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Volumn 287, Issue 2, 2012, Pages 1007-1021

Biochemical characterization of Warsaw breakage syndrome helicase

Author keywords

[No Author keywords available]

Indexed keywords

ADHESION; AMINO ACIDS; DEFECTS; DNA; RECOMBINANT PROTEINS; SUBSTRATES;

EID: 84862908251     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.276022     Document Type: Article
Times cited : (89)

References (44)
  • 1
    • 63449109208 scopus 로고    scopus 로고
    • Welcome the family of FANCJ-like helicases to the block of genome stability maintenance proteins
    • Wu, Y., Suhasini, A. N., and Brosh, R. M., Jr. (2009) Welcome the family of FANCJ-like helicases to the block of genome stability maintenance proteins. Cell. Mol. Life Sci. 66, 1209-1222
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1209-1222
    • Wu, Y.1    Suhasini, A.N.2    Brosh Jr., R.M.3
  • 2
    • 0035176067 scopus 로고    scopus 로고
    • The xeroderma pigmentosum group D (XPD) gene: One gene, two functions, three diseases
    • Lehmann, A. R. (2001) The xeroderma pigmentosum group D (XPD) gene: one gene, two functions, three diseases. Genes Dev. 15, 15-23
    • (2001) Genes Dev. , vol.15 , pp. 15-23
    • Lehmann, A.R.1
  • 5
    • 24944575242 scopus 로고    scopus 로고
    • BACH1 is critical for homologous recombination and appears to be the Fanconi anemia gene product FANCJ
    • DOI 10.1016/j.ccr.2005.08.004, PII S153561080500262X
    • Litman, R., Peng, M., Jin, Z., Zhang, F., Zhang, J., Powell, S., Andreassen, P. R., and Cantor, S. B. (2005) BACH1 is critical for homologous recombination and appears to be the Fanconi anemia gene product FANCJ. Cancer Cell 8, 255-265 (Pubitemid 41317595)
    • (2005) Cancer Cell , vol.8 , Issue.3 , pp. 255-265
    • Litman, R.1    Peng, M.2    Jin, Z.3    Zhang, F.4    Zhang, J.5    Powell, S.6    Andreassen, P.R.7    Cantor, S.B.8
  • 7
    • 0036699095 scopus 로고    scopus 로고
    • Disruption of dog-1 in Caenorhabditis elegans triggers deletions upstream of guanine-rich DNA
    • DOI 10.1038/ng928
    • Cheung, I., Schertzer, M., Rose, A., and Lansdorp, P. M. (2002) Disruption of dog-1 in Caenorhabditis elegans triggers deletions upstream of guanine- rich DNA. Nat. Genet. 31, 405-409 (Pubitemid 35154451)
    • (2002) Nature Genetics , vol.31 , Issue.4 , pp. 405-409
    • Cheung, I.1    Schertzer, M.2    Rose, A.3    Lansdorp, P.M.4
  • 8
    • 33749136403 scopus 로고    scopus 로고
    • Roles of Pif1-like helicases in the maintenance of genomic stability
    • Boulé, J. B., and Zakian, V. A. (2006) Roles of Pif1-like helicases in the maintenance of genomic stability. Nucleic Acids Res. 34, 4147-4153
    • (2006) Nucleic Acids Res. , vol.34 , pp. 4147-4153
    • Boulé, J.B.1    Zakian, V.A.2
  • 10
    • 79957556530 scopus 로고    scopus 로고
    • DNA replication through G-quadruplex motifs is promoted by the Saccharomyces cerevisiae Pif1 DNA helicase
    • Paeschke, K., Capra, J. A., and Zakian, V. A. (2011) DNA replication through G-quadruplex motifs is promoted by the Saccharomyces cerevisiae Pif1 DNA helicase. Cell 145, 678-691
    • (2011) Cell , vol.145 , pp. 678-691
    • Paeschke, K.1    Capra, J.A.2    Zakian, V.A.3
  • 11
    • 78649705898 scopus 로고    scopus 로고
    • Pif1- and Exo1-dependent nucleases coordinate checkpoint activation following telomere uncapping
    • Dewar, J. M., and Lydall, D. (2010) Pif1- and Exo1-dependent nucleases coordinate checkpoint activation following telomere uncapping. EMBO J. 29, 4020-4034
    • (2010) EMBO J. , vol.29 , pp. 4020-4034
    • Dewar, J.M.1    Lydall, D.2
  • 13
    • 1642360837 scopus 로고    scopus 로고
    • Chl1p, a DNA helicase-like protein in budding yeast, functions in sister-chromatid cohesion
    • Skibbens, R. V. (2004) Chl1p, a DNA helicase-like protein in budding yeast, functions in sister-chromatid cohesion. Genetics 166, 33-42
    • (2004) Genetics , vol.166 , pp. 33-42
    • Skibbens, R.V.1
  • 14
    • 4444292553 scopus 로고    scopus 로고
    • Sister-chromatid cohesion mediated by the alternative RF-CCtf18/Dcc1/ Ctf8, the helicase Chl1 and the polymerase-alpha-associated protein Ctf4 is essential for chromatid disjunction during meiosis II
    • Petronczki, M., Chwalla, B., Siomos, M. F., Yokobayashi, S., Helmhart, W., Deutschbauer, A. M., Davis, R. W., Watanabe, Y., and Nasmyth, K. (2004) Sister-chromatid cohesion mediated by the alternative RF-CCtf18/Dcc1/ Ctf8, the helicase Chl1 and the polymerase-alpha-associated protein Ctf4 is essential for chromatid disjunction during meiosis II. J. Cell Sci. 117, 3547-3559
    • (2004) J. Cell Sci. , vol.117 , pp. 3547-3559
    • Petronczki, M.1    Chwalla, B.2    Siomos, M.F.3    Yokobayashi, S.4    Helmhart, W.5    Deutschbauer, A.M.6    Davis, R.W.7    Watanabe, Y.8    Nasmyth, K.9
  • 15
    • 39449099352 scopus 로고    scopus 로고
    • Ctf18 and the Swi1-Swi3 complex function in separate and redundant pathways required for the stabilization of replication forks to facilitate sister chromatid cohesion in Schizosaccharomyces pombe
    • DOI 10.1091/mbc.E07-06-0618
    • Ansbach, A. B., Noguchi, C., Klansek, I. W., Heidlebaugh, M., Nakamura, T. M., and Noguchi, E. (2008) RFCCtf18 and the Swi1-Swi3 complex function in separate and redundant pathways required for the stabilization of replication forks to facilitate sister chromatid cohesion in Schizosaccharomyces pombe. Mol. Biol. Cell 19, 595-607 (Pubitemid 351272148)
    • (2008) Molecular Biology of the Cell , vol.19 , Issue.2 , pp. 595-607
    • Ansbach, A.B.1    Noguchi, C.2    Klansek, I.W.3    Heidlebaugh, M.4    Nakamura, T.M.5    Noguchi, E.6
  • 17
    • 33845657930 scopus 로고    scopus 로고
    • The DNA helicase ChlR1 is required for sister chromatid cohesion in mammalian cells
    • DOI 10.1242/jcs.03262
    • Parish, J. L., Rosa, J., Wang, X., Lahti, J. M., Doxsey, S. J., and Androphy, E. J. (2006) The DNA helicase ChlR1 is required for sister chromatid cohesion in mammalian cells. J. Cell Sci. 119, 4857-4865 (Pubitemid 46017799)
    • (2006) Journal of Cell Science , vol.119 , Issue.23 , pp. 4857-4865
    • Parish, J.L.1    Rosa, J.2    Wang, X.3    Lahti, J.M.4    Doxsey, S.J.5    Androphy, E.J.6
  • 18
    • 34548251989 scopus 로고    scopus 로고
    • Loss of ChlR1 helicase in mouse causes lethality due to the accumulation of aneuploid cells generated by cohesion defects and placental malformation
    • Inoue, A., Li, T., Roby, S. K., Valentine, M. B., Inoue, M., Boyd, K., Kidd, V. J., and Lahti, J. M. (2007) Loss of ChlR1 helicase in mouse causes lethality due to the accumulation of aneuploid cells generated by cohesion defects and placental malformation. Cell Cycle 6, 1646-1654 (Pubitemid 47327952)
    • (2007) Cell Cycle , vol.6 , Issue.13 , pp. 1646-1654
    • Inoue, A.1    Li, T.2    Roby, S.K.3    Valentine, M.B.4    Inoue, M.5    Boyd, K.6    Kidd, V.J.7    Lahti, J.M.8
  • 19
    • 33845629295 scopus 로고    scopus 로고
    • ChlR1 Is Required for Loading Papillomavirus E2 onto Mitotic Chromosomes and Viral Genome Maintenance
    • DOI 10.1016/j.molcel.2006.11.005, PII S1097276506007465
    • Parish, J. L., Bean, A. M., Park, R. B., and Androphy, E. J. (2006) ChlR1 is required for loading papillomavirus E2 onto mitotic chromosomes and viral genome maintenance. Mol. Cell 24, 867-876 (Pubitemid 44960091)
    • (2006) Molecular Cell , vol.24 , Issue.6 , pp. 867-876
    • Parish, J.L.1    Bean, A.M.2    Park, R.B.3    Androphy, E.J.4
  • 20
    • 0034651623 scopus 로고    scopus 로고
    • Characterization of the enzymatic activity of hChlR1, a novel human DNA helicase
    • Hirota, Y., and Lahti, J. M. (2000) Characterization of the enzymatic activity of hChlR1, a novel human DNA helicase. Nucleic Acids Res. 28, 917-924 (Pubitemid 30085317)
    • (2000) Nucleic Acids Research , vol.28 , Issue.4 , pp. 917-924
    • Hirota, Y.1    Lahti, J.M.2
  • 21
    • 51049121966 scopus 로고    scopus 로고
    • Studies with the human cohesin establishment factor, ChlR1. Association of ChlR1 with Ctf18-RFC and Fen1
    • Farina, A., Shin, J. H., Kim, D. H., Bermudez, V. P., Kelman, Z., Seo, Y. S., and Hurwitz, J. (2008) Studies with the human cohesin establishment factor, ChlR1. Association of ChlR1 with Ctf18-RFC and Fen1. J. Biol. Chem. 283, 20925-20936
    • (2008) J. Biol. Chem. , vol.283 , pp. 20925-20936
    • Farina, A.1    Shin, J.H.2    Kim, D.H.3    Bermudez, V.P.4    Kelman, Z.5    Seo, Y.S.6    Hurwitz, J.7
  • 22
    • 77149171759 scopus 로고    scopus 로고
    • Human Timeless and Tipin stabilize replication forks and facilitate sister-chromatid cohesion
    • Leman, A. R., Noguchi, C., Lee, C. Y., and Noguchi, E. (2010) Human Timeless and Tipin stabilize replication forks and facilitate sister-chromatid cohesion. J. Cell Sci. 123, 660-670
    • (2010) J. Cell Sci. , vol.123 , pp. 660-670
    • Leman, A.R.1    Noguchi, C.2    Lee, C.Y.3    Noguchi, E.4
  • 23
    • 21844445309 scopus 로고    scopus 로고
    • Analysis of the DNA substrate specificity of the human BACH1 helicase associated with breast cancer
    • DOI 10.1074/jbc.M501995200
    • Gupta, R., Sharma, S., Sommers, J. A., Jin, Z., Cantor, S. B., and Brosh, R. M., Jr. (2005) Analysis of the DNA substrate specificity of the human BACH1 helicase associated with breast cancer. J. Biol. Chem. 280, 25450-25460 (Pubitemid 40962249)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.27 , pp. 25450-25460
    • Gupta, R.1    Sharma, S.2    Sommers, J.A.3    Jin, Z.4    Cantor, S.B.5    Brosh Jr., R.M.6
  • 24
    • 0037189485 scopus 로고    scopus 로고
    • Biochemical characterization of the DNA substrate specificity of Werner syndrome helicase
    • DOI 10.1074/jbc.M111446200
    • Brosh, R. M., Jr., Waheed, J., and Sommers, J. A. (2002) Biochemical characterization of the DNA substrate specificity of Werner syndrome helicase. J. Biol. Chem. 277, 23236-23245 (Pubitemid 34952151)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.26 , pp. 23236-23245
    • Brosh Jr., R.M.1    Waheed, J.2    Sommers, J.A.3
  • 25
    • 0035393720 scopus 로고    scopus 로고
    • The Bloom's and Werner's syndrome proteins are DNA structure-specific helicases
    • Mohaghegh, P., Karow, J. K., Brosh, R. M., Jr., Bohr, V. A., and Hickson, I. D. (2001) The Bloom's and Werner's syndrome proteins are DNA structure- specific helicases. Nucleic Acids Res. 29, 2843-2849 (Pubitemid 32685049)
    • (2001) Nucleic Acids Research , vol.29 , Issue.13 , pp. 2843-2849
    • Mohaghegh, P.1    Karow, J.K.2    Brosh Jr., R.M.3    Bohr, V.A.4    Hickson, I.D.5
  • 27
    • 0032538453 scopus 로고    scopus 로고
    • The Bloom's syndrome helicase unwinds G4 DNA
    • DOI 10.1074/jbc.273.42.27587
    • Sun, H., Karow, J. K., Hickson, I. D., and Maizels, N. (1998) The Bloom's syndrome helicase unwinds G4 DNA. J. Biol. Chem. 273, 27587-27592 (Pubitemid 28500481)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.42 , pp. 27587-27592
    • Sun, H.1    Karow, J.K.2    Hickson, I.D.3    Maizels, N.4
  • 28
    • 0037337379 scopus 로고    scopus 로고
    • Analysis of helicase activity and substrate specificity of Drosophila RECQ5
    • DOI 10.1093/nar/gkg243
    • Ozsoy, A. Z., Ragonese, H. M., and Matson, S. W. (2003) Analysis of helicase activity and substrate specificity of Drosophila RECQ5. Nucleic Acids Res. 31, 1554-1564 (Pubitemid 36304917)
    • (2003) Nucleic Acids Research , vol.31 , Issue.5 , pp. 1554-1564
    • Ozsoy, A.Z.1    Ragonese, H.M.2    Matson, S.W.3
  • 29
    • 0032584598 scopus 로고    scopus 로고
    • Targeting Holliday junctions by the RecG branch migration protein of Escherichia coli
    • DOI 10.1074/jbc.273.31.19729
    • Whitby, M. C., and Lloyd, R. G. (1998) Targeting Holliday junctions by the RecG branch migration protein of Escherichia coli. J. Biol. Chem. 273, 19729-19739 (Pubitemid 28367032)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.31 , pp. 19729-19739
    • Whitby, M.C.1    Lloyd, R.G.2
  • 30
    • 0037008675 scopus 로고    scopus 로고
    • The MER3 DNA helicase catalyzes the unwinding of Holliday junctions
    • DOI 10.1074/jbc.M204165200
    • Nakagawa, T., and Kolodner, R. D. (2002) The MER3 DNA helicase catalyzes the unwinding of Holliday junctions. J. Biol. Chem. 277, 28019-28024 (Pubitemid 34966752)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.31 , pp. 28019-28024
    • Nakagawa, T.1    Kolodner, R.D.2
  • 31
    • 33748744378 scopus 로고    scopus 로고
    • Mechanisms of RecQ helicases in pathways of DNA metabolism and maintenance of genomic stability
    • DOI 10.1042/BJ20060450
    • Sharma, S., Doherty, K. M., and Brosh, R. M., Jr. (2006) Mechanisms of RecQ helicases in pathways of DNA metabolism and maintenance of genomic stability. Biochem. J. 398, 319-337 (Pubitemid 44453376)
    • (2006) Biochemical Journal , vol.398 , Issue.3 , pp. 319-337
    • Sharma, S.1    Doherty, K.M.2    Brosh Jr., R.M.3
  • 32
    • 65549113446 scopus 로고    scopus 로고
    • FANCJ uses its motor ATPase to destabilize protein-DNA complexes, unwind triplexes, and inhibit RAD51 strand exchange
    • Sommers, J. A., Rawtani, N., Gupta, R., Bugreev, D. V., Mazin, A. V., Cantor, S. B., and Brosh, R. M., Jr. (2009) FANCJ uses its motor ATPase to destabilize protein-DNA complexes, unwind triplexes, and inhibit RAD51 strand exchange. J. Biol. Chem. 284, 7505-7517
    • (2009) J. Biol. Chem. , vol.284 , pp. 7505-7517
    • Sommers, J.A.1    Rawtani, N.2    Gupta, R.3    Bugreev, D.V.4    Mazin, A.V.5    Cantor, S.B.6    Brosh Jr., R.M.7
  • 33
    • 33845352895 scopus 로고    scopus 로고
    • Dynamic roles for G4 DNA in the biology of eukaryotic cells
    • Maizels, N. (2006) Dynamic roles for G4 DNA in the biology of eukaryotic cells. Nat. Struct. Mol. Biol. 13, 1055-1059
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 1055-1059
    • Maizels, N.1
  • 35
    • 44949114282 scopus 로고    scopus 로고
    • FANCJ helicase defective in Fanconia anemia and breast cancer unwinds G-quadruplex DNA to defend genomic stability
    • DOI 10.1128/MCB.02210-07
    • Wu, Y., Shin-ya, K., and Brosh, R. M., Jr. (2008) FANCJ helicase defective in Fanconia anemia and breast cancer unwinds G-quadruplex DNA to defend genomic stability. Mol. Cell Biol. 28, 4116-4128 (Pubitemid 351812995)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.12 , pp. 4116-4128
    • Wu, Y.1    Kazuo, S.-Y.2    Brosh Jr., R.M.3
  • 36
    • 0029908928 scopus 로고    scopus 로고
    • +in DNA quadruplexes is dominated by relative free energies of hydration: A thermodynamic analysis by 1H NMR
    • + in DNA quadruplexes is dominated by relative free energies of hydration: a thermodynamic analysis by 1H NMR. Biochemistry 35, 15383-15390
    • (1996) Biochemistry , vol.35 , pp. 15383-15390
    • Hud, N.V.1    Smith, F.W.2    Anet, F.A.3    Feigon, J.4
  • 37
    • 0033178271 scopus 로고    scopus 로고
    • 4)
    • DOI 10.1093/nar/27.15.3018
    • Schultze, P., Hud, N. V., Smith, F. W., and Feigon, J. (1999) The effect of sodium, potassium and ammonium ions on the conformation of the dimeric quadruplex formed by the Oxytricha nova telomere repeat oligonucleotide d(G(4)T(4)G(4)). Nucleic Acids Res. 27, 3018-3028 (Pubitemid 29355713)
    • (1999) Nucleic Acids Research , vol.27 , Issue.15 , pp. 3018-3028
    • Schultze, P.1    Hud, N.V.2    Smith, F.W.3    Feigon, J.4
  • 38
    • 0026554887 scopus 로고
    • Quadruplex structure of Oxytricha telomeric DNA oligonucleotides
    • Smith, F. W., and Feigon, J. (1992) Quadruplex structure of Oxytricha telomeric DNA oligonucleotides. Nature 356, 164-168
    • (1992) Nature , vol.356 , pp. 164-168
    • Smith, F.W.1    Feigon, J.2
  • 39
    • 0036290781 scopus 로고    scopus 로고
    • Crystal structure of the potassium form of an Oxytricha nova G-quadruplex
    • DOI 10.1016/S0022-2836(02)00428-X
    • Haider, S., Parkinson, G. N., and Neidle, S. (2002) Crystal structure of the potassium form of an Oxytricha nova G-quadruplex. J. Mol. Biol. 320, 189-200 (Pubitemid 34722211)
    • (2002) Journal of Molecular Biology , vol.320 , Issue.2 , pp. 189-200
    • Haider, S.1    Parkinson, G.N.2    Neidle, S.3
  • 40
    • 0035816210 scopus 로고    scopus 로고
    • DNA G-quartets in a 1.86 A resolution structure of an Oxytricha nova telomeric protein-DNA complex
    • DOI 10.1006/jmbi.2001.4766
    • Horvath, M. P., and Schultz, S. C. (2001) DNA G-quartets in a 1.86 resolution structure of an Oxytricha nova telomeric protein-DNA complex. J. Mol. Biol. 310, 367-377 (Pubitemid 32664874)
    • (2001) Journal of Molecular Biology , vol.310 , Issue.2 , pp. 367-377
    • Horvath, M.P.1    Schultz, S.C.2
  • 41
    • 34547133987 scopus 로고    scopus 로고
    • The DinG protein from Escherichia coli is a structure-specific helicase
    • DOI 10.1074/jbc.M700376200
    • Voloshin, O. N., and Camerini-Otero, R. D. (2007) The DinG protein from Escherichia coli is a structure-specific helicase. J. Biol. Chem. 282, 18437-18447 (Pubitemid 47100196)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.25 , pp. 18437-18447
    • Voloshin, O.N.1    Camerini-Otero, R.D.2
  • 42
    • 38349091095 scopus 로고    scopus 로고
    • The iron-containing domain is essential in Rad3 helicases for coupling of ATP hydrolysis to DNA translocation and for targeting the helicase to the single-stranded DNA-doublestranded DNA junction
    • Pugh, R. A., Honda, M., Leesley, H., Thomas, A., Lin, Y., Nilges, M. J., Cann, I. K., and Spies, M. (2008) The iron-containing domain is essential in Rad3 helicases for coupling of ATP hydrolysis to DNA translocation and for targeting the helicase to the single-stranded DNA-doublestranded DNA junction. J. Biol. Chem. 283, 1732-1743
    • (2008) J. Biol. Chem. , vol.283 , pp. 1732-1743
    • Pugh, R.A.1    Honda, M.2    Leesley, H.3    Thomas, A.4    Lin, Y.5    Nilges, M.J.6    Cann, I.K.7    Spies, M.8
  • 43
    • 79955531958 scopus 로고    scopus 로고
    • In vivo analysis of the cell cycle dependent association of the bovine papillomavirus E2 protein and ChlR1
    • Feeney, K. M., Saade, A., Okrasa, K., and Parish, J. L. (2011) In vivo analysis of the cell cycle dependent association of the bovine papillomavirus E2 protein and ChlR1. Virology 414, 1-9
    • (2011) Virology , vol.414 , pp. 1-9
    • Feeney, K.M.1    Saade, A.2    Okrasa, K.3    Parish, J.L.4


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