메뉴 건너뛰기




Volumn 10, Issue 10, 2011, Pages 1066-1070

Mre11-Rad50 complex crystals suggest molecular calisthenics

Author keywords

DNA double strand breaks; DNA repair; Genome maintenance

Indexed keywords

ADENOSINE TRIPHOSPHATE; DOUBLE STRANDED DNA; MRE11 PROTEIN; NIBRIN; NUCLEASE; PROTEIN MUTS; RAD50 PROTEIN;

EID: 80053298982     PISSN: 15687864     EISSN: 15687856     Source Type: Journal    
DOI: 10.1016/j.dnarep.2011.07.008     Document Type: Article
Times cited : (12)

References (33)
  • 1
    • 77955841725 scopus 로고    scopus 로고
    • The MRN complex in double-strand break repair and telomere maintenance
    • Lamarche B.J., Orazio N.I., Weitzman M.D. The MRN complex in double-strand break repair and telomere maintenance. FEBS Lett. 2010, 584:3682-3695.
    • (2010) FEBS Lett. , vol.584 , pp. 3682-3695
    • Lamarche, B.J.1    Orazio, N.I.2    Weitzman, M.D.3
  • 2
    • 78649451417 scopus 로고    scopus 로고
    • Making the best of the loose ends: Mre11/Rad50 complexes and Sae2 promote DNA double-strand break resection
    • Paull T.T. Making the best of the loose ends: Mre11/Rad50 complexes and Sae2 promote DNA double-strand break resection. DNA Repair (Amst.) 2010, 9:1283-1291.
    • (2010) DNA Repair (Amst.) , vol.9 , pp. 1283-1291
    • Paull, T.T.1
  • 5
    • 79956301873 scopus 로고    scopus 로고
    • Crystal structure of the Mre11-Rad50-ATP{gamma}S complex: understanding the interplay between Mre11 and Rad50
    • Lim H.S., Kim J.S., Park Y.B., Gwon G.H., Cho Y. Crystal structure of the Mre11-Rad50-ATP{gamma}S complex: understanding the interplay between Mre11 and Rad50. Genes Dev. 2011, 25:1091-1104.
    • (2011) Genes Dev. , vol.25 , pp. 1091-1104
    • Lim, H.S.1    Kim, J.S.2    Park, Y.B.3    Gwon, G.H.4    Cho, Y.5
  • 7
    • 78649445307 scopus 로고    scopus 로고
    • Mre11-Rad50-Nbs1 conformations and the control of sensing, signaling, and effector responses at DNA double-strand breaks
    • Williams G.J., Lees-Miller S.P., Tainer J.A. Mre11-Rad50-Nbs1 conformations and the control of sensing, signaling, and effector responses at DNA double-strand breaks. DNA Repair (Amst.) 2010, 9:1299-1306.
    • (2010) DNA Repair (Amst.) , vol.9 , pp. 1299-1306
    • Williams, G.J.1    Lees-Miller, S.P.2    Tainer, J.A.3
  • 12
    • 24944540931 scopus 로고    scopus 로고
    • Mesoscale conformational changes in the DNA-repair complex Rad50/Mre11/Nbs1 upon binding DNA
    • Moreno-Herrero F., de Jager M., Dekker N.H., Kanaar R., Wyman C., Dekker C. Mesoscale conformational changes in the DNA-repair complex Rad50/Mre11/Nbs1 upon binding DNA. Nature 2005, 437:440-443.
    • (2005) Nature , vol.437 , pp. 440-443
    • Moreno-Herrero, F.1    de Jager, M.2    Dekker, N.H.3    Kanaar, R.4    Wyman, C.5    Dekker, C.6
  • 13
    • 68249116573 scopus 로고    scopus 로고
    • DNA end resection: many nucleases make light work
    • Mimitou E.P., Symington L.S. DNA end resection: many nucleases make light work. DNA Repair (Amst.) 2009, 8:983-995.
    • (2009) DNA Repair (Amst.) , vol.8 , pp. 983-995
    • Mimitou, E.P.1    Symington, L.S.2
  • 14
    • 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., Tainer J.A. Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase. Cell 2001, 105:473-485.
    • (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
  • 15
    • 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., Tainer J.A. Structural biology of Rad50 ATPase: ATP-driven conformational control in DNA double-strand break repair and the ABC-ATPase superfamily. Cell 2000, 101:789-800.
    • (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
  • 16
    • 52949087621 scopus 로고    scopus 로고
    • DNA repair by the MRN complex: break it to make it
    • Kanaar R., Wyman C. DNA repair by the MRN complex: break it to make it. Cell 2008, 135:14-16.
    • (2008) Cell , vol.135 , pp. 14-16
    • Kanaar, R.1    Wyman, C.2
  • 18
    • 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., Kleckner N. Analysis of wild-type and rad50 mutants of yeast suggests an intimate relationship between meiotic chromosome synapsis and recombination. Cell 1990, 61:419-436.
    • (1990) Cell , vol.61 , pp. 419-436
    • Alani, E.1    Padmore, R.2    Kleckner, N.3
  • 19
    • 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., Sung P. Nuclease activities in a complex of human recombination and DNA repair factors Rad50, Mre11, and p95. J. Biol. Chem. 1998, 273:21447-21450.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21447-21450
    • Trujillo, K.M.1    Yuan, S.S.2    Lee, E.Y.3    Sung, P.4
  • 20
    • 33846945734 scopus 로고    scopus 로고
    • Structural conservation of RecF and Rad50: implications for DNA recognition and RecF function
    • Koroleva O., Makharashvili N., Courcelle C.T., Courcelle J., Korolev S. Structural conservation of RecF and Rad50: implications for DNA recognition and RecF function. EMBO J. 2007, 26:867-877.
    • (2007) EMBO J. , vol.26 , pp. 867-877
    • Koroleva, O.1    Makharashvili, N.2    Courcelle, C.T.3    Courcelle, J.4    Korolev, S.5
  • 21
    • 4644220369 scopus 로고    scopus 로고
    • Structural biochemistry of ATP-driven dimerization and DNA-stimulated activation of SMC ATPases
    • Lammens A., Schele A., Hopfner K.P. Structural biochemistry of ATP-driven dimerization and DNA-stimulated activation of SMC ATPases. Curr. Biol. 2004, 14:1778-1782.
    • (2004) Curr. Biol. , vol.14 , pp. 1778-1782
    • Lammens, A.1    Schele, A.2    Hopfner, K.P.3
  • 23
    • 0033563229 scopus 로고    scopus 로고
    • Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex
    • Paull T.T., Gellert M. Nbs1 potentiates ATP-driven DNA unwinding and endonuclease cleavage by the Mre11/Rad50 complex. Genes Dev. 1999, 13:1276-1288.
    • (1999) Genes Dev. , vol.13 , pp. 1276-1288
    • Paull, T.T.1    Gellert, M.2
  • 24
    • 0035929667 scopus 로고    scopus 로고
    • DNA structure-specific nuclease activities in the Saccharomyces cerevisiae Rad50*Mre11 complex
    • Trujillo K.M., Sung P. DNA structure-specific nuclease activities in the Saccharomyces cerevisiae Rad50*Mre11 complex. J. Biol. Chem. 2001, 276:35458-35464.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35458-35464
    • Trujillo, K.M.1    Sung, P.2
  • 25
    • 0037109113 scopus 로고    scopus 로고
    • DNA end-binding specificity of human Rad50/Mre11 is influenced by ATP
    • de Jager M., Wyman C., van Gent D.C., Kanaar R. DNA end-binding specificity of human Rad50/Mre11 is influenced by ATP. Nucleic Acids Res. 2002, 30:4425-4431.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4425-4431
    • de Jager, M.1    Wyman, C.2    van Gent, D.C.3    Kanaar, R.4
  • 27
    • 0034641947 scopus 로고    scopus 로고
    • The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch
    • Lamers M.H., Perrakis A., Enzlin J.H., Winterwerp H.H., de Wind N., Sixma T.K. The crystal structure of DNA mismatch repair protein MutS binding to a G x T mismatch. Nature 2000, 407:711-717.
    • (2000) Nature , vol.407 , pp. 711-717
    • Lamers, M.H.1    Perrakis, A.2    Enzlin, J.H.3    Winterwerp, H.H.4    de Wind, N.5    Sixma, T.K.6
  • 28
    • 0034641938 scopus 로고    scopus 로고
    • Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA
    • Obmolova G., Ban C., Hsieh P., Yang W. Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA. Nature 2000, 407:703-710.
    • (2000) Nature , vol.407 , pp. 703-710
    • Obmolova, G.1    Ban, C.2    Hsieh, P.3    Yang, W.4
  • 29
    • 0037415693 scopus 로고    scopus 로고
    • The alternating ATPase domains of MutS control DNA mismatch repair
    • Lamers M.H., Winterwerp H.H., Sixma T.K. The alternating ATPase domains of MutS control DNA mismatch repair. EMBO J. 2003, 22:746-756.
    • (2003) EMBO J. , vol.22 , pp. 746-756
    • Lamers, M.H.1    Winterwerp, H.H.2    Sixma, T.K.3
  • 32
    • 0035869155 scopus 로고    scopus 로고
    • DNA-binding and strand-annealing activities of human Mre11: implications for its roles in DNA double-strand break repair pathways
    • de Jager M., Dronkert M.L., Modesti M., Beerens C.E., Kanaar R., van Gent D.C. DNA-binding and strand-annealing activities of human Mre11: implications for its roles in DNA double-strand break repair pathways. Nucleic Acids Res. 2001, 29:1317-1325.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1317-1325
    • de Jager, M.1    Dronkert, M.L.2    Modesti, M.3    Beerens, C.E.4    Kanaar, R.5    van Gent, D.C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.