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Volumn 287, Issue 42, 2012, Pages 35621-35630

RecFOR proteins target RecA protein to a DNA gap with either DNA or RNA at the 5′ terminus: Implication for repair of stalled replication forks

Author keywords

[No Author keywords available]

Indexed keywords

BINDING CONSTANT; DUPLEX DNA; FASTER RATES; HOMOLOGOUS RECOMBINATION; LAGGING STRAND; NUCLEOPROTEIN FILAMENTS; RECA FILAMENT; RECA PROTEINS; SINGLE-STRANDED DNA; SINGLE-STRANDED DNA-BINDING PROTEINS; STALLED REPLICATION;

EID: 84867406977     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.397034     Document Type: Article
Times cited : (57)

References (45)
  • 1
    • 0034176335 scopus 로고    scopus 로고
    • Initiation of genetic recombination and recombination-dependent replication
    • Kowalczykowski, S. C. (2000) Initiation of genetic recombination and recombination-dependent replication. Trends Biochem. Sci. 25, 156-165
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 156-165
    • Kowalczykowski, S.C.1
  • 2
    • 68249125048 scopus 로고    scopus 로고
    • Choreography of recombination proteins during the DNA damage response
    • Lisby, M., and Rothstein, R. (2009) Choreography of recombination proteins during the DNA damage response. DNA Repair 8, 1068-1076
    • (2009) DNA Repair , vol.8 , pp. 1068-1076
    • Lisby, M.1    Rothstein, R.2
  • 3
    • 34249938016 scopus 로고    scopus 로고
    • Recombination proteins and rescue of arrested replication forks
    • DOI 10.1016/j.dnarep.2007.02.016, PII S1568786407000675, Replication Fork Repair Processes
    • Michel, B., Boubakri, H., Baharoglu, Z., LeMasson, M., and Lestini, R. (2007) Recombination proteins and rescue of arrested replication forks. DNA Repair 6, 967-980 (Pubitemid 46880477)
    • (2007) DNA Repair , vol.6 , Issue.7 , pp. 967-980
    • Michel, B.1    Boubakri, H.2    Baharoglu, Z.3    LeMasson, M.4    Lestini, R.5
  • 4
    • 0032715175 scopus 로고    scopus 로고
    • Recombinational repair of DNA damage in Escherichia coli and bacteriophage λ
    • Kuzminov, A. (1999) Recombinational repair of DNA damage in Escherichia coli and bacteriophage λ. Microbiol. Mol. Biol. Rev. 63, 751-813
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 751-813
    • Kuzminov, A.1
  • 8
    • 0001865832 scopus 로고    scopus 로고
    • DNA strand exchange proteins: A biochemical and physical comparison
    • Bianco, P. R., Tracy, R. B., and Kowalczykowski, S. C. (1998) DNA strand exchange proteins: a biochemical and physical comparison. Front. Biosci. 3, D570-D603
    • (1998) Front. Biosci. , vol.3
    • Bianco, P.R.1    Tracy, R.B.2    Kowalczykowski, S.C.3
  • 9
    • 0035997347 scopus 로고    scopus 로고
    • The bacterial RecA protein and the recombinational DNA repair of stalled replication forks
    • DOI 10.1146/annurev.biochem.71.083101.133940
    • Lusetti, S. L., and Cox, M. M. (2002) The bacterial RecA protein and the recombinational DNA repair of stalled replication forks. Annu. Rev. Biochem. 71, 71-100 (Pubitemid 34800215)
    • (2002) Annual Review of Biochemistry , vol.71 , pp. 71-100
    • Lusetti, S.L.1    Cox, M.M.2
  • 10
    • 0023178465 scopus 로고
    • Regulatory role of recF in the SOS response of Escherichia coli: Impaired induction of SOS genes by UV irradiation and nalidixic acid in a recF mutant
    • Thoms, B., and Wackernagel, W. (1987) Regulatory role of recF in the SOS response of Escherichia coli: impaired induction of SOS genes by UV irradiation and nalidixic acid in a recF mutant. J. Bacteriol. 169, 1731-1736 (Pubitemid 17063507)
    • (1987) Journal of Bacteriology , vol.169 , Issue.4 , pp. 1731-1736
    • Thoms, B.1    Wackernagel, W.2
  • 11
    • 0023609641 scopus 로고
    • Effects of the Escherichia coli recF suppressor mutation, recAZ801, on recF-dependent DNA-repair associated phenomena
    • Volkert, M. R., and Hartke, M. A. (1987) Effects of the Escherichia coli recF suppressor mutation, recA801, on recF-dependent DNA-repair associated phenomena. Mutat. Res. 184, 181-186 (Pubitemid 18020250)
    • (1987) Mutation Research , vol.184 , Issue.3 , pp. 181-186
    • Volkert, M.R.1    Hartke, M.A.2
  • 12
    • 0028983464 scopus 로고
    • recO and recR mutations delay induction of the SOS response in Escherichia coli
    • Hegde, S., Sandler, S. J., Clark, A. J., and Madiraju, M. V. (1995) recO and recR mutations delay induction of the SOS response in Escherichia coli. Mol. Gen. Genet. 246, 254-258
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 254-258
    • Hegde, S.1    Sandler, S.J.2    Clark, A.J.3    Madiraju, M.V.4
  • 13
    • 0028797220 scopus 로고
    • Altered SOS induction associated with mutations in recF, recO, and recR
    • Whitby, M. C., and Lloyd, R. G. (1995) Altered SOS induction associated with mutations in recF, recO, and recR. Mol. Gen. Genet. 246, 174-179
    • (1995) Mol. Gen. Genet. , vol.246 , pp. 174-179
    • Whitby, M.C.1    Lloyd, R.G.2
  • 14
    • 0022973023 scopus 로고
    • recA (Srf) suppression of recF deficiency in the postreplication repair of UV-irradiated Escherichia coli K-12
    • Wang, T.-C., and Smith, K. C. (1986) recA (Srf) suppression of recF deficiency in the postreplication repair of UV-irradiated Escherichia coli K-12. J. Bacteriol. 168, 940-946 (Pubitemid 17172796)
    • (1986) Journal of Bacteriology , vol.168 , Issue.2 , pp. 940-946
    • Wang, T.-C.V.1    Smith, K.C.2
  • 15
    • 0027269936 scopus 로고
    • Cosuppression of recF, recR and recO mutations by mutant recA alleles in Escherichia coli cells
    • DOI 10.1016/0921-8777(93)90024-B
    • Wang, T.-C., Chang, H. Y., and Hung, J. L. (1993) Cosuppression of recF, recR, and recO mutations by mutant recA alleles in Escherichia coli cells. Mutat. Res. 294, 157-166 (Pubitemid 23188612)
    • (1993) Mutation Research - DNA Repair , vol.294 , Issue.2 , pp. 157-166
    • Wang, T.-C.V.1    Chang, H.-Y.2    Hung, J.-L.3
  • 16
    • 0023801207 scopus 로고
    • Properties of a mutant recA-encoded protein reveal a possible role for Escherichia coli recF-encoded protein in genetic recombination
    • Madiraju, M. V. V. S., Templin, A., and Clark, A. J. (1988) Properties of a mutant recA-encoded protein reveal a possible role for Escherichia coli recF-encoded protein in genetic recombination. Proc. Natl. Acad. Sci. U.S.A. 85, 6592-6596
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 6592-6596
    • Madiraju, M.V.V.S.1    Templin, A.2    Clark, A.J.3
  • 17
    • 0018686338 scopus 로고
    • Mutant single-strand binding protein of Escherichia coli: genetic and physiological characterization
    • Glassberg, J., Meyer, R. R., and Kornberg, A. (1979) Mutant single-strand binding protein of Escherichia coli: genetic and physiological characterization. J. Bacteriol. 140, 14-19 (Pubitemid 10248462)
    • (1979) Journal of Bacteriology , vol.140 , Issue.1 , pp. 14-19
    • Glassberg, J.1    Meyer, R.R.2    Kornberg, A.3
  • 19
    • 0023107920 scopus 로고
    • Genetic functions promoting homologous recombination in Escherichia coli: A study of inversions in phage λ
    • Ennis, D. G., Amundsen, S. K., and Smith, G. R. (1987) Genetic functions promoting homologous recombination in Escherichia coli: a study of inversions in phage λ. Genetics 115, 11-24 (Pubitemid 17001139)
    • (1987) Genetics , vol.115 , Issue.1 , pp. 11-24
    • Ennis, D.G.1    Amundsen, S.K.2    Smith, G.R.3
  • 20
    • 0023135142 scopus 로고
    • Effects of Escherichia coli SSB protein on the single-stranded DNA-dependent ATPase activity of Escherichia coli RecA protein. Evidence that SSB protein facilitates the binding of RecA protein to regions of secondary structure within single-stranded DNA
    • Kowalczykowski, S. C., and Krupp, R. A. (1987) Effects of Escherichia coli SSB protein on the single-stranded DNA-dependent ATPase activity of Escherichia coli RecA protein. Evidence that SSB protein facilitates the binding of RecA protein to regions of secondary structure within single-stranded DNA. J. Mol. Biol. 193, 97-113 (Pubitemid 17228121)
    • (1987) Journal of Molecular Biology , vol.193 , Issue.1 , pp. 97-113
    • Kowalczykowski, S.C.1    Krupp, R.A.2
  • 21
    • 0023108585 scopus 로고
    • Effects of the Escherichia coli SSB protein on the binding of Escherichia coli RecA protein to single-stranded DNA. Demonstration of competitive binding and the lack of a specific protein-protein interaction
    • Kowalczykowski, S. C., Clow, J., Somani, R., and Varghese, A. (1987) Effects of the Escherichia coli SSB protein on the binding of Escherichia coli RecA protein to single-stranded DNA. Demonstration of competitive binding and the lack of a specific protein-protein interaction. J. Mol. Biol. 193, 81-95 (Pubitemid 17228120)
    • (1987) Journal of Molecular Biology , vol.193 , Issue.1 , pp. 81-95
    • Kowalczykowski, S.C.1    Clow, J.2    Somani, R.3    Varghese, A.4
  • 22
    • 0025018843 scopus 로고
    • Kinetics of binding of single-stranded DNA binding protein from Escherichia coli to single-stranded nucleic acids
    • Urbanke, C., and Schaper, A. (1990) Kinetics of binding of single-stranded DNA binding protein from Escherichia coli to single-stranded nuclei acids. Biochemistry 29, 1744-1749 (Pubitemid 20074716)
    • (1990) Biochemistry , vol.29 , Issue.7 , pp. 1744-1749
    • Urbanke, C.1    Schaper, A.2
  • 23
    • 0021096846 scopus 로고
    • Investigation of binding between recA protein and single-stranded polynucleotides with the aid of a fluorescent deoxyribonucleic acid derivative
    • Silver, M. S., and Fersht, A. R. (1983) Investigation of binding between recA protein and single-stranded polynucleotides with the aid of a fluorescent deoxyribonucleic acid derivative. Biochemistry 22, 2860-2866
    • (1983) Biochemistry , vol.22 , pp. 2860-2866
    • Silver, M.S.1    Fersht, A.R.2
  • 24
    • 0024025051 scopus 로고
    • Overproduction of single-stranded-DNA-binding protein specifically inhibits recombination of UV-irradiated bacteriophage DNA in Escherichia coli
    • Moreau, P. L. (1988) Overproduction of single-stranded-DNA-binding protein specifically inhibits recombination of UV-irradiated bacteriophage DNA in Escherichia coli. J. Bacteriol. 170, 2493-2500
    • (1988) J. Bacteriol. , vol.170 , pp. 2493-2500
    • Moreau, P.L.1
  • 26
    • 0030026302 scopus 로고    scopus 로고
    • Preferential binding of Escherichia coli RecF protein to gapped DNA in the presence of adenosine (gamma-thio) triphosphate
    • Hegde, S. P., Rajagopalan, M., and Madiraju, M. V. V. S. (1996) Preferential binding of Escherichia coli RecF protein to gappedDNAin the presence of adenosine (γ-thio) triphosphate. J. Bacteriol. 178, 184-190 (Pubitemid 26006082)
    • (1996) Journal of Bacteriology , vol.178 , Issue.1 , pp. 184-190
    • Hegde, S.P.1    Rajagopalan, M.2    Madiraju, M.V.V.S.3
  • 27
    • 0030700498 scopus 로고    scopus 로고
    • Recombinational DNA repair: The RecF and RecR proteins limit the extension of RecA filaments beyond single-strand DNA gaps
    • DOI 10.1016/S0092-8674(00)80418-3
    • Webb, B. L., Cox, M. M., and Inman, R. B. (1997) Recombinational DNA repair: The RecF and RecR proteins limit the extension of RecA filaments beyond single strand DNA gaps. Cell 91, 347-356 (Pubitemid 27467965)
    • (1997) Cell , vol.91 , Issue.3 , pp. 347-356
    • Webb, B.L.1    Cox, M.M.2    Inman, R.B.3
  • 28
    • 0038392868 scopus 로고    scopus 로고
    • RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange: A universal step of recombinational repair
    • DOI 10.1016/S1097-2765(03)00188-6
    • Morimatsu, K., and Kowalczykowski, S. C. (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 (Pubitemid 36645151)
    • (2003) Molecular Cell , vol.11 , Issue.5 , pp. 1337-1347
    • Morimatsu, K.1    Kowalczykowski, S.C.2
  • 29
    • 0028921350 scopus 로고
    • Interaction of Tyr103 and Tyr264 of the RecA protein with DNA and nucleotide cofactors. Fluorescence study of engineered proteins
    • Morimatsu, K., Horii, T., and Takahashi, M. (1995) Interaction of Tyr103 and Tyr264 of the RecA protein with DNA and nucleotide cofactors. Fluorescence study of engineered proteins. Eur. J. Biochem. 228, 779-785
    • (1995) Eur. J. Biochem. , vol.228 , pp. 779-785
    • Morimatsu, K.1    Horii, T.2    Takahashi, M.3
  • 30
    • 0025902330 scopus 로고
    • Homologous pairing in vitro stimulated by the recombination hotspot, Chi
    • Dixon, D. A., and Kowalczykowski, S. C. (1991) Homologous pairing in vitro stimulated by the recombination hotspot, Chi. Cell 66, 361-371 (Pubitemid 121001373)
    • (1991) Cell , vol.66 , Issue.2 , pp. 361-371
    • Dixon, D.A.1    Kowalczykowski, S.C.2
  • 32
    • 0020645043 scopus 로고
    • New M13 Vectors for Cloning
    • Messing, J. (1983) New M13 Vectors for Cloning. Methods Enzymol. 101, 20-78
    • (1983) Methods Enzymol. , vol.101 , pp. 20-78
    • Messing, J.1
  • 33
    • 0018318912 scopus 로고
    • On the fidelity of DNA replication. Effect of divalent metal ion activators and deoxyribonucleoside triphosphate pools on in vitro mutagenesis
    • Kunkel, T. A., and Loeb, L. A. (1979) On the fidelity of DNA replication. Effect of divalent metal ion activators and deoxyribonucleoside triphosphate pools on in vitro mutagenesis. J. Biol. Chem. 254, 5718-5725 (Pubitemid 9245807)
    • (1979) Journal of Biological Chemistry , vol.254 , Issue.13 , pp. 5718-5725
    • Kunkel, T.A.1    Loeb, L.A.2
  • 34
    • 0032983974 scopus 로고    scopus 로고
    • ATP hydrolysis and DNA binding by the Escherichia coli RecF protein
    • Webb, B. L., Cox, M. M., and Inman, R. B. (1999) ATP hydrolysis and DNA binding by the Escherichia coli RecF protein. J. Biol. Chem. 274, 15367-15374
    • (1999) J. Biol. Chem. , vol.274 , pp. 15367-15374
    • Webb, B.L.1    Cox, M.M.2    Inman, R.B.3
  • 35
    • 57349157777 scopus 로고    scopus 로고
    • RecBCD enzyme and the repair of double-stranded DNA breaks
    • Dillingham, M. S., and Kowalczykowski, S. C. (2008) RecBCD enzyme and the repair of double-stranded DNA breaks. Microbiol. Mol. Biol. Rev. 72, 642-671
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , pp. 642-671
    • Dillingham, M.S.1    Kowalczykowski, S.C.2
  • 36
    • 33745852581 scopus 로고    scopus 로고
    • Identification of the RecR Toprim domain as the binding site for both recF and recO: A role of recR in recFOR assembly at double-stranded DNA-single-stranded DNA junctions
    • DOI 10.1074/jbc.M512658200
    • Honda, M., Inoue, J., Yoshimasu, M., Ito, Y., Shibata, T., and Mikawa, T. (2006) Identification of the RecR Toprim domain as the binding site for both RecF and RecO. A role of RecR in RecFOR assembly at double-stranded DNA single-stranded DNA junctions. J. Biol. Chem. 281, 18549-18559 (Pubitemid 44035514)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.27 , pp. 18549-18559
    • Honda, M.1    Inoue, J.2    Yoshimasu, M.3    Ito, Y.4    Shibata, T.5    Mikawa, T.6
  • 37
    • 59449105411 scopus 로고    scopus 로고
    • RecR-mediated modulation of RecF dimer specificity for single- and double-stranded DNA
    • Makharashvili, N., Mi, T., Koroleva, O., and Korolev, S. (2009) RecR-mediated modulation of RecF dimer specificity for single- and double-stranded DNA. J. Biol. Chem. 284, 1425-1434
    • (2009) J. Biol. Chem. , vol.284 , pp. 1425-1434
    • Makharashvili, N.1    Mi, T.2    Koroleva, O.3    Korolev, S.4
  • 38
    • 0028330518 scopus 로고
    • Purification and characterization of the Escherichia coli RecO protein: Renaturation of complementary single-stranded DNA molecules catalyzed by the RecO protein
    • Luisi-DeLuca, C., and Kolodner, R. (1994) Purification and characterization of the Escherichia coli RecO protein. Renaturation of complementary single-stranded DNA molecules catalyzed by the RecO protein. J. Mol. Biol. 236, 124-138 (Pubitemid 124001359)
    • (1994) Journal of Molecular Biology , vol.236 , Issue.1 , pp. 124-138
    • Luisi-DeLuca, C.1    Kolodner, R.2
  • 39
    • 0028034452 scopus 로고
    • Protein interactions in genetic recombination in Escherichia coli. Interactions involving RecO and RecR overcome the inhibition of RecA by single-stranded DNA-binding protein
    • Umezu, K., and Kolodner, R. D. (1994) Protein interactions in genetic recombination in Escherichia coli. Interactions involving RecO and RecR overcome the inhibition of RecA by single-stranded DNA-binding protein. J. Biol. Chem. 269, 30005-30013
    • (1994) J. Biol. Chem. , vol.269 , pp. 30005-30013
    • Umezu, K.1    Kolodner, R.D.2
  • 40
    • 0022360935 scopus 로고
    • The direction of RecA protein assembly onto single strand DNA is the same as the direction of strand assimilation during strand exchange
    • Register, J. C., 3rd, and Griffith, J. (1985) The direction of RecA protein assembly onto single strand DNA is the same as the direction of strand assimilation during strand exchange. J. Biol. Chem. 260, 12308-12312
    • (1985) J. Biol. Chem. , vol.260 , pp. 12308-12312
    • Register III, J.C.1    Griffith, J.2
  • 41
    • 31844456472 scopus 로고    scopus 로고
    • Replication fork reactivation downstream of a blocked nascent leading strand
    • DOI 10.1038/nature04329, PII NATURE04329
    • Heller, R. C., and Marians, K. J. (2006) Replication fork reactivation downstream of a blocked nascent leading strand. Nature 439, 557-562 (Pubitemid 43185374)
    • (2006) Nature , vol.439 , Issue.7076 , pp. 557-562
    • Heller, R.C.1    Marians, K.J.2
  • 42
    • 0021364455 scopus 로고
    • recF-dependent and recF recB-independent DNA gap-filling repair processes transfer dimer-containing parental strands to daughter strands in Escherichia coli K-12 uvrB
    • Wang, T. V., and Smith, K. C. (1984) recF-dependent and recF recB-independent DNA gap-filling repair processes transfer dimer-containing parental strands to daughter strands in Escherichia coli K-12 uvrB. J. Bacteriol. 158, 727-729
    • (1984) J. Bacteriol. , vol.158 , pp. 727-729
    • Wang, T.V.1    Smith, K.C.2
  • 43
    • 0015223483 scopus 로고
    • Exchanges between DNA strands in ultraviolet-irradiated Escherichia coli
    • Rupp, W. D., Wilde, C. E., 3rd, Reno, D. L., and Howard-Flanders, P. (1971) Exchanges between DNA strands in ultraviolet-irradiated Escherichia coli. J. Mol. Biol. 61, 25-44
    • (1971) J. Mol. Biol. , vol.61 , pp. 25-44
    • Rupp, W.D.1    Wilde III, C.E.2    Reno, D.L.3    Howard-Flanders, P.4
  • 44
    • 14144253224 scopus 로고    scopus 로고
    • The BRCA2 homologue Brh2 nucleates RAD51 filament formation at a dsDNA-ssDNA junction
    • DOI 10.1038/nature03234
    • Yang, H., Li, Q., Fan, J., Holloman, W. K., and Pavletich, N. P. (2005) The BRCA2 homologue Brh2 nucleates RAD51 filament formation at a dsDNA-ssDNA junction. Nature 433, 653-657 (Pubitemid 40283000)
    • (2005) Nature , vol.433 , Issue.7026 , pp. 653-657
    • Yang, H.1    Li, Q.2    Fan, J.3    Holloman, W.K.4    Pavletich, H.P.5
  • 45
    • 77957975815 scopus 로고    scopus 로고
    • Purified human BRCA2 stimulates RAD51-mediated recombination
    • Jensen, R. B., Carreira, A., and Kowalczykowski, S. C. (2010) Purified human BRCA2 stimulates RAD51-mediated recombination. Nature 467, 678-683
    • (2010) Nature , vol.467 , pp. 678-683
    • Jensen, R.B.1    Carreira, A.2    Kowalczykowski, S.C.3


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