메뉴 건너뛰기




Volumn 135, Issue 2, 2008, Pages 250-260

The P. furiosus Mre11/Rad50 Complex Promotes 5′ Strand Resection at a DNA Double-Strand Break

Author keywords

DNA

Indexed keywords

EXONUCLEASE; HELICASE; MRE11 PROTEIN; PROTEIN HERA; PROTEIN NURA; PROTEIN RADA; RAD50 PROTEIN; RECA PROTEIN; RECOMBINASE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 53549093050     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2008.09.054     Document Type: Article
Times cited : (138)

References (49)
  • 1
    • 0025334351 scopus 로고
    • Analysis of wild-type and rad50 mutants of yeast suggests an intimate relationship between meiotic chromosome synapsis and recombination
    • Alani E., Padmore R., and Kleckner N. 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    Padmore, R.2    Kleckner, N.3
  • 2
    • 10644271631 scopus 로고    scopus 로고
    • Archaeal genetics-the third way
    • Allers T., and Mevarech M. Archaeal genetics-the third way. Nat. Rev. Genet. 6 (2005) 58-73
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 58-73
    • Allers, T.1    Mevarech, M.2
  • 3
    • 37249047064 scopus 로고    scopus 로고
    • Intersubunit signaling in RecBCD enzyme, a complex protein machine regulated by Chi hot spots
    • Amundsen S.K., Taylor A.F., Reddy M., and Smith G.R. Intersubunit signaling in RecBCD enzyme, a complex protein machine regulated by Chi hot spots. Genes Dev. 21 (2007) 3296-3307
    • (2007) Genes Dev. , vol.21 , pp. 3296-3307
    • Amundsen, S.K.1    Taylor, A.F.2    Reddy, M.3    Smith, G.R.4
  • 4
    • 0034889360 scopus 로고    scopus 로고
    • Prokaryotic homologs of the eukaryotic DNA-end-binding protein Ku, novel domains in the Ku protein and prediction of a prokaryotic double-strand break repair system
    • Aravind L., and Koonin E.V. Prokaryotic homologs of the eukaryotic DNA-end-binding protein Ku, novel domains in the Ku protein and prediction of a prokaryotic double-strand break repair system. Genome Res. 11 (2001) 1365-1374
    • (2001) Genome Res. , vol.11 , pp. 1365-1374
    • Aravind, L.1    Koonin, E.V.2
  • 6
    • 11244269445 scopus 로고    scopus 로고
    • The CDK regulates repair of double-strand breaks by homologous recombination during the cell cycle
    • Aylon Y., Liefshitz B., and Kupiec M. 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    Liefshitz, B.2    Kupiec, M.3
  • 7
    • 39549114009 scopus 로고    scopus 로고
    • Differential regulation of the cellular response to DNA double-strand breaks in G1
    • Barlow J.H., Lisby M., and Rothstein R. Differential regulation of the cellular response to DNA double-strand breaks in G1. Mol. Cell 30 (2008) 73-85
    • (2008) Mol. Cell , vol.30 , pp. 73-85
    • Barlow, J.H.1    Lisby, M.2    Rothstein, R.3
  • 9
    • 0030756165 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of the SbcCD protein from Escherichia coli
    • Connelly J.C., de Leau E.S., Okely E.A., and Leach D.R. Overexpression, purification, and characterization of the SbcCD protein from Escherichia coli. J. Biol. Chem. 272 (1997) 19819-19826
    • (1997) J. Biol. Chem. , vol.272 , pp. 19819-19826
    • Connelly, J.C.1    de Leau, E.S.2    Okely, E.A.3    Leach, D.R.4
  • 10
    • 0033557344 scopus 로고    scopus 로고
    • DNA cleavage and degradation by the SbcCD protein complex from Escherichia coli
    • Connelly J.C., de Leau E.S., and Leach D.R.F. DNA cleavage and degradation by the SbcCD protein complex from Escherichia coli. Nucleic Acids Res. 27 (1999) 1039-1046
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1039-1046
    • Connelly, J.C.1    de Leau, E.S.2    Leach, D.R.F.3
  • 11
    • 0036305477 scopus 로고    scopus 로고
    • NurA, a novel 5′-3′ nuclease gene linked to rad50 and mre11 homologs of thermophilic Archaea
    • Constantinesco F., Forterre P., and Elie C. NurA, a novel 5′-3′ nuclease gene linked to rad50 and mre11 homologs of thermophilic Archaea. EMBO Rep. 3 (2002) 537-542
    • (2002) EMBO Rep. , vol.3 , pp. 537-542
    • Constantinesco, F.1    Forterre, P.2    Elie, C.3
  • 12
    • 2442670846 scopus 로고    scopus 로고
    • A bipolar DNA helicase gene, herA, clusters with rad50, mre11 and nurA genes in thermophilic archaea
    • Constantinesco F., Forterre P., Koonin E.V., Aravind L., and Elie C. A bipolar DNA helicase gene, herA, clusters with rad50, mre11 and nurA genes in thermophilic archaea. Nucleic Acids Res. 32 (2004) 1439-1447
    • (2004) Nucleic Acids Res. , vol.32 , pp. 1439-1447
    • Constantinesco, F.1    Forterre, P.2    Koonin, E.V.3    Aravind, L.4    Elie, C.5
  • 13
    • 0036276388 scopus 로고    scopus 로고
    • The Mre11 complex: at the crossroads of dna repair and checkpoint signalling
    • D'Amours D., and Jackson S.P. The Mre11 complex: at the crossroads of dna repair and checkpoint signalling. Nat. Rev. Mol. Cell Biol. 3 (2002) 317-327
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 317-327
    • D'Amours, D.1    Jackson, S.P.2
  • 14
    • 0035816444 scopus 로고    scopus 로고
    • Identification of bacterial homologues of the Ku DNA repair proteins
    • Doherty A.J., Jackson S.P., and Weller G.R. Identification of bacterial homologues of the Ku DNA repair proteins. FEBS Lett. 500 (2001) 186-188
    • (2001) FEBS Lett. , vol.500 , pp. 186-188
    • Doherty, A.J.1    Jackson, S.P.2    Weller, G.R.3
  • 15
    • 0033759543 scopus 로고    scopus 로고
    • Mre11 and Rad50 from Pyrococcus furiosus: cloning and biochemical characterization reveal an evolutionarily conserved multiprotein machine
    • Hopfner K.P., Karcher A., Shin D., Fairley C., Tainer J.A., and Carney J.P. Mre11 and Rad50 from Pyrococcus furiosus: cloning and biochemical characterization reveal an evolutionarily conserved multiprotein machine. J. Bacteriol. 182 (2000) 6036-6041
    • (2000) J. Bacteriol. , vol.182 , pp. 6036-6041
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.3    Fairley, C.4    Tainer, J.A.5    Carney, J.P.6
  • 16
    • 0034705293 scopus 로고    scopus 로고
    • Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily
    • Hopfner K.P., Karcher A., Shin D.S., Craig L., Arthur L.M., Carney J.P., and Tainer J.A. Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell 101 (2000) 789-800
    • (2000) Cell , vol.101 , pp. 789-800
    • Hopfner, K.P.1    Karcher, A.2    Shin, D.S.3    Craig, L.4    Arthur, L.M.5    Carney, J.P.6    Tainer, J.A.7
  • 17
    • 0035906860 scopus 로고    scopus 로고
    • Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase
    • Hopfner K.P., Karcher A., Craig L., Woo T.T., Carney J.P., and Tainer J.A. Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase. Cell 105 (2001) 473-485
    • (2001) Cell , vol.105 , pp. 473-485
    • Hopfner, K.P.1    Karcher, A.2    Craig, L.3    Woo, T.T.4    Carney, J.P.5    Tainer, J.A.6
  • 20
    • 0028212415 scopus 로고
    • Mutations in XRS2 and RAD50 delay but do not prevent mating-type switching in Saccharomyces cerevisiae
    • Ivanov E.L., Sugawara N., White C.I., Fabre F., and Haber J.E. 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    Sugawara, N.2    White, C.I.3    Fabre, F.4    Haber, J.E.5
  • 23
    • 40349106220 scopus 로고    scopus 로고
    • Insights into different dependence of dNTP triphosphohydrolase on metal ion species from intracellular ion concentrations in Thermus thermophilus
    • Kondo N., Nishikubo T., Wakamatsu T., Ishikawa H., Nakagawa N., Kuramitsu S., and Masui R. Insights into different dependence of dNTP triphosphohydrolase on metal ion species from intracellular ion concentrations in Thermus thermophilus. Extremophiles 12 (2008) 217-223
    • (2008) Extremophiles , vol.12 , pp. 217-223
    • Kondo, N.1    Nishikubo, T.2    Wakamatsu, T.3    Ishikawa, H.4    Nakagawa, N.5    Kuramitsu, S.6    Masui, R.7
  • 25
    • 0032715175 scopus 로고    scopus 로고
    • Recombinational repair of DNA damage in Escherichia coli and bacteriophage lambda
    • Kuzminov A. Recombinational repair of DNA damage in Escherichia coli and bacteriophage lambda. Microbiol. Mol. Biol. Rev. 63 (1999) 751-813
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 751-813
    • Kuzminov, A.1
  • 26
    • 4544281398 scopus 로고    scopus 로고
    • Choreography of the DNA damage response: Spatiotemporal relationships among checkpoint and repair proteins
    • Lisby M., Barlow J.H., Burgess R.C., and Rothstein R. 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    Barlow, J.H.2    Burgess, R.C.3    Rothstein, R.4
  • 28
    • 53649104599 scopus 로고    scopus 로고
    • Sae2/CtIP, Exo1 and Sgs1 collaborate in DNA double-strand break processing
    • 10.1038/nature07312 Published online September 21, 2008
    • Mimitou E.P., and Symington L.S. Sae2/CtIP, Exo1 and Sgs1 collaborate in DNA double-strand break processing. Nature (2008) 10.1038/nature07312 Published online September 21, 2008
    • (2008) Nature
    • Mimitou, E.P.1    Symington, L.S.2
  • 30
    • 0032931844 scopus 로고    scopus 로고
    • The nuclease activity of Mre11 is required for meiosis but not for mating type switching, end joining, or telomere maintenance
    • Moreau S., Ferguson J.R., and Symington L.S. The nuclease activity of Mre11 is required for meiosis but not for mating type switching, end joining, or telomere maintenance. Mol. Cell. Biol. 19 (1999) 556-566
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 556-566
    • Moreau, S.1    Ferguson, J.R.2    Symington, L.S.3
  • 31
    • 0030885998 scopus 로고    scopus 로고
    • mre11S-a yeast mutation that blocks double-strand-break processing and permits nonhomologous synapsis in meiosis
    • Nairz K., and Klein F. mre11S-a yeast mutation that blocks double-strand-break processing and permits nonhomologous synapsis in meiosis. Genes Dev. 11 (1997) 2272-2290
    • (1997) Genes Dev. , vol.11 , pp. 2272-2290
    • Nairz, K.1    Klein, F.2
  • 32
    • 0032085295 scopus 로고    scopus 로고
    • The 3′ to 5′ exonuclease activity of Mre11 facilitates repair of DNA double-strand breaks
    • Paull T.T., and Gellert M. The 3′ to 5′ exonuclease activity of Mre11 facilitates repair of DNA double-strand breaks. Mol. Cell 1 (1998) 969-979
    • (1998) Mol. Cell , vol.1 , pp. 969-979
    • Paull, T.T.1    Gellert, M.2
  • 33
    • 0033563229 scopus 로고    scopus 로고
    • Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex
    • Paull T.T., and Gellert M. Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex. Genes Dev. 13 (1999) 1276-1288
    • (1999) Genes Dev. , vol.13 , pp. 1276-1288
    • Paull, T.T.1    Gellert, M.2
  • 34
    • 41749101058 scopus 로고    scopus 로고
    • The Mre11 protein interacts with both Rad50 and the HerA bipolar helicase and is recruited to DNA following gamma irradiation in the archaeon Sulfolobus acidocaldarius
    • Quaiser A., Constantinesco F., White M.F., Forterre P., and Elie C. The Mre11 protein interacts with both Rad50 and the HerA bipolar helicase and is recruited to DNA following gamma irradiation in the archaeon Sulfolobus acidocaldarius. BMC Mol. Biol. 9 (2008) 25
    • (2008) BMC Mol. Biol. , vol.9 , pp. 25
    • Quaiser, A.1    Constantinesco, F.2    White, M.F.3    Forterre, P.4    Elie, C.5
  • 35
    • 0032079749 scopus 로고    scopus 로고
    • RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange
    • Seitz E.M., Brockman J.P., Sandler S.J., Clark A.J., and Kowalczykowski S.C. RadA protein is an archaeal RecA protein homolog that catalyzes DNA strand exchange. Genes Dev. 12 (1998) 1248-1253
    • (1998) Genes Dev. , vol.12 , pp. 1248-1253
    • Seitz, E.M.1    Brockman, J.P.2    Sandler, S.J.3    Clark, A.J.4    Kowalczykowski, S.C.5
  • 38
    • 0035671854 scopus 로고    scopus 로고
    • Homologous recombination near and far from DNA breaks: Alternative roles and contrasting views
    • Smith G.R. Homologous recombination near and far from DNA breaks: Alternative roles and contrasting views. Annu. Rev. Genet. 35 (2001) 243-274
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 243-274
    • Smith, G.R.1
  • 39
    • 33747889217 scopus 로고    scopus 로고
    • Differential usage of non-homologous end-joining and homologous recombination in double strand break repair
    • Sonoda E., Hochegger H., Saberi A., Taniguchi Y., and Takeda S. Differential usage of non-homologous end-joining and homologous recombination in double strand break repair. DNA Repair (Amst.) 5 (2006) 1021-1029
    • (2006) DNA Repair (Amst.) , vol.5 , pp. 1021-1029
    • Sonoda, E.1    Hochegger, H.2    Saberi, A.3    Taniguchi, Y.4    Takeda, S.5
  • 40
    • 32444451553 scopus 로고    scopus 로고
    • The RecA binding locus of RecBCD is a general domain for recruitment of DNA strand exchange proteins
    • Spies M., and Kowalczykowski S.C. The RecA binding locus of RecBCD is a general domain for recruitment of DNA strand exchange proteins. Mol. Cell 21 (2006) 573-580
    • (2006) Mol. Cell , vol.21 , pp. 573-580
    • Spies, M.1    Kowalczykowski, S.C.2
  • 41
    • 0141540814 scopus 로고    scopus 로고
    • A molecular throttle: The recombination hotspot chi controls DNA translocation by the RecBCD helicase
    • Spies M., Bianco P.R., Dillingham M.S., Handa N., Baskin R.J., and Kowalczykowski S.C. A molecular throttle: The recombination hotspot chi controls DNA translocation by the RecBCD helicase. Cell 114 (2003) 647-654
    • (2003) Cell , vol.114 , pp. 647-654
    • Spies, M.1    Bianco, P.R.2    Dillingham, M.S.3    Handa, N.4    Baskin, R.J.5    Kowalczykowski, S.C.6
  • 42
    • 0036900120 scopus 로고    scopus 로고
    • Role of RAD52 epistasis group genes in homologous recombination and double-strand break repair
    • Symington L.S. Role of RAD52 epistasis group genes in homologous recombination and double-strand break repair. Microbiol. Mol. Biol. Rev. 66 (2002) 630-670
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 630-670
    • Symington, L.S.1
  • 43
    • 0035929667 scopus 로고    scopus 로고
    • DNA structure-specific nuclease activities in the Saccharomyces cerevisiae Rad50/Mre11 complex
    • Trujillo K.M., and Sung P. DNA structure-specific nuclease activities in the Saccharomyces cerevisiae Rad50/Mre11 complex. J. Biol. Chem. 276 (2001) 35458-35464
    • (2001) J. Biol. Chem. , vol.276 , pp. 35458-35464
    • Trujillo, K.M.1    Sung, P.2
  • 44
    • 0032555480 scopus 로고    scopus 로고
    • Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, and p95
    • Trujillo K.M., Yuan S.S., Lee E.Y., and Sung P. Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, and p95. J. Biol. Chem. 273 (1998) 21447-21450
    • (1998) J. Biol. Chem. , vol.273 , pp. 21447-21450
    • Trujillo, K.M.1    Yuan, S.S.2    Lee, E.Y.3    Sung, P.4
  • 45
    • 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
  • 46
    • 0032567108 scopus 로고    scopus 로고
    • Complex formation and functional versatility of Mre11 of budding yeast in recombination
    • Usui T., Ohta T., Oshiumi H., Tomizawa J., Ogawa H., and Ogawa T. Complex formation and functional versatility of Mre11 of budding yeast in recombination. Cell 95 (1998) 705-716
    • (1998) Cell , vol.95 , pp. 705-716
    • Usui, T.1    Ohta, T.2    Oshiumi, H.3    Tomizawa, J.4    Ogawa, H.5    Ogawa, T.6
  • 47
    • 39149101784 scopus 로고    scopus 로고
    • Archaeal DNA helicase HerA interacts with Mre11 homologue and unwinds blunt-ended double-stranded DNA and recombination intermediates
    • Zhang S., Wei T., Hou G., Zhang C., Liang P., Ni J., Sheng D., and Shen Y. Archaeal DNA helicase HerA interacts with Mre11 homologue and unwinds blunt-ended double-stranded DNA and recombination intermediates. DNA Repair (Amst.) 7 (2008) 380-391
    • (2008) DNA Repair (Amst.) , vol.7 , pp. 380-391
    • Zhang, S.1    Wei, T.2    Hou, G.3    Zhang, C.4    Liang, P.5    Ni, J.6    Sheng, D.7    Shen, Y.8
  • 48
    • 51549095956 scopus 로고    scopus 로고
    • Sgs1 helicase and two nucleases Dna2 and Exo1 resect DNA double-strand break ends
    • Zhu Z., Chung W.H., Shim E.Y., Lee S.E., and Ira G. 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    Chung, W.H.2    Shim, E.Y.3    Lee, S.E.4    Ira, G.5
  • 49
    • 46949098616 scopus 로고    scopus 로고
    • Break dosage, cell cycle stage and DNA replication influence DNA double strand break response
    • Zierhut C., and Diffley J.F. Break dosage, cell cycle stage and DNA replication influence DNA double strand break response. EMBO J. 27 (2008) 1875-1885
    • (2008) EMBO J. , vol.27 , pp. 1875-1885
    • Zierhut, C.1    Diffley, J.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.