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Volumn 6, Issue 7, 2007, Pages 936-944

Role of the BLM helicase in replication fork management

Author keywords

BLM; Bloom's syndrome; Holliday junction dissolution; Homologous recombination; RecQ helicases; Replication fork repair; Topoisomerase III

Indexed keywords

DOUBLE STRANDED DNA; GENOMIC DNA; PROTEIN BLM; RECQ HELICASE; UNCLASSIFIED DRUG;

EID: 34249946979     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2007.02.007     Document Type: Article
Times cited : (52)

References (95)
  • 1
    • 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
  • 2
    • 0037364415 scopus 로고    scopus 로고
    • RecQ helicases: caretakers of the genome
    • Hickson I.D. RecQ helicases: caretakers of the genome. Nat. Rev. Cancer 3 (2003) 169-178
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 169-178
    • Hickson, I.D.1
  • 6
    • 0024591985 scopus 로고
    • Bloom's syndrome. XII. Report from the Registry for 1987
    • German J., and Passarge E. Bloom's syndrome. XII. Report from the Registry for 1987. Clin. Genet. 35 (1989) 57-69
    • (1989) Clin. Genet. , vol.35 , pp. 57-69
    • German, J.1    Passarge, E.2
  • 7
    • 0037202592 scopus 로고    scopus 로고
    • RecQ helicases and cellular responses to DNA damage
    • Wu L., and Hickson I.D. RecQ helicases and cellular responses to DNA damage. Mutat. Res. 509 (2002) 35-47
    • (2002) Mutat. Res. , vol.509 , pp. 35-47
    • Wu, L.1    Hickson, I.D.2
  • 8
    • 1642458364 scopus 로고    scopus 로고
    • Phosphorylation of the Bloom's syndrome helicase and its role in recovery from S-phase arrest
    • Davies S.L., North P.S., Dart A., Lakin N.D., and Hickson I.D. Phosphorylation of the Bloom's syndrome helicase and its role in recovery from S-phase arrest. Mol. Cell. Biol. 24 (2004) 1279-1291
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1279-1291
    • Davies, S.L.1    North, P.S.2    Dart, A.3    Lakin, N.D.4    Hickson, I.D.5
  • 9
    • 3142546346 scopus 로고
    • A retarded rate of DNA chain growth in Bloom's syndrome
    • Hand R., and German J. A retarded rate of DNA chain growth in Bloom's syndrome. Proc. Natl. Acad. Sci. U.S.A. 72 (1975) 758-762
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 758-762
    • Hand, R.1    German, J.2
  • 10
    • 0025302748 scopus 로고
    • An abnormal profile of DNA replication intermediates in Bloom's syndrome
    • Lonn U., Lonn S., Nylen U., Winblad G., and German J. An abnormal profile of DNA replication intermediates in Bloom's syndrome. Cancer Res. 50 (1990) 3141-3145
    • (1990) Cancer Res. , vol.50 , pp. 3141-3145
    • Lonn, U.1    Lonn, S.2    Nylen, U.3    Winblad, G.4    German, J.5
  • 11
    • 0022644068 scopus 로고
    • Delayed DNA maturation, a possible cause of the elevated sister-chromatid exchange in Bloom's syndrome
    • Ockey C.H., and Saffhill R. Delayed DNA maturation, a possible cause of the elevated sister-chromatid exchange in Bloom's syndrome. Carcinogenesis 7 (1986) 53-57
    • (1986) Carcinogenesis , vol.7 , pp. 53-57
    • Ockey, C.H.1    Saffhill, R.2
  • 12
    • 0346351375 scopus 로고
    • A manyfold increase in sister chromatid exchanges in Bloom's syndrome lymphocytes
    • Chaganti R.S., Schonberg S., and German J. 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    Schonberg, S.2    German, J.3
  • 13
    • 33749132155 scopus 로고    scopus 로고
    • Sit down, relax and unwind: structural insights into RecQ helicase mechanisms
    • Killoran M.P., and Keck J.L. Sit down, relax and unwind: structural insights into RecQ helicase mechanisms. Nucl. Acids Res. 34 (2006) 4098-4105
    • (2006) Nucl. Acids Res. , vol.34 , pp. 4098-4105
    • Killoran, M.P.1    Keck, J.L.2
  • 14
    • 19844372703 scopus 로고    scopus 로고
    • Structural and functional characterizations reveal the importance of a zinc binding domain in Bloom's syndrome helicase
    • Guo R.B., Rigolet P., Zargarian L., Fermandjian S., and Xi X.G. Structural and functional characterizations reveal the importance of a zinc binding domain in Bloom's syndrome helicase. Nucl. Acids Res. 33 (2005) 3109-3124
    • (2005) Nucl. Acids Res. , vol.33 , pp. 3109-3124
    • Guo, R.B.1    Rigolet, P.2    Zargarian, L.3    Fermandjian, S.4    Xi, X.G.5
  • 15
    • 33744959840 scopus 로고    scopus 로고
    • Three HRDC domains differentially modulate Deinococcus radiodurans RecQ DNA helicase biochemical activity
    • Killoran M.P., and Keck J.L. Three HRDC domains differentially modulate Deinococcus radiodurans RecQ DNA helicase biochemical activity. J. Biol. Chem. 281 (2006) 12849-12857
    • (2006) J. Biol. Chem. , vol.281 , pp. 12849-12857
    • Killoran, M.P.1    Keck, J.L.2
  • 16
    • 23444440610 scopus 로고    scopus 로고
    • Conferring substrate specificity to DNA helicases: role of the RecQ HRDC domain
    • Bernstein D.A., and Keck J.L. Conferring substrate specificity to DNA helicases: role of the RecQ HRDC domain. Structure (Cambridge) 13 (2005) 1173-1182
    • (2005) Structure (Cambridge) , vol.13 , pp. 1173-1182
    • Bernstein, D.A.1    Keck, J.L.2
  • 17
    • 0141865522 scopus 로고    scopus 로고
    • High-resolution structure of the E. coli RecQ helicase catalytic core
    • Bernstein D.A., Zittel M.C., and Keck J.L. High-resolution structure of the E. coli RecQ helicase catalytic core. EMBO J. 22 (2003) 4910-4921
    • (2003) EMBO J. , vol.22 , pp. 4910-4921
    • Bernstein, D.A.1    Zittel, M.C.2    Keck, J.L.3
  • 18
    • 5644256922 scopus 로고    scopus 로고
    • The zinc finger motif of Escherichia coli RecQ is implicated in both DNA binding and protein folding
    • Liu J.L., Rigolet P., Dou S.X., Wang P.Y., and Xi X.G. The zinc finger motif of Escherichia coli RecQ is implicated in both DNA binding and protein folding. J. Biol. Chem. 279 (2004) 42794-42802
    • (2004) J. Biol. Chem. , vol.279 , pp. 42794-42802
    • Liu, J.L.1    Rigolet, P.2    Dou, S.X.3    Wang, P.Y.4    Xi, X.G.5
  • 19
    • 0033573075 scopus 로고    scopus 로고
    • The three-dimensional structure of the HRDC domain and implications for the Werner and Bloom syndrome proteins
    • Liu Z., Macias M.J., Bottomley M.J., Stier G., Linge J.P., Nilges M., Bork P., and Sattler M. The three-dimensional structure of the HRDC domain and implications for the Werner and Bloom syndrome proteins. Structure 7 (1999) 1557-1566
    • (1999) Structure , vol.7 , pp. 1557-1566
    • Liu, Z.1    Macias, M.J.2    Bottomley, M.J.3    Stier, G.4    Linge, J.P.5    Nilges, M.6    Bork, P.7    Sattler, M.8
  • 20
    • 0030697336 scopus 로고    scopus 로고
    • A putative nucleic acid-binding domain in Bloom's and Werner's syndrome helicases
    • Morozov V., Mushegian A.R., Koonin E.V., and Bork P. A putative nucleic acid-binding domain in Bloom's and Werner's syndrome helicases. Trends Biochem. Sci. 22 (1997) 417-418
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 417-418
    • Morozov, V.1    Mushegian, A.R.2    Koonin, E.V.3    Bork, P.4
  • 23
    • 0032538453 scopus 로고    scopus 로고
    • The Bloom's syndrome helicase unwinds G4 DNA
    • Sun H., Karow J.K., Hickson I.D., and Maizels N. The Bloom's syndrome helicase unwinds G4 DNA. J. Biol. Chem. 273 (1998) 27587-27592
    • (1998) J. Biol. Chem. , vol.273 , pp. 27587-27592
    • Sun, H.1    Karow, J.K.2    Hickson, I.D.3    Maizels, N.4
  • 24
    • 22444447945 scopus 로고    scopus 로고
    • The Bloom's syndrome helicase promotes the annealing of complementary single-stranded DNA
    • Cheok C.F., Wu L., Garcia P.L., Janscak P., and Hickson I.D. The Bloom's syndrome helicase promotes the annealing of complementary single-stranded DNA. Nucl. Acids Res. 33 (2005) 3932-3941
    • (2005) Nucl. Acids Res. , vol.33 , pp. 3932-3941
    • Cheok, C.F.1    Wu, L.2    Garcia, P.L.3    Janscak, P.4    Hickson, I.D.5
  • 25
    • 20744437108 scopus 로고    scopus 로고
    • RecQ family members combine strand pairing and unwinding activities to catalyze strand exchange
    • Machwe A., Xiao L., Groden J., Matson S.W., and Orren D.K. RecQ family members combine strand pairing and unwinding activities to catalyze strand exchange. J. Biol. Chem. 280 (2005) 23397-23407
    • (2005) J. Biol. Chem. , vol.280 , pp. 23397-23407
    • Machwe, A.1    Xiao, L.2    Groden, J.3    Matson, S.W.4    Orren, D.K.5
  • 26
    • 33644596948 scopus 로고    scopus 로고
    • Competition between the DNA unwinding and strand pairing activities of the Werner and Bloom syndrome proteins
    • Machwe A., Lozada E.M., Xiao L., and Orren D.K. Competition between the DNA unwinding and strand pairing activities of the Werner and Bloom syndrome proteins. BMC Mol. Biol. 7 (2006) 1
    • (2006) BMC Mol. Biol. , vol.7 , pp. 1
    • Machwe, A.1    Lozada, E.M.2    Xiao, L.3    Orren, D.K.4
  • 28
    • 3543007196 scopus 로고    scopus 로고
    • Human RECQ5β, a protein with DNA helicase and strand-annealing activities in a single polypeptide
    • Garcia P.L., Liu Y., Jiricny J., West S.C., and Janscak P. Human RECQ5β, a protein with DNA helicase and strand-annealing activities in a single polypeptide. EMBO J. 23 (2004) 2882-2891
    • (2004) EMBO J. , vol.23 , pp. 2882-2891
    • Garcia, P.L.1    Liu, Y.2    Jiricny, J.3    West, S.C.4    Janscak, P.5
  • 29
    • 30344477373 scopus 로고    scopus 로고
    • Biochemical characterization of the RECQ4 protein, mutated in Rothmund-Thomson syndrome
    • Macris M.A., Krejci L., Bussen W., Shimamoto A., and Sung P. Biochemical characterization of the RECQ4 protein, mutated in Rothmund-Thomson syndrome. DNA Repair (Amsterdam) 5 (2006) 172-180
    • (2006) DNA Repair (Amsterdam) , vol.5 , pp. 172-180
    • Macris, M.A.1    Krejci, L.2    Bussen, W.3    Shimamoto, A.4    Sung, P.5
  • 30
    • 0035897415 scopus 로고    scopus 로고
    • Regulation and localization of the Bloom syndrome protein in response to DNA damage
    • Bischof O., Kim S.H., Irving J., Beresten S., Ellis N.A., and Campisi J. Regulation and localization of the Bloom syndrome protein in response to DNA damage. J. Cell. Biol. 153 (2001) 367-380
    • (2001) J. Cell. Biol. , vol.153 , pp. 367-380
    • Bischof, O.1    Kim, S.H.2    Irving, J.3    Beresten, S.4    Ellis, N.A.5    Campisi, J.6
  • 32
    • 0032760273 scopus 로고    scopus 로고
    • Localization of the Bloom syndrome helicase to punctate nuclear structures and the nuclear matrix and regulation during the cell cycle: comparison with the Werner's syndrome helicase
    • Gharibyan V., and Youssoufian H. Localization of the Bloom syndrome helicase to punctate nuclear structures and the nuclear matrix and regulation during the cell cycle: comparison with the Werner's syndrome helicase. Mol. Carcinog. 26 (1999) 261-273
    • (1999) Mol. Carcinog. , vol.26 , pp. 261-273
    • Gharibyan, V.1    Youssoufian, H.2
  • 34
    • 0033598931 scopus 로고    scopus 로고
    • A role for PML and the nuclear body in genomic stability
    • Zhong S., Hu P., Ye T.Z., Stan R., Ellis N.A., and Pandolfi P.P. A role for PML and the nuclear body in genomic stability. Oncogene 18 (1999) 7941-7947
    • (1999) Oncogene , vol.18 , pp. 7941-7947
    • Zhong, S.1    Hu, P.2    Ye, T.Z.3    Stan, R.4    Ellis, N.A.5    Pandolfi, P.P.6
  • 35
    • 4644351274 scopus 로고    scopus 로고
    • PML nuclear bodies: dynamic sensors of DNA damage and cellular stress
    • Dellaire G., and Bazett-Jones D.P. PML nuclear bodies: dynamic sensors of DNA damage and cellular stress. Bioessays 26 (2004) 963-977
    • (2004) Bioessays , vol.26 , pp. 963-977
    • Dellaire, G.1    Bazett-Jones, D.P.2
  • 36
    • 0037169341 scopus 로고    scopus 로고
    • The role of PML in tumor suppression
    • Salomoni P., and Pandolfi P.P. The role of PML in tumor suppression. Cell 108 (2002) 165-170
    • (2002) Cell , vol.108 , pp. 165-170
    • Salomoni, P.1    Pandolfi, P.P.2
  • 37
    • 19744378341 scopus 로고    scopus 로고
    • Intra-nuclear trafficking of the BLM helicase to DNA damage-induced foci is regulated by SUMO modification
    • Eladad S., Ye T.Z., Hu P., Leversha M., Beresten S., Matunis M.J., and Ellis N.A. Intra-nuclear trafficking of the BLM helicase to DNA damage-induced foci is regulated by SUMO modification. Hum. Mol. Genet. 14 (2005) 1351-1365
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 1351-1365
    • Eladad, S.1    Ye, T.Z.2    Hu, P.3    Leversha, M.4    Beresten, S.5    Matunis, M.J.6    Ellis, N.A.7
  • 38
    • 0035377356 scopus 로고    scopus 로고
    • Potential role for the BLM helicase in recombinational repair via a conserved interaction with RAD51
    • Wu L., Davies S.L., Levitt N.C., and Hickson I.D. Potential role for the BLM helicase in recombinational repair via a conserved interaction with RAD51. J. Biol. Chem. 276 (2001) 19375-19381
    • (2001) J. Biol. Chem. , vol.276 , pp. 19375-19381
    • Wu, L.1    Davies, S.L.2    Levitt, N.C.3    Hickson, I.D.4
  • 39
    • 17144395509 scopus 로고    scopus 로고
    • ATR and ATM-dependent movement of BLM helicase during replication stress ensures optimal ATM activation and 53BP1 focus formation
    • Davalos A.R., Kaminker P., Hansen R.K., and Campisi J. ATR and ATM-dependent movement of BLM helicase during replication stress ensures optimal ATM activation and 53BP1 focus formation. Cell Cycle 3 (2004) 1579-1586
    • (2004) Cell Cycle , vol.3 , pp. 1579-1586
    • Davalos, A.R.1    Kaminker, P.2    Hansen, R.K.3    Campisi, J.4
  • 40
    • 0034089029 scopus 로고    scopus 로고
    • Bipartite structure of the SGS1 DNA helicase in Saccharomyces cerevisiae
    • Mullen J.R., Kaliraman V., and Brill S.J. Bipartite structure of the SGS1 DNA helicase in Saccharomyces cerevisiae. Genetics 154 (2000) 1101-1114
    • (2000) Genetics , vol.154 , pp. 1101-1114
    • Mullen, J.R.1    Kaliraman, V.2    Brill, S.J.3
  • 41
    • 0028033989 scopus 로고
    • The yeast type I topoisomerase Top3 interacts with Sgs1, a DNA helicase homolog: a potential eukaryotic reverse gyrase
    • Gangloff S., McDonald J.P., Bendixen C., Arthur L., and Rothstein R. 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    McDonald, J.P.2    Bendixen, C.3    Arthur, L.4    Rothstein, R.5
  • 42
    • 0042466524 scopus 로고    scopus 로고
    • DNA polymerase stabilization at stalled replication forks requires Mec1 and the RecQ helicase Sgs1
    • Cobb J.A., Bjergbaek L., Shimada K., Frei C., and Gasser S.M. DNA polymerase stabilization at stalled replication forks requires Mec1 and the RecQ helicase Sgs1. EMBO J. 22 (2003) 4325-4336
    • (2003) EMBO J. , vol.22 , pp. 4325-4336
    • Cobb, J.A.1    Bjergbaek, L.2    Shimada, K.3    Frei, C.4    Gasser, S.M.5
  • 43
    • 0141864666 scopus 로고    scopus 로고
    • Bloom syndrome cells undergo p53-dependent apoptosis and delayed assembly of BRCA1 and NBS1 repair complexes at stalled replication forks
    • Davalos A.R., and Campisi J. Bloom syndrome cells undergo p53-dependent apoptosis and delayed assembly of BRCA1 and NBS1 repair complexes at stalled replication forks. J. Cell. Biol. 162 (2003) 1197-1209
    • (2003) J. Cell. Biol. , vol.162 , pp. 1197-1209
    • Davalos, A.R.1    Campisi, J.2
  • 44
    • 0036544565 scopus 로고    scopus 로고
    • Bloom's syndrome protein is required for correct relocalization of RAD50/MRE11/NBS1 complex after replication fork arrest
    • Franchitto A., and Pichierri P. Bloom's syndrome protein is required for correct relocalization of RAD50/MRE11/NBS1 complex after replication fork arrest. J. Cell. Biol. 157 (2002) 19-30
    • (2002) J. Cell. Biol. , vol.157 , pp. 19-30
    • Franchitto, A.1    Pichierri, P.2
  • 45
    • 13444283383 scopus 로고    scopus 로고
    • Mechanistically distinct roles for Sgs1p in checkpoint activation and replication fork maintenance
    • Bjergbaek L., Cobb J.A., Tsai-Pflugfelder M., and Gasser S.M. Mechanistically distinct roles for Sgs1p in checkpoint activation and replication fork maintenance. EMBO J. 24 (2005) 405-417
    • (2005) EMBO J. , vol.24 , pp. 405-417
    • Bjergbaek, L.1    Cobb, J.A.2    Tsai-Pflugfelder, M.3    Gasser, S.M.4
  • 46
    • 33749456218 scopus 로고    scopus 로고
    • Top3 processes recombination intermediates and modulates checkpoint activity after DNA damage
    • Mankouri H.W., and Hickson I.D. Top3 processes recombination intermediates and modulates checkpoint activity after DNA damage. Mol. Biol. Cell 17 (2006) 4473-4483
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4473-4483
    • Mankouri, H.W.1    Hickson, I.D.2
  • 48
    • 0035797444 scopus 로고    scopus 로고
    • Regulation of DNA replication fork progression through damaged DNA by the Mec1/Rad53 checkpoint
    • Tercero J.A., and Diffley J.F. Regulation of DNA replication fork progression through damaged DNA by the Mec1/Rad53 checkpoint. Nature 412 (2001) 553-557
    • (2001) Nature , vol.412 , pp. 553-557
    • Tercero, J.A.1    Diffley, J.F.2
  • 50
    • 0034176335 scopus 로고    scopus 로고
    • Initiation of genetic recombination and recombination-dependent replication
    • Kowalczykowski S.C. Initiation of genetic recombination and recombination-dependent replication. Trends Biochem. Sci. 25 (2000) 156-165
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 156-165
    • Kowalczykowski, S.C.1
  • 51
    • 0034026997 scopus 로고    scopus 로고
    • Replication and recombination intersect
    • Marians K.J. Replication and recombination intersect. Curr. Opin. Genet. Dev. 10 (2000) 151-156
    • (2000) Curr. Opin. Genet. Dev. , vol.10 , pp. 151-156
    • Marians, K.J.1
  • 52
    • 0033954246 scopus 로고    scopus 로고
    • Replication fork pausing and recombination or "gimme a break"
    • Rothstein R., Michel B., and Gangloff S. Replication fork pausing and recombination or "gimme a break". Genes Dev. 14 (2000) 1-10
    • (2000) Genes Dev. , vol.14 , pp. 1-10
    • Rothstein, R.1    Michel, B.2    Gangloff, S.3
  • 53
    • 2442686846 scopus 로고    scopus 로고
    • Functional uncoupling of twin polymerases: mechanism of polymerase dissociation from a lagging-strand block
    • McInerney P., and O'Donnell M. Functional uncoupling of twin polymerases: mechanism of polymerase dissociation from a lagging-strand block. J. Biol. Chem. 279 (2004) 21543-21551
    • (2004) J. Biol. Chem. , vol.279 , pp. 21543-21551
    • McInerney, P.1    O'Donnell, M.2
  • 54
    • 0037799191 scopus 로고    scopus 로고
    • Uncoupling of leading- and lagging-strand DNA replication during lesion bypass in vivo
    • Pages V., and Fuchs R.P. Uncoupling of leading- and lagging-strand DNA replication during lesion bypass in vivo. Science 300 (2003) 1300-1303
    • (2003) Science , vol.300 , pp. 1300-1303
    • Pages, V.1    Fuchs, R.P.2
  • 55
    • 0038365180 scopus 로고    scopus 로고
    • Fate of DNA replication fork encountering a single DNA lesion during oriC plasmid DNA replication in vitro
    • Higuchi K., Katayama T., Iwai S., Hidaka M., Horiuchi T., and Maki H. Fate of DNA replication fork encountering a single DNA lesion during oriC plasmid DNA replication in vitro. Genes Cells 8 (2003) 437-449
    • (2003) Genes Cells , vol.8 , pp. 437-449
    • Higuchi, K.1    Katayama, T.2    Iwai, S.3    Hidaka, M.4    Horiuchi, T.5    Maki, H.6
  • 56
    • 14644415982 scopus 로고    scopus 로고
    • The disposition of nascent strands at stalled replication forks dictates the pathway of replisome loading during restart
    • Heller R.C., and Marians K.J. The disposition of nascent strands at stalled replication forks dictates the pathway of replisome loading during restart. Mol. Cell 17 (2005) 733-743
    • (2005) Mol. Cell , vol.17 , pp. 733-743
    • Heller, R.C.1    Marians, K.J.2
  • 57
    • 33845330910 scopus 로고    scopus 로고
    • Replisome assembly and the direct restart of stalled replication forks
    • Heller R.C., and Marians K.J. Replisome assembly and the direct restart of stalled replication forks. Nat. Rev. Mol. Cell. Biol. 7 (2006) 932-943
    • (2006) Nat. Rev. Mol. Cell. Biol. , vol.7 , pp. 932-943
    • Heller, R.C.1    Marians, K.J.2
  • 58
    • 33747352774 scopus 로고    scopus 로고
    • The Bloom's syndrome helicase can promote the regression of a model replication fork
    • Ralf C., Hickson I.D., and Wu L. The Bloom's syndrome helicase can promote the regression of a model replication fork. J. Biol. Chem. (2006)
    • (2006) J. Biol. Chem.
    • Ralf, C.1    Hickson, I.D.2    Wu, L.3
  • 59
    • 28844506236 scopus 로고    scopus 로고
    • Suffering in silence: the tolerance of DNA damage
    • Friedberg E.C. Suffering in silence: the tolerance of DNA damage. Nat. Rev. Mol. Cell. Biol. 6 (2005) 943-953
    • (2005) Nat. Rev. Mol. Cell. Biol. , vol.6 , pp. 943-953
    • Friedberg, E.C.1
  • 60
    • 33646843592 scopus 로고    scopus 로고
    • D-loops are a preferred substrate for the Bloom's syndrome helicase
    • Bachrati C.Z., Borts R.H., Hickson I.D., and Mobile. D-loops are a preferred substrate for the Bloom's syndrome helicase. Nucl. Acids Res. 34 (2006) 2269-2279
    • (2006) Nucl. Acids Res. , vol.34 , pp. 2269-2279
    • Bachrati, C.Z.1    Borts, R.H.2    Hickson, I.D.3    Mobile4
  • 62
    • 0016290545 scopus 로고
    • Bloom's syndrome. III. Analysis of the chromosome aberration characteristic of this disorder
    • German J., Crippa L.P., and Bloom D. Bloom's syndrome. III. Analysis of the chromosome aberration characteristic of this disorder. Chromosoma 48 (1974) 361-366
    • (1974) Chromosoma , vol.48 , pp. 361-366
    • German, J.1    Crippa, L.P.2    Bloom, D.3
  • 63
    • 3042546122 scopus 로고    scopus 로고
    • Heteroduplex rejection during single-strand annealing requires Sgs1 helicase and mismatch repair proteins Msh2 and Msh6 but not Pms1
    • Sugawara N., Goldfarb T., Studamire B., Alani E., and Haber J.E. Heteroduplex rejection during single-strand annealing requires Sgs1 helicase and mismatch repair proteins Msh2 and Msh6 but not Pms1. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 9315-9320
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 9315-9320
    • Sugawara, N.1    Goldfarb, T.2    Studamire, B.3    Alani, E.4    Haber, J.E.5
  • 64
    • 8144220041 scopus 로고    scopus 로고
    • Formation of deletions during double-strand break repair in Drosophila DmBlm mutants occurs after strand invasion
    • McVey M., Larocque J.R., Adams M.D., and Sekelsky J.J. Formation of deletions during double-strand break repair in Drosophila DmBlm mutants occurs after strand invasion. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 15694-15699
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 15694-15699
    • McVey, M.1    Larocque, J.R.2    Adams, M.D.3    Sekelsky, J.J.4
  • 65
    • 0037428069 scopus 로고    scopus 로고
    • Drosophila BLM in double-strand break repair by synthesis-dependent strand annealing
    • Adams M.D., McVey M., and Sekelsky J.J. Drosophila BLM in double-strand break repair by synthesis-dependent strand annealing. Science 299 (2003) 265-267
    • (2003) Science , vol.299 , pp. 265-267
    • Adams, M.D.1    McVey, M.2    Sekelsky, J.J.3
  • 71
    • 18944395928 scopus 로고    scopus 로고
    • Yeast Rmi1/Nce4 controls genome stability as a subunit of the Sgs1-Top3 complex
    • Mullen J.R., Nallaseth F.S., Lan Y.Q., Slagle C.E., and Brill S.J. Yeast Rmi1/Nce4 controls genome stability as a subunit of the Sgs1-Top3 complex. Mol. Cell. Biol. 25 (2005) 4476-4487
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 4476-4487
    • Mullen, J.R.1    Nallaseth, F.S.2    Lan, Y.Q.3    Slagle, C.E.4    Brill, S.J.5
  • 73
    • 17844386117 scopus 로고    scopus 로고
    • BLAP75, an essential component of Bloom's syndrome protein complexes that maintain genome integrity
    • Yin J., Sobeck A., Xu C., Meetei A.R., Hoatlin M., Li L., and Wang W. BLAP75, an essential component of Bloom's syndrome protein complexes that maintain genome integrity. EMBO J. 24 (2005) 1465-1476
    • (2005) EMBO J. , vol.24 , pp. 1465-1476
    • Yin, J.1    Sobeck, A.2    Xu, C.3    Meetei, A.R.4    Hoatlin, M.5    Li, L.6    Wang, W.7
  • 74
    • 0032477804 scopus 로고    scopus 로고
    • Mammalian DNA topoisomerase IIIα is essential in early embryogenesis
    • Li W., and Wang J.C. Mammalian DNA topoisomerase IIIα is essential in early embryogenesis. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 1010-1013
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 1010-1013
    • Li, W.1    Wang, J.C.2
  • 75
    • 0036812236 scopus 로고    scopus 로고
    • Mutations in homologous recombination genes rescue top3 slow growth in Saccharomyces cerevisiae
    • Shor E., Gangloff S., Wagner M., Weinstein J., Price G., and Rothstein R. Mutations in homologous recombination genes rescue top3 slow growth in Saccharomyces cerevisiae. Genetics 162 (2002) 647-662
    • (2002) Genetics , vol.162 , pp. 647-662
    • Shor, E.1    Gangloff, S.2    Wagner, M.3    Weinstein, J.4    Price, G.5    Rothstein, R.6
  • 76
    • 0037150495 scopus 로고    scopus 로고
    • Inactivation of homologous recombination suppresses defects in topoisomerase III-deficient mutants
    • Oakley T.J., Goodwin A., Chakraverty R.K., and Hickson I.D. Inactivation of homologous recombination suppresses defects in topoisomerase III-deficient mutants. DNA Rep. (Amsterdam) 1 (2002) 463-482
    • (2002) DNA Rep. (Amsterdam) , vol.1 , pp. 463-482
    • Oakley, T.J.1    Goodwin, A.2    Chakraverty, R.K.3    Hickson, I.D.4
  • 78
    • 33746600628 scopus 로고    scopus 로고
    • Topoisomerase IIIα and Bloom's helicase can resolve a mobile double Holliday junction substrate through convergent branch migration
    • Plank J.L., Wu J., and Hsieh T.S. Topoisomerase IIIα and Bloom's helicase can resolve a mobile double Holliday junction substrate through convergent branch migration. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 11118-111123
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 11118-111123
    • Plank, J.L.1    Wu, J.2    Hsieh, T.S.3
  • 79
    • 33744927719 scopus 로고    scopus 로고
    • A double Holliday junction dissolvasome comprising BLM, topoisomerase IIIα, and BLAP75
    • Raynard S., Bussen W., and Sung P. A double Holliday junction dissolvasome comprising BLM, topoisomerase IIIα, and BLAP75. J. Biol. Chem. 281 (2006) 13861-13864
    • (2006) J. Biol. Chem. , vol.281 , pp. 13861-13864
    • Raynard, S.1    Bussen, W.2    Sung, P.3
  • 81
    • 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
  • 83
    • 0345447604 scopus 로고    scopus 로고
    • Srs2 and Sgs1-Top3 suppress crossovers during double-strand break repair in yeast
    • Ira G., Malkova A., Liberi G., Foiani M., and Haber J.E. 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    Malkova, A.2    Liberi, G.3    Foiani, M.4    Haber, J.E.5
  • 84
    • 0037107402 scopus 로고    scopus 로고
    • Holliday junction resolution in human cells: two junction endonucleases with distinct substrate specificities
    • Constantinou A., Chen X.B., McGowan C.H., and West S.C. Holliday junction resolution in human cells: two junction endonucleases with distinct substrate specificities. EMBO J. 21 (2002) 5577-5585
    • (2002) EMBO J. , vol.21 , pp. 5577-5585
    • Constantinou, A.1    Chen, X.B.2    McGowan, C.H.3    West, S.C.4
  • 85
    • 0035951396 scopus 로고    scopus 로고
    • Branch migration and Holliday junction resolution catalyzed by activities from mammalian cells
    • Constantinou A., Davies A.A., and West S.C. Branch migration and Holliday junction resolution catalyzed by activities from mammalian cells. Cell 104 (2001) 259-268
    • (2001) Cell , vol.104 , pp. 259-268
    • Constantinou, A.1    Davies, A.A.2    West, S.C.3
  • 86
    • 0346340054 scopus 로고    scopus 로고
    • RAD51C is required for Holliday junction processing in mammalian cells
    • Liu Y., Masson J.Y., Shah R., O'Regan P., and West S.C. RAD51C is required for Holliday junction processing in mammalian cells. Science 303 (2004) 243-246
    • (2004) Science , vol.303 , pp. 243-246
    • Liu, Y.1    Masson, J.Y.2    Shah, R.3    O'Regan, P.4    West, S.C.5
  • 87
    • 0036085460 scopus 로고    scopus 로고
    • Cellular roles of DNA topoisomerases: a molecular perspective
    • Wang J.C. Cellular roles of DNA topoisomerases: a molecular perspective. Nat. Rev. Mol. Cell. Biol. 3 (2002) 430-440
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 430-440
    • Wang, J.C.1
  • 88
    • 0033214032 scopus 로고    scopus 로고
    • Knot what we thought before: the twisted story of replication
    • Postow L., Peter B.J., and Cozzarelli N.R. Knot what we thought before: the twisted story of replication. Bioessays 21 (1999) 805-808
    • (1999) Bioessays , vol.21 , pp. 805-808
    • Postow, L.1    Peter, B.J.2    Cozzarelli, N.R.3
  • 89
    • 0027976667 scopus 로고
    • Decatenating activity of Escherichia coli DNA gyrase and topoisomerases I and III during oriC and pBR322 DNA replication in vitro
    • Hiasa H., DiGate R.J., and Marians K.J. Decatenating activity of Escherichia coli DNA gyrase and topoisomerases I and III during oriC and pBR322 DNA replication in vitro. J. Biol. Chem. 269 (1994) 2093-2099
    • (1994) J. Biol. Chem. , vol.269 , pp. 2093-2099
    • Hiasa, H.1    DiGate, R.J.2    Marians, K.J.3
  • 90
    • 0028589156 scopus 로고
    • Topoisomerase III, but not topoisomerase I, can support nascent chain elongation during theta-type DNA replication
    • Hiasa H., and Marians K.J. Topoisomerase III, but not topoisomerase I, can support nascent chain elongation during theta-type DNA replication. J. Biol. Chem. 269 (1994) 32655-32659
    • (1994) J. Biol. Chem. , vol.269 , pp. 32655-32659
    • Hiasa, H.1    Marians, K.J.2
  • 91
    • 0037424533 scopus 로고    scopus 로고
    • Topoisomerase III can serve as the cellular decatenase in Escherichia coli
    • Nurse P., Levine C., Hassing H., and Marians K.J. Topoisomerase III can serve as the cellular decatenase in Escherichia coli. J. Biol. Chem. 278 (2003) 8653-8660
    • (2003) J. Biol. Chem. , vol.278 , pp. 8653-8660
    • Nurse, P.1    Levine, C.2    Hassing, H.3    Marians, K.J.4
  • 92
    • 17644410077 scopus 로고    scopus 로고
    • Recql5 and Blm RecQ DNA helicases have nonredundant roles in suppressing crossovers
    • Hu Y., Lu X., Barnes E., Yan M., Lou H., and Luo G. Recql5 and Blm RecQ DNA helicases have nonredundant roles in suppressing crossovers. Mol. Cell. Biol. 25 (2005) 3431-3442
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 3431-3442
    • Hu, Y.1    Lu, X.2    Barnes, E.3    Yan, M.4    Lou, H.5    Luo, G.6
  • 93
    • 0034164070 scopus 로고    scopus 로고
    • Human RecQ5β, a large isomer of RecQ5 DNA helicase, localizes in the nucleoplasm and interacts with topoisomerases 3α and 3β
    • Shimamoto A., Nishikawa K., Kitao S., and Furuichi Y. Human RecQ5β, a large isomer of RecQ5 DNA helicase, localizes in the nucleoplasm and interacts with topoisomerases 3α and 3β. Nucl. Acids Res. 28 (2000) 1647-1655
    • (2000) Nucl. Acids Res. , vol.28 , pp. 1647-1655
    • Shimamoto, A.1    Nishikawa, K.2    Kitao, S.3    Furuichi, Y.4
  • 95
    • 26444467122 scopus 로고    scopus 로고
    • Phosphorylation of BLM, dissociation from topoisomerase IIIα, and colocalization with gamma-H2AX after topoisomerase I-induced replication damage
    • Rao V.A., Fan A.M., Meng L., Doe C.F., North P.S., Hickson I.D., and Pommier Y. Phosphorylation of BLM, dissociation from topoisomerase IIIα, and colocalization with gamma-H2AX after topoisomerase I-induced replication damage. Mol. Cell. Biol. 25 (2005) 8925-8937
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8925-8937
    • Rao, V.A.1    Fan, A.M.2    Meng, L.3    Doe, C.F.4    North, P.S.5    Hickson, I.D.6    Pommier, Y.7


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