • (1999) Mol. Gen. Genet. , vol.262 , pp. 543-551
    • Courcelle, J.1    Hanawalt, P.C.2
  • 11
    • 0345587483 scopus 로고
    • Identification and purification of a single-stranded-DNA-specific exonuclease encoded by the recJ gene of Escherichia coli
    • Lovett, S. T. and Kolodner, R. D. (1989) Identification and purification of a single-stranded-DNA-specific exonuclease encoded by the recJ gene of Escherichia coli Proc. Natl. Acad. Sci. U. S. A. 86, 2627-2631
    • (1989) Proc. Natl. Acad. Sci. U. S. A. , vol.86 , pp. 2627-2631
    • Lovett, S.T.1    Kolodner, R.D.2
  • 12
    • 66149130735 scopus 로고    scopus 로고
    • Reconstitution of initial steps of dsDNA break repair by the RecF pathway of E. coli
    • Handa, N., Morimatsu, K., Lovett, S. T., and Kowalczykowski, S. C. (2009) Reconstitution of initial steps of dsDNA break repair by the RecF pathway of E. coli Genes Dev. 23, 1234-1245
    • (2009) Genes Dev. , vol.23 , pp. 1234-1245
    • Handa, N.1    Morimatsu, K.2    Lovett, S.T.3    Kowalczykowski, S.C.4
  • 13
  • 14
    • 0032522789 scopus 로고    scopus 로고
    • RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination
    • Harmon, F. G. and Kowalczykowski, S. C. (1998) RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination Genes Dev. 12, 1134-1144
    • (1998) Genes Dev. , vol.12 , pp. 1134-1144
    • Harmon, F.G.1    Kowalczykowski, S.C.2
  • 15
    • 0142180061 scopus 로고    scopus 로고
    • RecQ helicase stimulates both DNA catenation and changes in DNA topology by topoisomerase III
    • Harmon, F. G., Brockman, J. P., and Kowalczykowski, S. C. (2003) RecQ helicase stimulates both DNA catenation and changes in DNA topology by topoisomerase III J. Biol. Chem. 278, 42668-42678
    • (2003) J. Biol. Chem. , vol.278 , pp. 42668-42678
    • Harmon, F.G.1    Brockman, J.P.2    Kowalczykowski, S.C.3
  • 16
    • 0033031935 scopus 로고    scopus 로고
    • RecQ helicase and topoisomerase III comprise a novel DNA strand passage function: A conserved mechanism for control of DNA recombination
    • Harmon, F. G., DiGate, R. J., and Kowalczykowski, S. C. (1999) RecQ helicase and topoisomerase III comprise a novel DNA strand passage function: a conserved mechanism for control of DNA recombination Mol. Cell 3, 611-620
    • (1999) Mol. Cell , vol.3 , pp. 611-620
    • Harmon, F.G.1    Digate, R.J.2    Kowalczykowski, S.C.3
  • 17
    • 0037364415 scopus 로고    scopus 로고
    • RecQ helicases: Caretakers of the genome
    • Hickson, I. D. (2003) RecQ helicases: caretakers of the genome Nat. Rev. Cancer 3, 169-178
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 169-178
    • Hickson, I.D.1
  • 18
    • 0347987856 scopus 로고    scopus 로고
    • The Blooms syndrome helicase suppresses crossing over during homologous recombination
    • Wu, L. and Hickson, I. D. (2003) The Blooms syndrome helicase suppresses crossing over during homologous recombination Nature 426, 870-874
    • (2003) Nature , vol.426 , pp. 870-874
    • Wu, L.1    Hickson, I.D.2
  • 19
    • 33746600628 scopus 로고    scopus 로고
    • Topoisomerase IIIα and Blooms helicase can resolve a mobile double Holliday junction substrate through convergent branch migration
    • Plank, J. L., Wu, J., and Hsieh, T. S. (2006) Topoisomerase IIIα and Blooms helicase can resolve a mobile double Holliday junction substrate through convergent branch migration Proc. Natl. Acad. Sci. U. S. A. 103, 11118-11123
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 11118-11123
    • Plank, J.L.1    Wu, J.2    Hsieh, T.S.3
  • 21
    • 44949225070 scopus 로고    scopus 로고
    • Resolution of converging replication forks by RecQ and topoisomerase III
    • Suski, C. and Marians, K. J. (2008) Resolution of converging replication forks by RecQ and topoisomerase III Mol. Cell 30, 779-789
    • (2008) Mol. Cell , vol.30 , pp. 779-789
    • Suski, C.1    Marians, K.J.2
  • 22
    • 0027158626 scopus 로고
    • RecQ DNA helicase of Escherichia coli. Characterization of the helix-unwinding activity with emphasis on the effect of single-stranded DNA-binding protein
    • Umezu, K. and Nakayama, H. (1993) RecQ DNA helicase of Escherichia coli. Characterization of the helix-unwinding activity with emphasis on the effect of single-stranded DNA-binding protein J. Mol. Biol. 230, 1145-1150
    • (1993) J. Mol. Biol. , vol.230 , pp. 1145-1150
    • Umezu, K.1    Nakayama, H.2
  • 23
    • 3543089707 scopus 로고    scopus 로고
    • Role of the Escherichia coli RecQ DNA helicase in SOS signaling and genome stabilization at stalled replication forks
    • Hishida, T., Han, Y. W., Shibata, T., Kubota, Y., Ishino, Y., Iwasaki, H., and Shinagawa, H. (2004) Role of the Escherichia coli RecQ DNA helicase in SOS signaling and genome stabilization at stalled replication forks Genes Dev. 18, 1886-1897
    • (2004) Genes Dev. , vol.18 , pp. 1886-1897
    • Hishida, T.1    Han, Y.W.2    Shibata, T.3    Kubota, Y.4    Ishino, Y.5    Iwasaki, H.6    Shinagawa, H.7
  • 24
    • 0035808456 scopus 로고    scopus 로고
    • Biochemical characterization of the DNA helicase activity of the Escherichia coli RecQ helicase
    • Harmon, F. G. and Kowalczykowski, S. C. (2001) Biochemical characterization of the DNA helicase activity of the Escherichia coli RecQ helicase J. Biol. Chem. 276, 232-243
    • (2001) J. Biol. Chem. , vol.276 , pp. 232-243
    • Harmon, F.G.1    Kowalczykowski, S.C.2
  • 25
    • 34547121734 scopus 로고    scopus 로고
    • A central role for SSB in Escherichia coli RecQ DNA helicase function
    • Shereda, R. D., Bernstein, D. A., and Keck, J. L. (2007) A central role for SSB in Escherichia coli RecQ DNA helicase function J. Biol. Chem. 282, 19247-19258
    • (2007) J. Biol. Chem. , vol.282 , pp. 19247-19258
    • Shereda, R.D.1    Bernstein, D.A.2    Keck, J.L.3
  • 26
    • 1342346600 scopus 로고    scopus 로고
    • The DNA binding properties of the Escherichia coli RecQ helicase
    • Dou, S. X., Wang, P. Y., Xu, H. Q., and Xi, X. G. (2004) The DNA binding properties of the Escherichia coli RecQ helicase J. Biol. Chem. 279, 6354-6363
    • (2004) J. Biol. Chem. , vol.279 , pp. 6354-6363
    • Dou, S.X.1    Wang, P.Y.2    Xu, H.Q.3    Xi, X.G.4
  • 27
    • 33744951869 scopus 로고    scopus 로고
    • Escherichia coli RecQ is a rapid, efficient, and monomeric helicase
    • Zhang, X. D., Dou, S. X., Xie, P., Hu, J. S., Wang, P. Y., and Xi, X. G. (2006) Escherichia coli RecQ is a rapid, efficient, and monomeric helicase J. Biol. Chem. 281, 12655-12663
    • (2006) J. Biol. Chem. , vol.281 , pp. 12655-12663
    • Zhang, X.D.1    Dou, S.X.2    Xie, P.3    Hu, J.S.4    Wang, P.Y.5    Xi, X.G.6
  • 28
    • 0028275036 scopus 로고
    • Kinetic theory of ATP-driven translocases on one-dimensional polymer lattices
    • Young, M. C., Kuhl, S. B., and von Hippel, P. H. (1994) Kinetic theory of ATP-driven translocases on one-dimensional polymer lattices J. Mol. Biol. 235, 1436-1446
    • (1994) J. Mol. Biol. , vol.235 , pp. 1436-1446
    • Young, M.C.1    Kuhl, S.B.2    Von Hippel, P.H.3
  • 29
    • 0028217551 scopus 로고
    • Kinetic parameters of the translocation of bacteriophage T4 gene 41 protein helicase on single-stranded DNA
    • Young, M. C., Schultz, D. E., Ring, D., and von Hippel, P. H. (1994) Kinetic parameters of the translocation of bacteriophage T4 gene 41 protein helicase on single-stranded DNA J. Mol. Biol. 235, 1447-1458
    • (1994) J. Mol. Biol. , vol.235 , pp. 1447-1458
    • Young, M.C.1    Schultz, D.E.2    Ring, D.3    Von Hippel, P.H.4
  • 30
    • 0029118974 scopus 로고
    • Bacteriophage T4 Dda helicase translocates in a unidirectional fashion on single-stranded DNA
    • Raney, K. D. and Benkovic, S. J. (1995) Bacteriophage T4 Dda helicase translocates in a unidirectional fashion on single-stranded DNA J. Biol. Chem. 270, 22236-22242
    • (1995) J. Biol. Chem. , vol.270 , pp. 22236-22242
    • Raney, K.D.1    Benkovic, S.J.2
  • 32
    • 0018726495 scopus 로고
    • Purification of the T4 gene 32 protein free from detectable deoxyribonuclease activities
    • Bittner, M., Burke, R. L., and Alberts, B. M. (1979) Purification of the T4 gene 32 protein free from detectable deoxyribonuclease activities J. Biol. Chem. 254, 9565-9572
    • (1979) J. Biol. Chem. , vol.254 , pp. 9565-9572
    • Bittner, M.1    Burke, R.L.2    Alberts, B.M.3
  • 33
    • 0019321176 scopus 로고
    • A DNA-dependent ATPase from T4-infected E.coli Purification and properties of a 63,000-Dalton enzyme and its conversion to a 22,000-Dalton form
    • Panuska, J. R. and Goldthwait, D. A. (1980) A DNA-dependent ATPase from T4-infected E.coli Purification and properties of a 63,000-Dalton enzyme and its conversion to a 22,000-Dalton form J. Biol. Chem. 255, 5208-5214
    • (1980) J. Biol. Chem. , vol.255 , pp. 5208-5214
    • Panuska, J.R.1    Goldthwait, D.A.2
  • 34
    • 0019072839 scopus 로고
    • On the thermodynamics and kinetics of the cooperative binding of bacteriophage T4-coded gene 32 (helix destabilizing) protein to nucleic acid lattices
    • Kowalczykowski, S. C., Lonberg, N., Newport, J. W., Paul, L. S., and von Hippel, P. H. (1980) On the thermodynamics and kinetics of the cooperative binding of bacteriophage T4-coded gene 32 (helix destabilizing) protein to nucleic acid lattices Biophys. J. 32, 403-418
    • (1980) Biophys. J. , vol.32 , pp. 403-418
    • Kowalczykowski, S.C.1    Lonberg, N.2    Newport, J.W.3    Paul, L.S.4    Von Hippel, P.H.5
  • 35
    • 0026346185 scopus 로고
    • Gel retardation
    • Carey, J. (1991) Gel retardation Methods Enzymol. 208, 103-117
    • (1991) Methods Enzymol. , vol.208 , pp. 103-117
    • Carey, J.1
  • 36
    • 9244237061 scopus 로고    scopus 로고
    • ATP-dependent translocation of proteins along single-stranded DNA: Models and methods of analysis of pre-steady state kinetics
    • Fischer, C. J. and Lohman, T. M. (2004) ATP-dependent translocation of proteins along single-stranded DNA: models and methods of analysis of pre-steady state kinetics J. Mol. Biol. 344, 1265-1286
    • (2004) J. Mol. Biol. , vol.344 , pp. 1265-1286
    • Fischer, C.J.1    Lohman, T.M.2
  • 37
    • 0016175370 scopus 로고
    • Theoretical aspects of DNA-protein interactions: Co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice
    • McGhee, J. D. and von Hippel, P. H. (1974) Theoretical aspects of DNA-protein interactions: co-operative and non-co-operative binding of large ligands to a one-dimensional homogeneous lattice J. Mol. Biol. 86, 469-489
    • (1974) J. Mol. Biol. , vol.86 , pp. 469-489
    • McGhee, J.D.1    Von Hippel, P.H.2
  • 38
    • 84857137035 scopus 로고    scopus 로고
    • Efficient coupling of ATP hydrolysis to translocation by RecQ helicase
    • Rad, B. and Kowalczykowski, S. C. (2012) Efficient coupling of ATP hydrolysis to translocation by RecQ helicase Proc. Natl. Acad. Sci. U. S. A. 109, 1443-1448
    • (2012) Proc. Natl. Acad. Sci. U. S. A. , vol.109 , pp. 1443-1448
    • Rad, B.1    Kowalczykowski, S.C.2
  • 39
    • 0034635172 scopus 로고    scopus 로고
    • Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: Measurement of step size and translocation speed
    • Dillingham, M. S., Wigley, D. B., and Webb, M. R. (2000) Demonstration of unidirectional single-stranded DNA translocation by PcrA helicase: measurement of step size and translocation speed Biochemistry 39, 205-212
    • (2000) Biochemistry , vol.39 , pp. 205-212
    • Dillingham, M.S.1    Wigley, D.B.2    Webb, M.R.3
  • 40
    • 34247602963 scopus 로고    scopus 로고
    • A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA
    • Tomko, E. J., Fischer, C. J., Niedziela-Majka, A., and Lohman, T. M. (2007) A nonuniform stepping mechanism for E. coli UvrD monomer translocation along single-stranded DNA Mol. Cell 26, 335-347
    • (2007) Mol. Cell , vol.26 , pp. 335-347
    • Tomko, E.J.1    Fischer, C.J.2    Niedziela-Majka, A.3    Lohman, T.M.4
  • 41
    • 9244235535 scopus 로고    scopus 로고
    • Mechanism of ATP-dependent translocation of E.coli UvrD monomers along single-stranded DNA
    • Fischer, C. J., Maluf, N. K., and Lohman, T. M. (2004) Mechanism of ATP-dependent translocation of E.coli UvrD monomers along single-stranded DNA J. Mol. Biol. 344, 1287-1309
    • (2004) J. Mol. Biol. , vol.344 , pp. 1287-1309
    • Fischer, C.J.1    Maluf, N.K.2    Lohman, T.M.3
  • 42
    • 34848840105 scopus 로고    scopus 로고
    • Bacillus stearothermophilus PcrA monomer is a single-stranded DNA translocase but not a processive helicase in vitro
    • Niedziela-Majka, A., Chesnik, M. A., Tomko, E. J., and Lohman, T. M. (2007) Bacillus stearothermophilus PcrA monomer is a single-stranded DNA translocase but not a processive helicase in vitro J. Biol. Chem. 282, 27076-27085
    • (2007) J. Biol. Chem. , vol.282 , pp. 27076-27085
    • Niedziela-Majka, A.1    Chesnik, M.A.2    Tomko, E.J.3    Lohman, T.M.4
  • 43
    • 65249083349 scopus 로고    scopus 로고
    • Kinetic mechanism for single-stranded DNA binding and translocation by Saccharomyces cerevisiae Isw2
    • Fischer, C. J., Yamada, K., and Fitzgerald, D. J. (2009) Kinetic mechanism for single-stranded DNA binding and translocation by Saccharomyces cerevisiae Isw2 Biochemistry 48, 2960-2968
    • (2009) Biochemistry , vol.48 , pp. 2960-2968
    • Fischer, C.J.1    Yamada, K.2    Fitzgerald, D.J.3
  • 44
    • 48249113056 scopus 로고    scopus 로고
    • Translocation and unwinding mechanisms of RNA and DNA helicases
    • Pyle, A. M. (2008) Translocation and unwinding mechanisms of RNA and DNA helicases Annu. Rev. Biophys. 37, 317-336
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 317-336
    • Pyle, A.M.1
  • 45
    • 35648966525 scopus 로고    scopus 로고
    • Single molecule imaging of Tid1/Rdh54, a Rad54 homolog that translocates on duplex DNA and can disrupt joint molecules
    • Nimonkar, A. V., Amitani, I., Baskin, R. J., and Kowalczykowski, S. C. (2007) Single molecule imaging of Tid1/Rdh54, a Rad54 homolog that translocates on duplex DNA and can disrupt joint molecules J. Biol. Chem. 282, 30776-30784
    • (2007) J. Biol. Chem. , vol.282 , pp. 30776-30784
    • Nimonkar, A.V.1    Amitani, I.2    Baskin, R.J.3    Kowalczykowski, S.C.4
  • 46
    • 33745498749 scopus 로고    scopus 로고
    • Visualization of Rad54, a chromatin remodeling protein, translocating on single DNA molecules
    • Amitani, I., Baskin, R. J., and Kowalczykowski, S. C. (2006) Visualization of Rad54, a chromatin remodeling protein, translocating on single DNA molecules Mol. Cell 23, 143-148
    • (2006) Mol. Cell , vol.23 , pp. 143-148
    • Amitani, I.1    Baskin, R.J.2    Kowalczykowski, S.C.3
  • 47
    • 35648958216 scopus 로고    scopus 로고
    • Kinetic model for the ATP-dependent translocation of Saccharomyces cerevisiae RSC along double-stranded DNA
    • Fischer, C. J., Saha, A., and Cairns, B. R. (2007) Kinetic model for the ATP-dependent translocation of Saccharomyces cerevisiae RSC along double-stranded DNA Biochemistry 46, 12416-12426
    • (2007) Biochemistry , vol.46 , pp. 12416-12426
    • Fischer, C.J.1    Saha, A.2    Cairns, B.R.3
  • 48
    • 84859407146 scopus 로고    scopus 로고
    • Tracking the RecQ helicase on DNA: An insight into the mechanism of molecular motors
    • University of California, Davis
    • Rad, B. (2010) Tracking the RecQ helicase on DNA: An insight into the mechanism of molecular motors, in Graduate Group in Biophysics, p 194, University of California, Davis.
    • (2010) Graduate Group in Biophysics , pp. 194
    • Rad, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.