메뉴 건너뛰기




Volumn 26, Issue 2, 2012, Pages 151-162

SMARCAL1 catalyzes fork regression and holliday junction migration to maintain genome stability during DNA replication

Author keywords

DNA repair; Fork reversal; HARP; Holliday junction; SAXS; SIOD

Indexed keywords

ADENOSINE TRIPHOSPHATASE; NUCLEAR MATRIX PROTEIN; PROTEIN SWI; SINGLE STRANDED DNA; TRANSCRIPTION FACTOR SNF;

EID: 84856246154     PISSN: 08909369     EISSN: 15495477     Source Type: Journal    
DOI: 10.1101/gad.178459.111     Document Type: Article
Times cited : (227)

References (43)
  • 1
    • 80052159311 scopus 로고    scopus 로고
    • Coordinated protein and DNA remodeling by human HLTF on stalled replication fork
    • Achar YJ, Balogh D, Haracska L. 2011. Coordinated protein and DNA remodeling by human HLTF on stalled replication fork. Proc Natl Acad Sci 108: 14073-14078
    • (2011) Proc Natl Acad Sci , vol.108 , pp. 14073-14078
    • Achar, Y.J.1    Balogh, D.2    Haracska, L.3
  • 2
    • 67649862225 scopus 로고    scopus 로고
    • Replication fork reversal and the maintenance of genome stability
    • Atkinson J, McGlynn P. 2009. Replication fork reversal and the maintenance of genome stability. Nucleic Acids Res 37: 3475-3492
    • (2009) Nucleic Acids Res , vol.37 , pp. 3475-3492
    • Atkinson, J.1    McGlynn, P.2
  • 3
    • 70350111290 scopus 로고    scopus 로고
    • The annealing helicase SMARCAL1 maintains genome integrity at stalled replication forks
    • Bansbach CE, Betous R, Lovejoy CA, Glick GG, Cortez D. 2009. The annealing helicase SMARCAL1 maintains genome integrity at stalled replication forks. Genes Dev 23: 2405-2414
    • (2009) Genes Dev , vol.23 , pp. 2405-2414
    • Bansbach, C.E.1    Betous, R.2    Lovejoy, C.A.3    Glick, G.G.4    Cortez, D.5
  • 4
    • 77957686153 scopus 로고    scopus 로고
    • SMARCAL1 and replication stress: An explanation for SIOD?
    • Bansbach CE, Boerkoel CF, Cortez D. 2010. SMARCAL1 and replication stress: An explanation for SIOD? Nucleus 1: 245-248.
    • (2010) Nucleus , vol.1 , pp. 245-248
    • Bansbach, C.E.1    Boerkoel, C.F.2    Cortez, D.3
  • 5
    • 35148847451 scopus 로고    scopus 로고
    • Yeast Rad5 protein required for postreplication repair has a DNA helicase activity specific for replication fork regression
    • Blastyak A, Pinter L, Unk I, Prakash L, Prakash S, Haracska L. 2007. Yeast Rad5 protein required for postreplication repair has a DNA helicase activity specific for replication fork regression. Mol Cell 28: 167-175
    • (2007) Mol Cell , vol.28 , pp. 167-175
    • Blastyak, A.1    Pinter, L.2    Unk, I.3    Prakash, L.4    Prakash, S.5    Haracska, L.6
  • 8
    • 33746715608 scopus 로고    scopus 로고
    • Rad54 protein promotes branch migration of Holliday junctions
    • Bugreev DV, Mazina OM, Mazin AV. 2006. Rad54 protein promotes branch migration of Holliday junctions. Nature 442: 590-593
    • (2006) Nature , vol.442 , pp. 590-593
    • Bugreev, D.V.1    Mazina, O.M.2    Mazin, A.V.3
  • 10
    • 0034231844 scopus 로고    scopus 로고
    • Werner's syndrome protein (WRN) migrates Holliday junctions and co-localizes with RPA upon replication arrest
    • Constantinou A, Tarsounas M, Karow JK, Brosh RM, Bohr VA, Hickson ID, West SC. 2000. Werner's syndrome protein (WRN) migrates Holliday junctions and co-localizes with RPA upon replication arrest. EMBO Rep 1: 80-84
    • (2000) EMBO Rep , vol.1 , pp. 80-84
    • Constantinou, A.1    Tarsounas, M.2    Karow, J.K.3    Brosh, R.M.4    Bohr, V.A.5    Hickson, I.D.6    West, S.C.7
  • 11
    • 70350124025 scopus 로고    scopus 로고
    • HARPing on about the DNA damage response during replication
    • Driscoll R, Cimprich KA. 2009. HARPing on about the DNA damage response during replication. Genes Dev 23: 2359-2365
    • (2009) Genes Dev , vol.23 , pp. 2359-2365
    • Driscoll, R.1    Cimprich, K.A.2
  • 12
    • 18844457346 scopus 로고    scopus 로고
    • X-ray structures of the Sulfolobus solfataricus SWI2/SNF2 ATPase core and its complex with DNA
    • Durr H, Korner C, Muller M, Hickmann V, Hopfner KP. 2005. X-ray structures of the Sulfolobus solfataricus SWI2/SNF2 ATPase core and its complex with DNA. Cell 121: 363-373
    • (2005) Cell , vol.121 , pp. 363-373
    • Durr, H.1    Korner, C.2    Muller, M.3    Hickmann, V.4    Hopfner, K.P.5
  • 13
    • 33745122231 scopus 로고    scopus 로고
    • Identification of multiple distinct Snf2 subfamilies with conserved structural motifs
    • Flaus A, Martin DM, Barton GJ, Owen-Hughes T. 2006. Identification of multiple distinct Snf2 subfamilies with conserved structural motifs. Nucleic Acids Res 34: 2887-2905
    • (2006) Nucleic Acids Res , vol.34 , pp. 2887-2905
    • Flaus, A.1    Martin, D.M.2    Barton, G.J.3    Owen-Hughes, T.4
  • 14
    • 55949108120 scopus 로고    scopus 로고
    • Replication fork stalling in WRN-deficient cells is overcome by prompt activation of a MUS81-dependent pathway
    • Franchitto A, Pirzio LM, Prosperi E, Sapora O, Bignami M, Pichierri P. 2008. Replication fork stalling in WRN-deficient cells is overcome by prompt activation of a MUS81-dependent pathway. J Cell Biol 183: 241-252
    • (2008) J Cell Biol , vol.183 , pp. 241-252
    • Franchitto, A.1    Pirzio, L.M.2    Prosperi, E.3    Sapora, O.4    Bignami, M.5    Pichierri, P.6
  • 15
    • 55849133052 scopus 로고    scopus 로고
    • Remodeling of DNA replication structures by the branch point translocase FANCM
    • Gari K, Decaillet C, Delannoy M, Wu L, Constantinou A. 2008a. Remodeling of DNA replication structures by the branch point translocase FANCM. Proc Natl Acad Sci 105: 16107-16112
    • (2008) Proc Natl Acad Sci , vol.105 , pp. 16107-16112
    • Gari, K.1    Decaillet, C.2    Delannoy, M.3    Wu, L.4    Constantinou, A.5
  • 16
    • 38349050087 scopus 로고    scopus 로고
    • The Fanconi anemia protein FANCM can promote branch migration of Holliday junctions and replication forks
    • Gari K, Decaillet C, Stasiak AZ, Stasiak A, Constantinou A. 2008b. The Fanconi anemia protein FANCM can promote branch migration of Holliday junctions and replication forks. Mol Cell 29: 141-148
    • (2008) Mol Cell , vol.29 , pp. 141-148
    • Gari, K.1    Decaillet, C.2    Stasiak, A.Z.3    Stasiak, A.4    Constantinou, A.5
  • 17
    • 79957996057 scopus 로고    scopus 로고
    • The HARP domain dictates the annealing helicase activity of HARP/SMARCAL1
    • Ghosal G, Yuan J, Chen J. 2011. The HARP domain dictates the annealing helicase activity of HARP/SMARCAL1. EMBO Rep 12: 574-580
    • (2011) EMBO Rep , vol.12 , pp. 574-580
    • Ghosal, G.1    Yuan, J.2    Chen, J.3
  • 18
    • 73249115808 scopus 로고    scopus 로고
    • X-ray structure of Pur-a reveals a Whirly-like fold and an unusual nucleic-acid binding surface
    • Graebsch A, Roche S, Niessing D. 2009. X-ray structure of Pur-a reveals a Whirly-like fold and an unusual nucleic-acid binding surface. Proc Natl Acad Sci 106: 18521-18526
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 18521-18526
    • Graebsch, A.1    Roche, S.2    Niessing, D.3
  • 21
    • 41849142342 scopus 로고    scopus 로고
    • Conformational changes of a Swi2/Snf2 ATPase during its mechano-chemical cycle
    • Lewis R, Durr H, Hopfner KP, Michaelis J. 2008. Conformational changes of a Swi2/Snf2 ATPase during its mechano-chemical cycle. Nucleic Acids Res 36: 1881-1890
    • (2008) Nucleic Acids Res , vol.36 , pp. 1881-1890
    • Lewis, R.1    Durr, H.2    Hopfner, K.P.3    Michaelis, J.4
  • 23
    • 0034678127 scopus 로고    scopus 로고
    • A eukaryotic SWI2/SNF2 domain, an exquisite detector of double-stranded to single-stranded DNA transition elements
    • Muthuswami R, Truman PA, Mesner LD, Hockensmith JW. 2000. A eukaryotic SWI2/SNF2 domain, an exquisite detector of double-stranded to single-stranded DNA transition elements. J Biol Chem 275: 7648-7655
    • (2000) J Biol Chem , vol.275 , pp. 7648-7655
    • Muthuswami, R.1    Truman, P.A.2    Mesner, L.D.3    Hockensmith, J.W.4
  • 24
    • 62849091779 scopus 로고    scopus 로고
    • The Werner syndrome helicase/exonuclease processes mobile D-loops through branch migration and degradation
    • doi: 10.1371/journal.pone.0004825
    • Opresko PL, Sowd G, Wang H. 2009. The Werner syndrome helicase/exonuclease processes mobile D-loops through branch migration and degradation. PLoS ONE 4: e4825. doi: 10.1371/journal.pone.0004825.
    • (2009) PLoS ONE , vol.e4825 , pp. 4
    • Opresko, P.L.1    Sowd, G.2    Wang, H.3
  • 25
    • 34249942213 scopus 로고    scopus 로고
    • Exploring the roles of Mus81-Eme1/Mms4 at perturbed replication forks
    • Osman F, Whitby MC. 2007. Exploring the roles of Mus81-Eme1/Mms4 at perturbed replication forks. DNA Repair (Amst) 6: 1004-1017
    • (2007) DNA Repair (Amst) , vol.6 , pp. 1004-1017
    • Osman, F.1    Whitby, M.C.2
  • 26
    • 77957123627 scopus 로고    scopus 로고
    • Pathways of mammalian replication fork restart
    • Petermann E, Helleday T. 2010. Pathways of mammalian replication fork restart. Nat Rev Mol Cell Biol 11: 683-687
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 683-687
    • Petermann, E.1    Helleday, T.2
  • 27
    • 76849109722 scopus 로고    scopus 로고
    • Hydroxyurea-stalled replication forks become progressively inactivated and require two different RAD51-mediated pathways for restart and repair
    • Petermann E, Orta ML, Issaeva N, Schultz N, Helleday T. 2010. Hydroxyurea-stalled replication forks become progressively inactivated and require two different RAD51-mediated pathways for restart and repair. Mol Cell 37: 492-502
    • (2010) Mol Cell , vol.37 , pp. 492-502
    • Petermann, E.1    Orta, M.L.2    Issaeva, N.3    Schultz, N.4    Helleday, T.5
  • 28
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modeling of macromolecular complexes against small-angle scattering data
    • Petoukhov MV, Svergun DI. 2005. Global rigid body modeling of macromolecular complexes against small-angle scattering data. Biophys J 89: 1237-1250
    • (2005) Biophys J , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 29
    • 72149132821 scopus 로고    scopus 로고
    • Identification of SMARCAL1 as a component of the DNA damage response
    • Postow L, Woo EM, Chait BT, Funabiki H. 2009. Identification of SMARCAL1 as a component of the DNA damage response. J Biol Chem284: 35951-35961
    • (2009) J Biol Chem284 , pp. 35951-35961
    • Postow, L.1    Woo, E.M.2    Chait, B.T.3    Funabiki, H.4
  • 30
    • 37149049312 scopus 로고    scopus 로고
    • X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution
    • Putnam CD, Hammel M, Hura GL, Tainer JA. 2007. X-ray solution scattering (SAXS) combined with crystallography and computation: Defining accurate macromolecular structures, conformations and assemblies in solution. Q Rev Biophys 40: 191-285
    • (2007) Q Rev Biophys , vol.40 , pp. 191-285
    • Putnam, C.D.1    Hammel, M.2    Hura, G.L.3    Tainer, J.A.4
  • 31
    • 33747352774 scopus 로고    scopus 로고
    • The Bloom's syndrome helicase can promote the regression of a model replication fork
    • Ralf C, Hickson ID, Wu L. 2006. The Bloom's syndrome helicase can promote the regression of a model replication fork. J Biol Chem 281: 22839-22846
    • (2006) J Biol Chem , vol.281 , pp. 22839-22846
    • Ralf, C.1    Hickson, I.D.2    Wu, L.3
  • 32
    • 77749311718 scopus 로고    scopus 로고
    • Bridging the solution divide: Comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering
    • Rambo RP, Tainer JA. 2010. Bridging the solution divide: Comprehensive structural analyses of dynamic RNA, DNA, and protein assemblies by small-angle X-ray scattering. Curr Opin Struct Biol 20: 128-137
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 128-137
    • Rambo, R.P.1    Tainer, J.A.2
  • 33
    • 79958045453 scopus 로고    scopus 로고
    • Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law
    • Rambo RP, Tainer JA. 2011. Characterizing flexible and intrinsically unstructured biological macromolecules by SAS using the Porod-Debye law. Biopolymers 95: 559-571
    • (2011) Biopolymers , vol.95 , pp. 559-571
    • Rambo, R.P.1    Tainer, J.A.2
  • 34
    • 0035967880 scopus 로고    scopus 로고
    • FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties
    • Shi J, Blundell TL, Mizuguchi K. 2001. FUGUE: Sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties. J Mol Biol 310: 243-257
    • (2001) J Mol Biol , vol.310 , pp. 243-257
    • Shi, J.1    Blundell, T.L.2    Mizuguchi, K.3
  • 36
    • 3242875210 scopus 로고    scopus 로고
    • ElNemo: A normal mode Web server for protein movement analysis and the generation of templates for molecular replacement
    • doi: 10.1093/nar/gkh368
    • Suhre K, Sanejouand YH. 2004. ElNemo: A normal mode Web server for protein movement analysis and the generation of templates for molecular replacement. Nucleic Acids Res 32: W610-W614. doi: 10.1093/nar/gkh368
    • (2004) Nucleic Acids Res , vol.32
    • Suhre, K.1    Sanejouand, Y.H.2
  • 37
    • 0026910457 scopus 로고
    • Determination of the regularization parameter in indirect-transform methods using perceptual criteria
    • Svergun DI. 1992. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J Appl Crystallogr 25: 495-503
    • (1992) J Appl Crystallogr , vol.25 , pp. 495-503
    • Svergun, D.I.1
  • 39
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • Volkov VV, Svergun DI. 2003. Uniqueness of ab initio shape determination in small-angle scattering. J Appl Crystallogr 36: 860-864
    • (2003) J Appl Crystallogr , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 40
    • 70350118815 scopus 로고    scopus 로고
    • The annealing helicase HARP protects stalled replication forks
    • Yuan J, Ghosal G, Chen J. 2009. The annealing helicase HARP protects stalled replication forks. Genes Dev 23: 2394-2399
    • (2009) Genes Dev , vol.23 , pp. 2394-2399
    • Yuan, J.1    Ghosal, G.2    Chen, J.3
  • 41
    • 55349121223 scopus 로고    scopus 로고
    • HARP is an ATP-driven annealing helicase
    • Yusufzai T, Kadonaga JT. 2008. HARP is an ATP-driven annealing helicase. Science 322: 748-750
    • (2008) Science , vol.322 , pp. 748-750
    • Yusufzai, T.1    Kadonaga, J.T.2
  • 42
    • 78650448305 scopus 로고    scopus 로고
    • Annealing helicase 2 (AH2), a DNA-rewinding motor with an HNH motif
    • Yusufzai T, Kadonaga JT. 2010. Annealing helicase 2 (AH2), a DNA-rewinding motor with an HNH motif. Proc Natl Acad Sci 107: 20970-20973
    • (2010) Proc Natl Acad Sci , vol.107 , pp. 20970-20973
    • Yusufzai, T.1    Kadonaga, J.T.2
  • 43
    • 70350103969 scopus 로고    scopus 로고
    • The annealing helicase HARP is recruited to DNA repair sites via an interaction with RPA
    • Yusufzai T, Kong X, Yokomori K, Kadonaga JT. 2009. The annealing helicase HARP is recruited to DNA repair sites via an interaction with RPA. Genes Dev 23: 2400-2404.
    • (2009) Genes Dev , vol.23 , pp. 2400-2404
    • Yusufzai, T.1    Kong, X.2    Yokomori, K.3    Kadonaga, J.T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.