메뉴 건너뛰기




Volumn 24, Issue 1, 2005, Pages 180-189

UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli

Author keywords

Helicase; RecA; RecF; Rep; UvrD

Indexed keywords

BACTERIAL ENZYME; HELICASE; MUTANT PROTEIN; NUCLEOPROTEIN; RECA PROTEIN; REP HELICASE; SRS2 HELICASE; UNCLASSIFIED DRUG; UVRD HELICASE;

EID: 13244252309     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.emboj.7600485     Document Type: Article
Times cited : (224)

References (66)
  • 1
    • 0026751086 scopus 로고
    • Semidominant suppressors of Srs2 helicase mutations of Saccharomyces cerevisiae map in the RAD51 gene, whose sequence predicts a protein with similarities to procaryotic RecA proteins
    • Aboussekhra A, Chanet R, Adjiri A, Fabre F (1992) Semidominant suppressors of Srs2 helicase mutations of Saccharomyces cerevisiae map in the RAD51 gene, whose sequence predicts a protein with similarities to procaryotic RecA proteins. Mol Cell Biol 12: 3224-3234
    • (1992) Mol Cell Biol , vol.12 , pp. 3224-3234
    • Aboussekhra, A.1    Chanet, R.2    Adjiri, A.3    Fabre, F.4
  • 2
    • 0024445751 scopus 로고
    • RADH, a gene of Saccharomyces cerevisiae encoding a putative DNA helicase involved in DNA repair. Characteristics of radH mutants and sequence of the gene
    • Aboussekhra A, Chanet R, Zgaga Z, Cassier-Chauvat C, Heude M, Fabre F (1989) RADH, a gene of Saccharomyces cerevisiae encoding a putative DNA helicase involved in DNA repair. Characteristics of radH mutants and sequence of the gene. Nucleic Acids Res 17: 7211-7219
    • (1989) Nucleic Acids Res , vol.17 , pp. 7211-7219
    • Aboussekhra, A.1    Chanet, R.2    Zgaga, Z.3    Cassier-Chauvat, C.4    Heude, M.5    Fabre, F.6
  • 3
    • 0024058351 scopus 로고
    • Genetic control of intrachromosomal recombination in Saccharomyces cerevisiae. I. Isolation and genetic characterization of hyper-recombination mutations
    • Aguilera A, Klein HL (1988) Genetic control of intrachromosomal recombination in Saccharomyces cerevisiae. I. Isolation and genetic characterization of hyper-recombination mutations. Genetics 119: 779-790
    • (1988) Genetics , vol.119 , pp. 779-790
    • Aguilera, A.1    Klein, H.L.2
  • 4
    • 1642368750 scopus 로고    scopus 로고
    • Bacillus anthracis and Bacillus cereus PcrA helicases can support DNA unwinding and in vitro rolling-circle replication of plasmid pT181 of Staphylococcus aureus
    • Anand SP, Mitra P, Naqvi A, Khan SA (2004) Bacillus anthracis and Bacillus cereus PcrA helicases can support DNA unwinding and in vitro rolling-circle replication of plasmid pT181 of Staphylococcus aureus. J Bacteriol 186: 2195-2199
    • (2004) J Bacteriol , vol.186 , pp. 2195-2199
    • Anand, S.P.1    Mitra, P.2    Naqvi, A.3    Khan, S.A.4
  • 5
    • 0019122884 scopus 로고
    • Hyper-recombination in uvrD mutants of Escherichia coli K-12
    • Arthur HM, Lloyd RG (1980) Hyper-recombination in uvrD mutants of Escherichia coli K-12. Mol Gen Genet 180: 185-191
    • (1980) Mol Gen Genet , vol.180 , pp. 185-191
    • Arthur, H.M.1    Lloyd, R.G.2
  • 6
    • 0038136948 scopus 로고    scopus 로고
    • Contribution of DNA conformation and topology in right-handed DNA wrapping by the Bacillus subtilis LrpC protein
    • Beloin C, Jeusset J, Revet B, Mirambeau G, Le Hegarat F, Le Cam E (2003) Contribution of DNA conformation and topology in right-handed DNA wrapping by the Bacillus subtilis LrpC protein. J Biol Chem 278: 5333-5342
    • (2003) J Biol Chem , vol.278 , pp. 5333-5342
    • Beloin, C.1    Jeusset, J.2    Revet, B.3    Mirambeau, G.4    Le Hegarat, F.5    Le Cam, E.6
  • 7
    • 0030660145 scopus 로고    scopus 로고
    • uvrD mutations enhance tandem repeat deletion in the Escherichia coli chromosome via SOS induction of the RecF recombination pathway
    • Bierne H, Seigneur M, Ehrlich SD, Michel B (1997a) uvrD mutations enhance tandem repeat deletion in the Escherichia coli chromosome via SOS induction of the RecF recombination pathway. Mol Microbiol 26: 557-567
    • (1997) Mol Microbiol , vol.26 , pp. 557-567
    • Bierne, H.1    Seigneur, M.2    Ehrlich, S.D.3    Michel, B.4
  • 8
    • 0030844430 scopus 로고    scopus 로고
    • Isolation of a dnaE mutation which enhances RecA-independent homologous recombination in the Escherichia coli chromosome
    • Bierne H, Vilette D, Ehrlich SD, Michel B (1997b) Isolation of a dnaE mutation which enhances RecA-independent homologous recombination in the Escherichia coli chromosome. Mol Microbiol 24: 1225-1234
    • (1997) Mol Microbiol , vol.24 , pp. 1225-1234
    • Bierne, H.1    Vilette, D.2    Ehrlich, S.D.3    Michel, B.4
  • 9
    • 0016392709 scopus 로고
    • Detection of transcribable recombination products following conjugation in rec +, reCB- and recC-strains of Escherichia coli K12
    • Birge EA, Low KB (1974) Detection of transcribable recombination products following conjugation in rec +, reCB- and recC-strains of Escherichia coli K12. J Mol Biol 83: 447-457
    • (1974) J Mol Biol , vol.83 , pp. 447-457
    • Birge, E.A.1    Low, K.B.2
  • 10
    • 0038575033 scopus 로고    scopus 로고
    • RdgB acts to avoid chromosome fragmentation in Escherichia coli
    • Bradshaw JS, Kuzminov A (2003) RdgB acts to avoid chromosome fragmentation in Escherichia coli. Mol Microbiol 48: 1711-1725
    • (2003) Mol Microbiol , vol.48 , pp. 1711-1725
    • Bradshaw, J.S.1    Kuzminov, A.2
  • 11
    • 0035081951 scopus 로고    scopus 로고
    • Viability of rep recA mutants depends on their capacity to cope with spontaneous oxidative damage and on the DnaK chaperone protein
    • Bredeche MF, Ehrlich SD, Michel B (2001) Viability of rep recA mutants depends on their capacity to cope with spontaneous oxidative damage and on the DnaK chaperone protein. J Bacteriol 183: 2165-2171
    • (2001) J Bacteriol , vol.183 , pp. 2165-2171
    • Bredeche, M.F.1    Ehrlich, S.D.2    Michel, B.3
  • 12
    • 0033958431 scopus 로고    scopus 로고
    • UvrD-dependent replication of rolling-circle plasmids in Escherichia coli
    • Bruand C, Ehrlich SD (2000) UvrD-dependent replication of rolling-circle plasmids in Escherichia coli. Mol Microbiol 35: 204-210
    • (2000) Mol Microbiol , vol.35 , pp. 204-210
    • Bruand, C.1    Ehrlich, S.D.2
  • 13
    • 0942287233 scopus 로고    scopus 로고
    • RecO acts with RecF and RecR to protect and maintain replication forks blocked by UV-induced DNA damage in Escherichia coli
    • Chow KH, Courcelle J (2004) RecO acts with RecF and RecR to protect and maintain replication forks blocked by UV-induced DNA damage in Escherichia coli. J Biol Chem 279: 3492-3496
    • (2004) J Biol Chem , vol.279 , pp. 3492-3496
    • Chow, K.H.1    Courcelle, J.2
  • 14
    • 0023405041 scopus 로고
    • The Escherichia coli rep mutation. X. Consequences of increased and decreased Rep protein levels
    • Colasanti J, Denhardt DT (1987) The Escherichia coli rep mutation. X. Consequences of increased and decreased Rep protein levels. Mol Gen Genet 209: 382-390
    • (1987) Mol Gen Genet , vol.209 , pp. 382-390
    • Colasanti, J.1    Denhardt, D.T.2
  • 15
    • 0030890705 scopus 로고    scopus 로고
    • recF and recR are required for the resumption of replication at DNA replication forks in Escherichia coli
    • Courcelle J, Carswell-Crumpton C, Hanawalt PC (1997) recF and recR are required for the resumption of replication at DNA replication forks in Escherichia coli. Proc Natl Acad Sci USA 94: 3714-3719
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 3714-3719
    • Courcelle, J.1    Carswell-Crumpton, C.2    Hanawalt, P.C.3
  • 16
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci USA 97: 6640-6645
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 17
    • 0036880196 scopus 로고    scopus 로고
    • Helicase mechanisms and the coupling of helicases within macromolar machines. Part I: Structures and properties of isolated helicases
    • Delagoutte E, von Hippel PH (2002a) Helicase mechanisms and the coupling of helicases within macromolar machines. Part I: structures and properties of isolated helicases. Q Rev Biophys 35: 431-478
    • (2002) Q Rev Biophys , vol.35 , pp. 431-478
    • Delagoutte, E.1    Von Hippel, P.H.2
  • 18
    • 0037294467 scopus 로고    scopus 로고
    • Helicase mechanisms and the coupling of helicases within macromolar machines. Part II: Integration of helicases into cellular processes
    • Delagoutte E, von Hippel PH (2002b) Helicase mechanisms and the coupling of helicases within macromolar machines. Part II: integration of helicases into cellular processes. Q Rev Biophys 36: 1-69
    • (2002) Q Rev Biophys , vol.36 , pp. 1-69
    • Delagoutte, E.1    Von Hippel, P.H.2
  • 20
    • 0037168658 scopus 로고    scopus 로고
    • Alternate pathways involving Sgs1/Top3, Mus81/Mms4, and Srs2 prevent formation of toxic recombination intermediates from single-stranded gaps created by DNA replication
    • Fabre F, Chan A, Heyer WD, Gangloff S (2002) Alternate pathways involving Sgs1/Top3, Mus81/Mms4, and Srs2 prevent formation of toxic recombination intermediates from single-stranded gaps created by DNA replication. Proc Natl Acad Sci USA 99: 16887-16892
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16887-16892
    • Fabre, F.1    Chan, A.2    Heyer, W.D.3    Gangloff, S.4
  • 22
    • 8844265345 scopus 로고    scopus 로고
    • The DNA repair helicase UvrD is essential for replication fork reversal in replication mutants
    • Flores MJ, Bidnenko V, Michel B (2004) The DNA repair helicase UvrD is essential for replication fork reversal in replication mutants. EMBO Rep 5: 983-988
    • (2004) EMBO Rep , vol.5 , pp. 983-988
    • Flores, M.J.1    Bidnenko, V.2    Michel, B.3
  • 23
    • 0035254234 scopus 로고    scopus 로고
    • Impairment of lagging strand synthesis triggers the formation of a RuvABC substrate at replication forks
    • Flores MJ, Bierne H, Ehrlich SD, Michel B (2001) Impairment of lagging strand synthesis triggers the formation of a RuvABC substrate at replication forks. EMBO J 20: 619-629
    • (2001) EMBO J , vol.20 , pp. 619-629
    • Flores, M.J.1    Bierne, H.2    Ehrlich, S.D.3    Michel, B.4
  • 24
    • 0034119866 scopus 로고    scopus 로고
    • Homologous recombination is responsible for cell death in the absence of the Sgs1 and Srs2 helicases
    • Gangloff S, Soustelle C, Fabre F (2000) Homologous recombination is responsible for cell death in the absence of the Sgs1 and Srs2 helicases. Nat Genet 25: 192-194
    • (2000) Nat Genet , vol.25 , pp. 192-194
    • Gangloff, S.1    Soustelle, C.2    Fabre, F.3
  • 25
    • 0028047403 scopus 로고
    • A dominant negative allele of the Escherichia coli uvrD gene encoding DNA helicase II. A biochemical and genetic characterization
    • George JW, Brosh Jr RM, Matson SW (1994) A dominant negative allele of the Escherichia coli uvrD gene encoding DNA helicase II. A biochemical and genetic characterization. J Mol Biol 235: 424-435
    • (1994) J Mol Biol , vol.235 , pp. 424-435
    • George, J.W.1    Brosh Jr., R.M.2    Matson, S.W.3
  • 26
    • 0025953630 scopus 로고
    • ColE1-type vectors with fully repressible replication
    • Gil D, Bouche JP (1991) ColE1-type vectors with fully repressible replication. Gene 105: 17-22
    • (1991) Gene , vol.105 , pp. 17-22
    • Gil, D.1    Bouche, J.P.2
  • 27
    • 0026686379 scopus 로고
    • Differential inhibition of the DNA translocation and DNA unwinding activities of DNA helicases by the Escherichia coli Tus protein
    • Hiasa H, Marians KJ (1992) Differential inhibition of the DNA translocation and DNA unwinding activities of DNA helicases by the Escherichia coli Tus protein. J Biol Chem 267: 11379-11385
    • (1992) J Biol Chem , vol.267 , pp. 11379-11385
    • Hiasa, H.1    Marians, K.J.2
  • 28
    • 0017298802 scopus 로고
    • A model for replication repair in mammalian cells
    • Higgins NP, Kato K, Strauss B (1976) A model for replication repair in mammalian cells. J Mol Biol 101: 417-425
    • (1976) J Mol Biol , vol.101 , pp. 417-425
    • Higgins, N.P.1    Kato, K.2    Strauss, B.3
  • 30
    • 0027507727 scopus 로고
    • Characterization of the Staphylococcus aureus chromosomal gene pcrA, identified by mutations affecting plasmid pT181 replication
    • Iordanescu S (1993) Characterization of the Staphylococcus aureus chromosomal gene pcrA, identified by mutations affecting plasmid pT181 replication. Mol Gen Genet 241: 185-192
    • (1993) Mol Gen Genet , vol.241 , pp. 185-192
    • Iordanescu, S.1
  • 31
    • 0035808566 scopus 로고    scopus 로고
    • Active disruption of an RNA-protein interaction by a DExH/D RNA helicase
    • Jankowsky E, Gross CH, Shuman S, Pyle AM (2001) Active disruption of an RNA-protein interaction by a DExH/D RNA helicase. Science 291: 121-125
    • (2001) Science , vol.291 , pp. 121-125
    • Jankowsky, E.1    Gross, C.H.2    Shuman, S.3    Pyle, A.M.4
  • 32
    • 0035108094 scopus 로고    scopus 로고
    • Mutations in recombinational repair and in checkpoint control genes suppress the lethal combination of srs2A with other DNA repair genes in Saccharomyces cerevisiae
    • Klein HL (2001) Mutations in recombinational repair and in checkpoint control genes suppress the lethal combination of srs2A with other DNA repair genes in Saccharomyces cerevisiae. Genetics 157: 557-565
    • (2001) Genetics , vol.157 , pp. 557-565
    • Klein, H.L.1
  • 35
    • 0032715175 scopus 로고    scopus 로고
    • Recombinational repair of DNA damage in Escherichia coli and bacteriophage lambda
    • Kuzminov A (1999) Recombinational repair of DNA damage in Escherichia coli and bacteriophage lambda. Microbiol Mol Biol Rev 63: 751-813
    • (1999) Microbiol Mol Biol Rev , vol.63 , pp. 751-813
    • Kuzminov, A.1
  • 36
    • 0016710698 scopus 로고
    • The rep mutation. IV. Slower movement of replication forks in Escherichia coli rep strains
    • Lane HE, Denhardt DT (1975) The rep mutation. IV. Slower movement of replication forks in Escherichia coli rep strains. J Mol Biol 97: 99-112
    • (1975) J Mol Biol , vol.97 , pp. 99-112
    • Lane, H.E.1    Denhardt, D.T.2
  • 37
    • 0026781991 scopus 로고
    • Biochemical basis of the constitutive repressor cleavage activity of recA730 protein. A comparison to recA441 and recA803 proteins
    • Lavery PE, Kowalczykowski SC (1992) Biochemical basis of the constitutive repressor cleavage activity of recA730 protein. A comparison to recA441 and recA803 proteins. J Biol Chem 267: 20648-20658
    • (1992) J Biol Chem , vol.267 , pp. 20648-20658
    • Lavery, P.E.1    Kowalczykowski, S.C.2
  • 38
    • 18844473550 scopus 로고
    • Genetic analysis of conjugational recombination in Escherichia coli K12 strains deficient in RecBCD enzyme
    • Lloyd RG, Buckman C, Benson FE (1987a) Genetic analysis of conjugational recombination in Escherichia coli K12 strains deficient in RecBCD enzyme. J Gen Microbiol 133: 2531-2538
    • (1987) J Gen Microbiol , vol.133 , pp. 2531-2538
    • Lloyd, R.G.1    Buckman, C.2    Benson, F.E.3
  • 39
    • 0023219669 scopus 로고
    • Formation of recombinant lacZ+ DNA in conjugational crosses with a recB mutant of Escherichia coli K12 depends on recF, recJ, and recO
    • Lloyd RG, Evans NP, Buckman C (1987b) Formation of recombinant lacZ+ DNA in conjugational crosses with a recB mutant of Escherichia coli K12 depends on recF, recJ, and recO. Mol Gen Genet 209: 135-141
    • (1987) Mol Gen Genet , vol.209 , pp. 135-141
    • Lloyd, R.G.1    Evans, N.P.2    Buckman, C.3
  • 40
    • 1842318884 scopus 로고
    • DNA repair in Escherichia coli: Identification of the uvrD gene product
    • Maples VF, Kushner SR (1982) DNA repair in Escherichia coli: identification of the uvrD gene product. Proc Natl Acad Sci USA 79: 5616-5620
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 5616-5620
    • Maples, V.F.1    Kushner, S.R.2
  • 41
    • 0003785155 scopus 로고
    • Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Miller J (1972) Experiments in Molecular Genetics. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • (1972) Experiments in Molecular Genetics
    • Miller, J.1
  • 42
    • 0028564949 scopus 로고
    • Mismatch repair, genetic stability, and cancer
    • Modrich P (1994) Mismatch repair, genetic stability, and cancer. Science 266: 1959-1960
    • (1994) Science , vol.266 , pp. 1959-1960
    • Modrich, P.1
  • 43
    • 0027203925 scopus 로고
    • Antipairing and strand transferase activities of E. coli helicase II (UvrD)
    • Morel P, Hejna JA, Ehrlich SD, Cassuto E (1993) Antipairing and strand transferase activities of E. coli helicase II (UvrD). Nucleic Acids Res 21: 3205-3209
    • (1993) Nucleic Acids Res , vol.21 , pp. 3205-3209
    • Morel, P.1    Hejna, J.A.2    Ehrlich, S.D.3    Cassuto, E.4
  • 44
    • 0038392868 scopus 로고    scopus 로고
    • RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange: A universal step of recombinational repair
    • Morimatsu K, Kowalczykowski SC (2003) RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange: a universal step of recombinational repair. Mol Cell 11: 1337-1347
    • (2003) Mol Cell , vol.11 , pp. 1337-1347
    • Morimatsu, K.1    Kowalczykowski, S.C.2
  • 45
    • 0026595890 scopus 로고
    • Post-incision steps of nucleotide excision repair in Escherichia coli. Disassembly of the UvrBC-DNA complex by helicase II and DNA polymerase 1
    • Orren DK, Selby CP, Hearst JE, Sancar A (1992) Post-incision steps of nucleotide excision repair in Escherichia coli. Disassembly of the UvrBC-DNA complex by helicase II and DNA polymerase 1. J Biol Chem 267: 780-788
    • (1992) J Biol Chem , vol.267 , pp. 780-788
    • Orren, D.K.1    Selby, C.P.2    Hearst, J.E.3    Sancar, A.4
  • 46
    • 0031854048 scopus 로고    scopus 로고
    • PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication
    • Petit MA, Dervyn E, Rose M, Entian KD, McGovern S, Ehrlich SD, Bruand C (1998) PcrA is an essential DNA helicase of Bacillus subtilis fulfilling functions both in repair and rolling-circle replication. Mol Microbiol 29: 261-273
    • (1998) Mol Microbiol , vol.29 , pp. 261-273
    • Petit, M.A.1    Dervyn, E.2    Rose, M.3    Entian, K.D.4    McGovern, S.5    Ehrlich, S.D.6    Bruand, C.7
  • 47
    • 0037124327 scopus 로고    scopus 로고
    • Essential bacterial helicases that counteract the toxicity of recombination proteins
    • Petit MA, Ehrlich D (2002) Essential bacterial helicases that counteract the toxicity of recombination proteins. EMBO J 21: 3137-3147
    • (2002) EMBO J , vol.21 , pp. 3137-3147
    • Petit, M.A.1    Ehrlich, D.2
  • 48
    • 0035687216 scopus 로고    scopus 로고
    • Genetic evidence that the elevated levels of Escherichia coli helicase II antagonize recombinational DNA repair
    • Petranovic M, Zahradka K, Zahradka D, Petranovic D, Nagy B, Salaj-Smic E (2001) Genetic evidence that the elevated levels of Escherichia coli helicase II antagonize recombinational DNA repair. Biochimie 83: 1041-1047
    • (2001) Biochimie , vol.83 , pp. 1041-1047
    • Petranovic, M.1    Zahradka, K.2    Zahradka, D.3    Petranovic, D.4    Nagy, B.5    Salaj-Smic, E.6
  • 49
    • 0001728083 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorylation. I. Purification and properties of soluble dinitrophenol-stimulated adenosine triphosphatase
    • Pullman ME, Penefsky HS, Datta A, Racker E (1960) Partial resolution of the enzymes catalyzing oxidative phosphorylation. I. Purification and properties of soluble dinitrophenol-stimulated adenosine triphosphatase. J Biol Chem 235: 3322-3329
    • (1960) J Biol Chem , vol.235 , pp. 3322-3329
    • Pullman, M.E.1    Penefsky, H.S.2    Datta, A.3    Racker, E.4
  • 50
    • 0034123356 scopus 로고    scopus 로고
    • Multiple genetic pathways for restarting DNA replication forks in Escherichia coli K-12
    • Sandler SJ (2000) Multiple genetic pathways for restarting DNA replication forks in Escherichia coli K-12. Genetics 155: 487-497
    • (2000) Genetics , vol.155 , pp. 487-497
    • Sandler, S.J.1
  • 51
    • 0017814971 scopus 로고
    • Purification of the rep protein of Escherichia coli. An ATPase which separates duplex DNA strands in advance of replication
    • Scott JF, Kornberg A (1978) Purification of the rep protein of Escherichia coli. An ATPase which separates duplex DNA strands in advance of replication. J Biol Chem 253: 3292-3297
    • (1978) J Biol Chem , vol.253 , pp. 3292-3297
    • Scott, J.F.1    Kornberg, A.2
  • 53
    • 0027265542 scopus 로고
    • Degradation of individual chromosomes in recA mutants of Escherichia coli
    • Skarstad K, Boye E (1993) Degradation of individual chromosomes in recA mutants of Escherichia coli. J Bacteriol 175: 5505-5509
    • (1993) J Bacteriol , vol.175 , pp. 5505-5509
    • Skarstad, K.1    Boye, E.2
  • 54
    • 0035150184 scopus 로고    scopus 로고
    • Unwinding the 'Gordian knot' of helicase action
    • Soultanas P, Wigley DB (2001) Unwinding the 'Gordian knot' of helicase action. Trends Biochem Sci 26: 47-54
    • (2001) Trends Biochem Sci , vol.26 , pp. 47-54
    • Soultanas, P.1    Wigley, D.B.2
  • 55
    • 0018291009 scopus 로고
    • The rep mutation. VI. Purification and properties of the Escherichia coli rep protein, DNA helicase III
    • Takahashi S, Hours C, Chu A, Denhardt DT (1979) The rep mutation. VI. Purification and properties of the Escherichia coli rep protein, DNA helicase III. Can J Biochem 57: 855-866
    • (1979) Can J Biochem , vol.57 , pp. 855-866
    • Takahashi, S.1    Hours, C.2    Chu, A.3    Denhardt, D.T.4
  • 57
    • 0021105603 scopus 로고
    • Identification of the gene for DNA helicase II of Escherichia coli
    • Taucher-Scholz G, Hoffmann-Berling H (1983) Identification of the gene for DNA helicase II of Escherichia coli. Eur J Biochem 137: 573-580
    • (1983) Eur J Biochem , vol.137 , pp. 573-580
    • Taucher-Scholz, G.1    Hoffmann-Berling, H.2
  • 58
    • 0027238208 scopus 로고
    • Biochemical interaction of the Escherichia coli RecF, RecO, and RecR proteins with RecA protein and single-stranded DNA binding protein
    • Umezu K, Chi NW, Kolodner RD (1993) Biochemical interaction of the Escherichia coli RecF, RecO, and RecR proteins with RecA protein and single-stranded DNA binding protein. Proc Natl Acad Sci USA 90: 3875-3879
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 3875-3879
    • Umezu, K.1    Chi, N.W.2    Kolodner, R.D.3
  • 59
    • 0037673943 scopus 로고    scopus 로고
    • The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments
    • Veaute X, Jeusset J, Soustelle C, Kowalczykowski SC, Le Cam E, 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
  • 60
    • 0027269936 scopus 로고
    • Cosuppression of recF, recR and recO mutations by mutant recA alleles in Escherichia coli cells
    • Wang TC, Chang HY, Hung JL (1993) Cosuppression of recF, recR and recO mutations by mutant recA alleles in Escherichia coli cells. Mutat Res 294: 157-166
    • (1993) Mutat Res , vol.294 , pp. 157-166
    • Wang, T.C.1    Chang, H.Y.2    Hung, J.L.3
  • 61
    • 0030700498 scopus 로고    scopus 로고
    • Recombinational DNA repair: The RecF and RecR proteins limit the extension of RecA filaments beyond single-strand DNA gaps
    • Webb BL, Cox MM, Inman RB (1997) Recombinational DNA repair: the RecF and RecR proteins limit the extension of RecA filaments beyond single-strand DNA gaps. Cell 91: 347-356
    • (1997) Cell , vol.91 , pp. 347-356
    • Webb, B.L.1    Cox, M.M.2    Inman, R.B.3
  • 62
    • 0022917641 scopus 로고
    • Host/vector interactions which affect the viability of recombinant phage lambda clones
    • Wertman KF, Wyman AR, Botstein D (1986) Host/vector interactions which affect the viability of recombinant phage lambda clones. Gene 49: 253-262
    • (1986) Gene , vol.49 , pp. 253-262
    • Wertman, K.F.1    Wyman, A.R.2    Botstein, D.3
  • 63
    • 0021319941 scopus 로고
    • Processing of plasmid DNA during bacterial conjugation
    • Willetts N, Wilkins B (1984) Processing of plasmid DNA during bacterial conjugation. Microbiol Rev 48: 24-41
    • (1984) Microbiol Rev , vol.48 , pp. 24-41
    • Willetts, N.1    Wilkins, B.2
  • 64
    • 1842315125 scopus 로고
    • Non-inducible mutants of the regulator gene in the 'lactose' system of Escherichia coli
    • Willson C, Perrin D, Cohn M, Jacob F, Monod J (1964) Non-inducible mutants of the regulator gene in the 'lactose' system of Escherichia coli. J Mol Biol 141: 582-592
    • (1964) J Mol Biol , vol.141 , pp. 582-592
    • Willson, C.1    Perrin, D.2    Cohn, M.3    Jacob, F.4    Monod, J.5
  • 65
    • 0027078134 scopus 로고
    • Bound Lac repressor protein differentially inhibits the unwinding reactions catalyzed by DNA helicases
    • Yancey-Wrona JE, Matson SW (1992) Bound Lac repressor protein differentially inhibits the unwinding reactions catalyzed by DNA helicases. Nucleic Acids Res 20: 6713-6721
    • (1992) Nucleic Acids Res , vol.20 , pp. 6713-6721
    • Yancey-Wrona, J.E.1    Matson, S.W.2
  • 66
    • 0017905113 scopus 로고
    • Recombinant levels of Escherichia coli K-12 mutants deficient in various replication, recombination, or repair genes
    • Zieg J, Maples VF, Kushner SR (1978) Recombinant levels of Escherichia coli K-12 mutants deficient in various replication, recombination, or repair genes. J Bacteriol 134: 958-966
    • (1978) J Bacteriol , vol.134 , pp. 958-966
    • Zieg, J.1    Maples, V.F.2    Kushner, S.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.