메뉴 건너뛰기




Volumn 34, Issue 5, 2009, Pages 264-272

Nucleases and helicases take center stage in homologous recombination

Author keywords

[No Author keywords available]

Indexed keywords

BLOOM SYNDROME HELICASE; CHECKPOINT KINASE 2; DNA2 NUCLEASE; DOUBLE STRANDED DNA; HELICASE; MRE11 PROTEIN; NUCLEASE; PROTEIN MLH1; PROTEIN RAD9; RAD50 PROTEIN; RAD51 PROTEIN; RESOLVASE; SACCHAROMYCES CEREVISIAE PROTEIN; SCHIZOSACCHAROMYCES POMBE PROTEIN; SINGLE STRANDED DNA; SPO11 PROTEIN; UNCLASSIFIED DRUG; YEN1 ENZYME;

EID: 65549095526     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibs.2009.01.010     Document Type: Review
Times cited : (175)

References (76)
  • 1
    • 50649100744 scopus 로고    scopus 로고
    • Mechanism of eukaryotic homologous recombination
    • San Filippo J., et al. Mechanism of eukaryotic homologous recombination. Annu. Rev. Biochem. 77 (2008) 229-257
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 229-257
    • San Filippo, J.1
  • 2
  • 3
    • 38049173021 scopus 로고    scopus 로고
    • Homologous recombination in DNA repair and DNA damage tolerance
    • Li X., and Heyer W.D. Homologous recombination in DNA repair and DNA damage tolerance. Cell Res. 18 (2008) 99-113
    • (2008) Cell Res. , vol.18 , pp. 99-113
    • Li, X.1    Heyer, W.D.2
  • 4
    • 3242891189 scopus 로고    scopus 로고
    • The Mre11 complex and the metabolism of chromosome breaks: the importance of communicating and holding things together
    • Stracker T.H., et al. The Mre11 complex and the metabolism of chromosome breaks: the importance of communicating and holding things together. DNA Repair (Amst.) 3 (2004) 845-854
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 845-854
    • Stracker, T.H.1
  • 5
    • 0025334351 scopus 로고
    • Analysis of wild-type and rad50 mutants of yeast suggests an intimate relationship between meiotic chromosome synapsis and recombination
    • Alani E., et al. Analysis of wild-type and rad50 mutants of yeast suggests an intimate relationship between meiotic chromosome synapsis and recombination. Cell 61 (1990) 419-436
    • (1990) Cell , vol.61 , pp. 419-436
    • Alani, E.1
  • 6
    • 0025315699 scopus 로고
    • A pathway for generation and processing of double-strand breaks during meiotic recombination in S. cerevisiae
    • Cao L., et al. A pathway for generation and processing of double-strand breaks during meiotic recombination in S. cerevisiae. Cell 61 (1990) 1089-1101
    • (1990) Cell , vol.61 , pp. 1089-1101
    • Cao, L.1
  • 7
    • 0030987132 scopus 로고    scopus 로고
    • An atypical topoisomerase II from Archaea with implications for meiotic recombination
    • Bergerat A., et al. An atypical topoisomerase II from Archaea with implications for meiotic recombination. Nature 386 (1997) 414-417
    • (1997) Nature , vol.386 , pp. 414-417
    • Bergerat, A.1
  • 8
    • 0030893115 scopus 로고    scopus 로고
    • Meiosis-specific DNA double-strand breaks are catalyzed by Spo11, a member of a widely conserved protein family
    • Keeney S., et al. Meiosis-specific DNA double-strand breaks are catalyzed by Spo11, a member of a widely conserved protein family. Cell 88 (1997) 375-384
    • (1997) Cell , vol.88 , pp. 375-384
    • Keeney, S.1
  • 9
    • 3142704347 scopus 로고    scopus 로고
    • Conserved and nonconserved proteins for meiotic DNA breakage and repair in yeasts
    • Young J.A., et al. Conserved and nonconserved proteins for meiotic DNA breakage and repair in yeasts. Genetics 167 (2004) 593-605
    • (2004) Genetics , vol.167 , pp. 593-605
    • Young, J.A.1
  • 10
    • 23944459784 scopus 로고    scopus 로고
    • Endonucleolytic processing of covalent protein-linked DNA double-strand breaks
    • Neale M.J., et al. Endonucleolytic processing of covalent protein-linked DNA double-strand breaks. Nature 436 (2005) 1053-1057
    • (2005) Nature , vol.436 , pp. 1053-1057
    • Neale, M.J.1
  • 11
    • 36248942617 scopus 로고    scopus 로고
    • Sae2 is an endonuclease that processes hairpin DNA cooperatively with the Mre11/Rad50/Xrs2 complex
    • Lengsfeld B.M., et al. Sae2 is an endonuclease that processes hairpin DNA cooperatively with the Mre11/Rad50/Xrs2 complex. Mol. Cell 28 (2007) 638-651
    • (2007) Mol. Cell , vol.28 , pp. 638-651
    • Lengsfeld, B.M.1
  • 12
    • 0028212415 scopus 로고
    • Mutations in XRS2 and RAD50 delay but do not prevent mating-type switching in Saccharomyces cerevisiae
    • Ivanov E.L., et al. Mutations in XRS2 and RAD50 delay but do not prevent mating-type switching in Saccharomyces cerevisiae. Mol. Cell. Biol. 14 (1994) 3414-3425
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 3414-3425
    • Ivanov, E.L.1
  • 13
    • 0031983191 scopus 로고    scopus 로고
    • A novel mre11 mutation impairs processing of double-strand breaks of DNA during both mitosis and meiosis
    • Tsubouchi H., and Ogawa H. A novel mre11 mutation impairs processing of double-strand breaks of DNA during both mitosis and meiosis. Mol. Cell. Biol. 18 (1998) 260-268
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 260-268
    • Tsubouchi, H.1    Ogawa, H.2
  • 14
    • 33644691699 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Sae2 protein promotes resection and bridging of double strand break ends
    • Clerici M., et al. The Saccharomyces cerevisiae Sae2 protein promotes resection and bridging of double strand break ends. J. Biol. Chem. 280 (2005) 38631-38638
    • (2005) J. Biol. Chem. , vol.280 , pp. 38631-38638
    • Clerici, M.1
  • 15
    • 6344254299 scopus 로고    scopus 로고
    • The Mre11 nuclease is not required for 5′ to 3′ resection at multiple HO-induced double-strand breaks
    • Llorente B., and Symington L.S. The Mre11 nuclease is not required for 5′ to 3′ resection at multiple HO-induced double-strand breaks. Mol. Cell. Biol. 24 (2004) 9682-9694
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9682-9694
    • Llorente, B.1    Symington, L.S.2
  • 16
    • 0037169325 scopus 로고    scopus 로고
    • The Mre11 complex is required for repair of hairpin-capped double-strand breaks and prevention of chromosome rearrangements
    • Lobachev K.S., et al. The Mre11 complex is required for repair of hairpin-capped double-strand breaks and prevention of chromosome rearrangements. Cell 108 (2002) 183-193
    • (2002) Cell , vol.108 , pp. 183-193
    • Lobachev, K.S.1
  • 17
    • 0035022013 scopus 로고    scopus 로고
    • Fidelity of mitotic double-strand-break repair in Saccharomyces cerevisiae: a role for SAE2/COM1
    • Rattray A.J., et al. Fidelity of mitotic double-strand-break repair in Saccharomyces cerevisiae: a role for SAE2/COM1. Genetics 158 (2001) 109-122
    • (2001) Genetics , vol.158 , pp. 109-122
    • Rattray, A.J.1
  • 18
    • 53649104599 scopus 로고    scopus 로고
    • Sae2, Exo1 and Sgs1 collaborate in DNA double-strand break processing
    • Mimitou E.P., and Symington L.S. Sae2, Exo1 and Sgs1 collaborate in DNA double-strand break processing. Nature 455 (2008) 770-774
    • (2008) Nature , vol.455 , pp. 770-774
    • Mimitou, E.P.1    Symington, L.S.2
  • 19
    • 51549095956 scopus 로고    scopus 로고
    • Sgs1 helicase and two nucleases Dna2 and Exo1 resect DNA double-strand break ends
    • Zhu Z., et al. Sgs1 helicase and two nucleases Dna2 and Exo1 resect DNA double-strand break ends. Cell 134 (2008) 981-994
    • (2008) Cell , vol.134 , pp. 981-994
    • Zhu, Z.1
  • 20
    • 47949121598 scopus 로고    scopus 로고
    • Mre11-Rad50-Nbs1-dependent processing of DNA breaks generates oligonucleotides that stimulate ATM activity
    • Jazayeri A., et al. Mre11-Rad50-Nbs1-dependent processing of DNA breaks generates oligonucleotides that stimulate ATM activity. EMBO J. 27 (2008) 1953-1962
    • (2008) EMBO J. , vol.27 , pp. 1953-1962
    • Jazayeri, A.1
  • 21
    • 4544281398 scopus 로고    scopus 로고
    • Choreography of the DNA damage response: spatiotemporal relationships among checkpoint and repair proteins
    • Lisby M., et al. Choreography of the DNA damage response: spatiotemporal relationships among checkpoint and repair proteins. Cell 118 (2004) 699-713
    • (2004) Cell , vol.118 , pp. 699-713
    • Lisby, M.1
  • 22
    • 4644257681 scopus 로고    scopus 로고
    • Distribution and dynamics of chromatin modification induced by a defined DNA double-strand break
    • Shroff R., et al. Distribution and dynamics of chromatin modification induced by a defined DNA double-strand break. Curr. Biol. 14 (2004) 1703-1711
    • (2004) Curr. Biol. , vol.14 , pp. 1703-1711
    • Shroff, R.1
  • 23
    • 34948872046 scopus 로고    scopus 로고
    • Ctp1 is a cell-cycle-regulated protein that functions with Mre11 complex to control double-strand break repair by homologous recombination
    • Limbo O., et al. Ctp1 is a cell-cycle-regulated protein that functions with Mre11 complex to control double-strand break repair by homologous recombination. Mol. Cell 28 (2007) 134-146
    • (2007) Mol. Cell , vol.28 , pp. 134-146
    • Limbo, O.1
  • 24
    • 52949149420 scopus 로고    scopus 로고
    • Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair
    • Williams R.S., et al. Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair. Cell 135 (2008) 97-109
    • (2008) Cell , vol.135 , pp. 97-109
    • Williams, R.S.1
  • 25
    • 52949109260 scopus 로고    scopus 로고
    • Mre11 nuclease activity has essential roles in DNA repair and genomic stability distinct from ATM activation
    • Buis J., et al. Mre11 nuclease activity has essential roles in DNA repair and genomic stability distinct from ATM activation. Cell 135 (2008) 85-96
    • (2008) Cell , vol.135 , pp. 85-96
    • Buis, J.1
  • 26
    • 36549060102 scopus 로고    scopus 로고
    • Human CtIP promotes DNA end resection
    • Sartori A.A., et al. Human CtIP promotes DNA end resection. Nature 450 (2007) 509-514
    • (2007) Nature , vol.450 , pp. 509-514
    • Sartori, A.A.1
  • 27
    • 5044219898 scopus 로고    scopus 로고
    • EXO1 - a multi-tasking eukaryotic nuclease
    • Tran P.T., et al. EXO1 - a multi-tasking eukaryotic nuclease. DNA Repair (Amst.) 3 (2004) 1549-1559
    • (2004) DNA Repair (Amst.) , vol.3 , pp. 1549-1559
    • Tran, P.T.1
  • 28
    • 11344268431 scopus 로고    scopus 로고
    • Exo1 processes stalled replication forks and counteracts fork reversal in checkpoint-defective cells
    • Cotta-Ramusino C., et al. Exo1 processes stalled replication forks and counteracts fork reversal in checkpoint-defective cells. Mol. Cell 17 (2005) 153-159
    • (2005) Mol. Cell , vol.17 , pp. 153-159
    • Cotta-Ramusino, C.1
  • 29
    • 0036682516 scopus 로고    scopus 로고
    • EXO1-dependent single-stranded DNA at telomeres activates subsets of DNA damage and spindle checkpoint pathways in budding yeast yku70Δ mutants
    • Maringele L., and Lydall D. EXO1-dependent single-stranded DNA at telomeres activates subsets of DNA damage and spindle checkpoint pathways in budding yeast yku70Δ mutants. Genes Dev. 16 (2002) 1919-1933
    • (2002) Genes Dev. , vol.16 , pp. 1919-1933
    • Maringele, L.1    Lydall, D.2
  • 30
    • 0042991423 scopus 로고    scopus 로고
    • Competition between the Rad50 complex and the Ku heterodimer reveals a role for Exo1 in processing double-strand breaks but not telomeres
    • Tomita K., et al. Competition between the Rad50 complex and the Ku heterodimer reveals a role for Exo1 in processing double-strand breaks but not telomeres. Mol. Cell. Biol. 23 (2003) 5186-5197
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 5186-5197
    • Tomita, K.1
  • 31
    • 0037459374 scopus 로고    scopus 로고
    • Interchangeable parts of the Escherichia coli recombination machinery
    • Amundsen S.K., and Smith G.R. Interchangeable parts of the Escherichia coli recombination machinery. Cell 112 (2003) 741-744
    • (2003) Cell , vol.112 , pp. 741-744
    • Amundsen, S.K.1    Smith, G.R.2
  • 32
    • 0028033989 scopus 로고
    • The yeast type I topoisomerase Top3 interacts with Sgs1, a DNA helicase homolog: a potential eukaryotic reverse gyrase
    • Gangloff S., et al. The yeast type I topoisomerase Top3 interacts with Sgs1, a DNA helicase homolog: a potential eukaryotic reverse gyrase. Mol. Cell. Biol. 14 (1994) 8391-8398
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 8391-8398
    • Gangloff, S.1
  • 33
    • 53649090109 scopus 로고    scopus 로고
    • DNA helicases Sgs1 and BLM promote DNA double-strand break resection
    • Gravel S., et al. DNA helicases Sgs1 and BLM promote DNA double-strand break resection. Genes Dev. 22 (2008) 2767-2772
    • (2008) Genes Dev. , vol.22 , pp. 2767-2772
    • Gravel, S.1
  • 34
    • 0028785586 scopus 로고
    • The Bloom's syndrome gene product is homologous to RecQ helicases
    • Ellis N.A., et al. The Bloom's syndrome gene product is homologous to RecQ helicases. Cell 83 (1995) 655-666
    • (1995) Cell , vol.83 , pp. 655-666
    • Ellis, N.A.1
  • 35
    • 0141567744 scopus 로고    scopus 로고
    • RecQ helicases: suppressors of tumorigenesis and premature aging
    • Bachrati C.Z., and Hickson I.D. RecQ helicases: suppressors of tumorigenesis and premature aging. Biochem. J. 374 (2003) 577-606
    • (2003) Biochem. J. , vol.374 , pp. 577-606
    • Bachrati, C.Z.1    Hickson, I.D.2
  • 36
    • 33645215616 scopus 로고    scopus 로고
    • Evidence suggesting that Pif1 helicase functions in DNA replication with the Dna2 helicase/nuclease and DNA polymerase delta
    • Budd M.E., et al. Evidence suggesting that Pif1 helicase functions in DNA replication with the Dna2 helicase/nuclease and DNA polymerase delta. Mol. Cell. Biol. 26 (2006) 2490-2500
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2490-2500
    • Budd, M.E.1
  • 37
    • 56049111594 scopus 로고    scopus 로고
    • Identification of the Xenopus DNA2 protein as a major nuclease for the 5′→3′ strand-specific processing of DNA ends
    • Liao S., et al. Identification of the Xenopus DNA2 protein as a major nuclease for the 5′→3′ strand-specific processing of DNA ends. Nucleic Acids Res. 36 (2008) 6091-6100
    • (2008) Nucleic Acids Res. , vol.36 , pp. 6091-6100
    • Liao, S.1
  • 38
    • 55949105327 scopus 로고    scopus 로고
    • Human exonuclease 1 and BLM helicase interact to resect DNA and initiate DNA repair
    • Nimonkar A.V., et al. Human exonuclease 1 and BLM helicase interact to resect DNA and initiate DNA repair. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 16906-16911
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 16906-16911
    • Nimonkar, A.V.1
  • 39
    • 53549093050 scopus 로고    scopus 로고
    • The P. furiosus mre11/rad50 complex promotes 5′ strand resection at a DNA double-strand break
    • Hopkins B.B., and Paull T.T. The P. furiosus mre11/rad50 complex promotes 5′ strand resection at a DNA double-strand break. Cell 135 (2008) 250-260
    • (2008) Cell , vol.135 , pp. 250-260
    • Hopkins, B.B.1    Paull, T.T.2
  • 40
    • 29244463205 scopus 로고    scopus 로고
    • Nonhomologous end joining in yeast
    • Daley J.M., et al. Nonhomologous end joining in yeast. Annu. Rev. Genet. 39 (2005) 431-451
    • (2005) Annu. Rev. Genet. , vol.39 , pp. 431-451
    • Daley, J.M.1
  • 41
    • 11244269445 scopus 로고    scopus 로고
    • The CDK regulates repair of double-strand breaks by homologous recombination during the cell cycle
    • Aylon Y., et al. The CDK regulates repair of double-strand breaks by homologous recombination during the cell cycle. EMBO J. 23 (2004) 4868-4875
    • (2004) EMBO J. , vol.23 , pp. 4868-4875
    • Aylon, Y.1
  • 42
    • 7244220162 scopus 로고    scopus 로고
    • DNA end resection, homologous recombination and DNA damage checkpoint activation require CDK1
    • Ira G., et al. DNA end resection, homologous recombination and DNA damage checkpoint activation require CDK1. Nature 431 (2004) 1011-1017
    • (2004) Nature , vol.431 , pp. 1011-1017
    • Ira, G.1
  • 43
    • 48649086824 scopus 로고    scopus 로고
    • The Yku70-Yku80 complex contributes to regulate double-strand break processing and checkpoint activation during the cell cycle
    • Clerici M., et al. The Yku70-Yku80 complex contributes to regulate double-strand break processing and checkpoint activation during the cell cycle. EMBO Rep. 9 (2008) 810-818
    • (2008) EMBO Rep. , vol.9 , pp. 810-818
    • Clerici, M.1
  • 44
    • 2942594756 scopus 로고    scopus 로고
    • The functions of budding yeast Sae2 in the DNA damage response require Mec1- and Tel1-dependent phosphorylation
    • Baroni E., et al. The functions of budding yeast Sae2 in the DNA damage response require Mec1- and Tel1-dependent phosphorylation. Mol. Cell. Biol. 24 (2004) 4151-4165
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 4151-4165
    • Baroni, E.1
  • 45
    • 53349162987 scopus 로고    scopus 로고
    • CDK targets Sae2 to control DNA-end resection and homologous recombination
    • Huertas P., et al. CDK targets Sae2 to control DNA-end resection and homologous recombination. Nature 455 (2008) 689-692
    • (2008) Nature , vol.455 , pp. 689-692
    • Huertas, P.1
  • 46
    • 34147205098 scopus 로고    scopus 로고
    • Inverted DNA repeats channel repair of distant double-strand breaks into chromatid fusions and chromosomal rearrangements
    • VanHulle K., et al. Inverted DNA repeats channel repair of distant double-strand breaks into chromatid fusions and chromosomal rearrangements. Mol. Cell. Biol. 27 (2007) 2601-2614
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 2601-2614
    • VanHulle, K.1
  • 47
    • 33751419716 scopus 로고    scopus 로고
    • Surviving the breakup: the DNA damage checkpoint
    • Harrison J.C., and Haber J.E. Surviving the breakup: the DNA damage checkpoint. Annu. Rev. Genet. 40 (2006) 209-235
    • (2006) Annu. Rev. Genet. , vol.40 , pp. 209-235
    • Harrison, J.C.1    Haber, J.E.2
  • 48
    • 38349073475 scopus 로고    scopus 로고
    • DNA damage response at functional and dysfunctional telomeres
    • Longhese M.P. DNA damage response at functional and dysfunctional telomeres. Genes Dev. 22 (2008) 125-140
    • (2008) Genes Dev. , vol.22 , pp. 125-140
    • Longhese, M.P.1
  • 49
    • 44349180168 scopus 로고    scopus 로고
    • Histone methyltransferase Dot1 and Rad9 inhibit single-stranded DNA accumulation at DSBs and uncapped telomeres
    • Lazzaro F., et al. Histone methyltransferase Dot1 and Rad9 inhibit single-stranded DNA accumulation at DSBs and uncapped telomeres. EMBO J. 27 (2008) 1502-1512
    • (2008) EMBO J. , vol.27 , pp. 1502-1512
    • Lazzaro, F.1
  • 50
    • 39149129387 scopus 로고    scopus 로고
    • ATR-dependent pathways control hEXO1 stability in response to stalled forks
    • El-Shemerly M., et al. ATR-dependent pathways control hEXO1 stability in response to stalled forks. Nucleic Acids Res. 36 (2008) 511-519
    • (2008) Nucleic Acids Res. , vol.36 , pp. 511-519
    • El-Shemerly, M.1
  • 51
    • 51949118680 scopus 로고    scopus 로고
    • Checkpoint-dependent phosphorylation of Exo1 modulates the DNA damage response
    • Morin I., et al. Checkpoint-dependent phosphorylation of Exo1 modulates the DNA damage response. EMBO J. 27 (2008) 2400-2410
    • (2008) EMBO J. , vol.27 , pp. 2400-2410
    • Morin, I.1
  • 52
    • 34547499407 scopus 로고    scopus 로고
    • Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases
    • Smolka M.B., et al. Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 10364-10369
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 10364-10369
    • Smolka, M.B.1
  • 53
    • 33645799075 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae Sae2 protein negatively regulates DNA damage checkpoint signalling
    • Clerici M., et al. The Saccharomyces cerevisiae Sae2 protein negatively regulates DNA damage checkpoint signalling. EMBO Rep. 7 (2006) 212-218
    • (2006) EMBO Rep. , vol.7 , pp. 212-218
    • Clerici, M.1
  • 54
    • 0026331068 scopus 로고
    • Formation and resolution of recombination intermediates by E. coli RecA and RuvC proteins
    • Dunderdale H.J., et al. Formation and resolution of recombination intermediates by E. coli RecA and RuvC proteins. Nature 354 (1991) 506-510
    • (1991) Nature , vol.354 , pp. 506-510
    • Dunderdale, H.J.1
  • 55
    • 56749119855 scopus 로고    scopus 로고
    • Identification of Holliday junction resolvases from humans and yeast
    • Ip S.C., et al. Identification of Holliday junction resolvases from humans and yeast. Nature 456 (2008) 357-361
    • (2008) Nature , vol.456 , pp. 357-361
    • Ip, S.C.1
  • 56
    • 33749603235 scopus 로고    scopus 로고
    • A network of multi-tasking proteins at the DNA replication fork preserves genome stability
    • Budd M.E., et al. A network of multi-tasking proteins at the DNA replication fork preserves genome stability. PLoS Genet. 1 (2005) e61
    • (2005) PLoS Genet. , vol.1
    • Budd, M.E.1
  • 57
    • 0345447604 scopus 로고    scopus 로고
    • Srs2 and Sgs1-Top3 suppress crossovers during double-strand break repair in yeast
    • Ira G., et al. Srs2 and Sgs1-Top3 suppress crossovers during double-strand break repair in yeast. Cell 115 (2003) 401-411
    • (2003) Cell , vol.115 , pp. 401-411
    • Ira, G.1
  • 58
    • 34447536139 scopus 로고    scopus 로고
    • BLM ortholog, Sgs1, prevents aberrant crossing-over by suppressing formation of multichromatid joint molecules
    • Oh S.D., et al. BLM ortholog, Sgs1, prevents aberrant crossing-over by suppressing formation of multichromatid joint molecules. Cell 130 (2007) 259-272
    • (2007) Cell , vol.130 , pp. 259-272
    • Oh, S.D.1
  • 59
    • 0347987856 scopus 로고    scopus 로고
    • The Bloom's syndrome helicase suppresses crossing over during homologous recombination
    • Wu L., and Hickson I.D. The Bloom's syndrome helicase suppresses crossing over during homologous recombination. Nature 426 (2003) 870-874
    • (2003) Nature , vol.426 , pp. 870-874
    • Wu, L.1    Hickson, I.D.2
  • 60
    • 54349099705 scopus 로고    scopus 로고
    • RMI, a new OB-fold complex essential for Bloom syndrome protein to maintain genome stability
    • Xu D., et al. RMI, a new OB-fold complex essential for Bloom syndrome protein to maintain genome stability. Genes Dev. 22 (2008) 2843-2855
    • (2008) Genes Dev. , vol.22 , pp. 2843-2855
    • Xu, D.1
  • 61
    • 54349114671 scopus 로고    scopus 로고
    • BLAP18/RMI2, a novel OB-fold-containing protein, is an essential component of the Bloom helicase-double Holliday junction dissolvasome
    • Singh T.R., et al. BLAP18/RMI2, a novel OB-fold-containing protein, is an essential component of the Bloom helicase-double Holliday junction dissolvasome. Genes Dev. 22 (2008) 2856-2868
    • (2008) Genes Dev. , vol.22 , pp. 2856-2868
    • Singh, T.R.1
  • 62
    • 0346351375 scopus 로고
    • A manyfold increase in sister chromatid exchanges in Bloom's syndrome lymphocytes
    • Chaganti R.S., et al. A manyfold increase in sister chromatid exchanges in Bloom's syndrome lymphocytes. Proc. Natl. Acad. Sci. U. S. A. 71 (1974) 4508-4512
    • (1974) Proc. Natl. Acad. Sci. U. S. A. , vol.71 , pp. 4508-4512
    • Chaganti, R.S.1
  • 63
    • 0942279596 scopus 로고    scopus 로고
    • The Mus81 solution to resolution: generating meiotic crossovers without Holliday junctions
    • Hollingsworth N.M., and Brill S.J. The Mus81 solution to resolution: generating meiotic crossovers without Holliday junctions. Genes Dev. 18 (2004) 117-125
    • (2004) Genes Dev. , vol.18 , pp. 117-125
    • Hollingsworth, N.M.1    Brill, S.J.2
  • 64
    • 0035900652 scopus 로고    scopus 로고
    • Mus81-Eme1 are essential components of a Holliday junction resolvase
    • Boddy M.N., et al. Mus81-Eme1 are essential components of a Holliday junction resolvase. Cell 107 (2001) 537-548
    • (2001) Cell , vol.107 , pp. 537-548
    • Boddy, M.N.1
  • 65
    • 0141707817 scopus 로고    scopus 로고
    • Generating crossovers by resolution of nicked Holliday junctions: a role for Mus81-Eme1 in meiosis
    • Osman F., et al. Generating crossovers by resolution of nicked Holliday junctions: a role for Mus81-Eme1 in meiosis. Mol. Cell 12 (2003) 761-774
    • (2003) Mol. Cell , vol.12 , pp. 761-774
    • Osman, F.1
  • 66
    • 34248202607 scopus 로고    scopus 로고
    • Mus81-Eme1-dependent and -independent crossovers form in mitotic cells during double-strand break repair in Schizosaccharomyces pombe
    • Hope J.C., et al. Mus81-Eme1-dependent and -independent crossovers form in mitotic cells during double-strand break repair in Schizosaccharomyces pombe. Mol. Cell. Biol. 27 (2007) 3828-3838
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 3828-3838
    • Hope, J.C.1
  • 67
    • 53149087431 scopus 로고    scopus 로고
    • The FANCM ortholog Fml1 promotes recombination at stalled replication forks and limits crossing over during DNA double-strand break repair
    • Sun W., et al. The FANCM ortholog Fml1 promotes recombination at stalled replication forks and limits crossing over during DNA double-strand break repair. Mol. Cell 32 (2008) 118-128
    • (2008) Mol. Cell , vol.32 , pp. 118-128
    • Sun, W.1
  • 68
    • 11244321837 scopus 로고    scopus 로고
    • Competing crossover pathways act during meiosis in Saccharomyces cerevisiae
    • Argueso J.L., et al. Competing crossover pathways act during meiosis in Saccharomyces cerevisiae. Genetics 168 (2004) 1805-1816
    • (2004) Genetics , vol.168 , pp. 1805-1816
    • Argueso, J.L.1
  • 69
    • 52949098362 scopus 로고    scopus 로고
    • MUS81 generates a subset of MLH1-MLH3-independent crossovers in mammalian meiosis
    • Holloway J.K., et al. MUS81 generates a subset of MLH1-MLH3-independent crossovers in mammalian meiosis. PLoS Genet. 4 (2008) e1000186
    • (2008) PLoS Genet. , vol.4
    • Holloway, J.K.1
  • 70
    • 33746189409 scopus 로고    scopus 로고
    • Endonucleolytic function of MutLα in human mismatch repair
    • Kadyrov F.A., et al. Endonucleolytic function of MutLα in human mismatch repair. Cell 126 (2006) 297-308
    • (2006) Cell , vol.126 , pp. 297-308
    • Kadyrov, F.A.1
  • 71
    • 49849087552 scopus 로고    scopus 로고
    • A mutation in the putative MLH3 endonuclease domain confers a defect in both mismatch repair and meiosis in Saccharomyces cerevisiae
    • Nishant K.T., et al. A mutation in the putative MLH3 endonuclease domain confers a defect in both mismatch repair and meiosis in Saccharomyces cerevisiae. Genetics 179 (2008) 747-755
    • (2008) Genetics , vol.179 , pp. 747-755
    • Nishant, K.T.1
  • 72
    • 0034727684 scopus 로고    scopus 로고
    • Binding and melting of D-loops by the Bloom syndrome helicase
    • van Brabant A.J., et al. Binding and melting of D-loops by the Bloom syndrome helicase. Biochemistry 39 (2000) 14617-14625
    • (2000) Biochemistry , vol.39 , pp. 14617-14625
    • van Brabant, A.J.1
  • 73
    • 53549122238 scopus 로고    scopus 로고
    • RTEL1 maintains genomic stability by suppressing homologous recombination
    • Barber L.J., et al. RTEL1 maintains genomic stability by suppressing homologous recombination. Cell 135 (2008) 261-271
    • (2008) Cell , vol.135 , pp. 261-271
    • Barber, L.J.1
  • 74
    • 38649130654 scopus 로고    scopus 로고
    • The Srs2 helicase activity is stimulated by Rad51 filaments on dsDNA: implications for crossover incidence during mitotic recombination
    • Dupaigne P., et al. The Srs2 helicase activity is stimulated by Rad51 filaments on dsDNA: implications for crossover incidence during mitotic recombination. Mol. Cell 29 (2008) 243-254
    • (2008) Mol. Cell , vol.29 , pp. 243-254
    • Dupaigne, P.1
  • 75
    • 55849133052 scopus 로고    scopus 로고
    • Remodeling of DNA replication structures by the branch point translocase FANCM
    • Gari K., et al. Remodeling of DNA replication structures by the branch point translocase FANCM. Proc. Natl. Acad. Sci. U. S. A. 105 (2008) 16107-16112
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 16107-16112
    • Gari, K.1
  • 76
    • 21244434850 scopus 로고    scopus 로고
    • RMI1/NCE4, a suppressor of genome instability, encodes a member of the RecQ helicase/Topo III complex
    • Chang M., et al. RMI1/NCE4, a suppressor of genome instability, encodes a member of the RecQ helicase/Topo III complex. EMBO J. 24 (2005) 2024-2033
    • (2005) EMBO J. , vol.24 , pp. 2024-2033
    • Chang, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.