메뉴 건너뛰기




Volumn 5, Issue 2, 2006, Pages 172-180

Biochemical characterization of the RECQ4 protein, mutated in Rothmund-Thomson syndrome

Author keywords

ATPase; DNA repair; Helicase; RECQ4; RTS; ssDNA annealing

Indexed keywords

ADENOSINE TRIPHOSPHATASE; DNA; DNA BINDING PROTEIN; HELICASE; PROTEIN RECQ4; RECQ HELICASE; SINGLE STRANDED DNA; UNCLASSIFIED DRUG;

EID: 30344477373     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2005.09.005     Document Type: Article
Times cited : (132)

References (52)
  • 1
    • 0037364415 scopus 로고    scopus 로고
    • RecQ helicases: Caretakers of the genome
    • I.D. Hickson 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
  • 8
    • 0034737004 scopus 로고    scopus 로고
    • Rothmund-Thomson syndrome due to RECQ4 helicase mutations: Report and clinical and molecular comparisons with Bloom syndrome and Werner syndrome
    • N.M. Lindor, Y. Furuichi, S. Kitao, A. Shimamoto, C. Arndt, and S. Jalal Rothmund-Thomson syndrome due to RECQ4 helicase mutations: report and clinical and molecular comparisons with Bloom syndrome and Werner syndrome Am. J. Med. Genet. 90 2000 223 228
    • (2000) Am. J. Med. Genet. , vol.90 , pp. 223-228
    • Lindor, N.M.1    Furuichi, Y.2    Kitao, S.3    Shimamoto, A.4    Arndt, C.5    Jalal, S.6
  • 12
    • 0032535661 scopus 로고    scopus 로고
    • Cloning of two new human helicase genes of the RecQ family: Biological significance of multiple species in higher eukaryotes
    • S. Kitao, I. Ohsugi, K. Ichikawa, M. Goto, Y. Furuichi, and A. Shimamoto Cloning of two new human helicase genes of the RecQ family: biological significance of multiple species in higher eukaryotes Genomics 54 1998 443 452
    • (1998) Genomics , vol.54 , pp. 443-452
    • Kitao, S.1    Ohsugi, I.2    Ichikawa, K.3    Goto, M.4    Furuichi, Y.5    Shimamoto, A.6
  • 13
    • 0032736140 scopus 로고    scopus 로고
    • Rothmund-Thomson syndrome responsible gene, RECQL4: Genomic structure and products
    • S. Kitao, N.M. Lindor, M. Shiratori, Y. Furuichi, and A. Shimamoto Rothmund-Thomson syndrome responsible gene, RECQL4: genomic structure and products Genomics 61 1999 268 276
    • (1999) Genomics , vol.61 , pp. 268-276
    • Kitao, S.1    Lindor, N.M.2    Shiratori, M.3    Furuichi, Y.4    Shimamoto, A.5
  • 14
    • 19544366597 scopus 로고    scopus 로고
    • RECQL4, mutated in the Rothmund-Thomson and RAPADILINO syndromes, interacts with ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway
    • J. Yin, Y.T. Kwon, A. Varshavsky, and W. Wang RECQL4, mutated in the Rothmund-Thomson and RAPADILINO syndromes, interacts with ubiquitin ligases UBR1 and UBR2 of the N-end rule pathway Hum. Mol. Genet. 13 2004 2421 2430
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2421-2430
    • Yin, J.1    Kwon, Y.T.2    Varshavsky, A.3    Wang, W.4
  • 15
    • 0035062128 scopus 로고    scopus 로고
    • DNA helicase deficiencies associated with cancer predisposition and premature ageing disorders
    • P. Mohaghegh, and I.D. Hickson DNA helicase deficiencies associated with cancer predisposition and premature ageing disorders Hum. Mol. Genet. 10 2001 741 746
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 741-746
    • Mohaghegh, P.1    Hickson, I.D.2
  • 16
    • 0346351375 scopus 로고
    • A manyfold increase in sister chromatid exchanges in Bloom's syndrome lymphocytes
    • R.S. Chaganti, S. Schonberg, and J. German 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
  • 19
    • 0025215315 scopus 로고
    • Rothmund-Thomson syndrome associated with trisomy 8 mosaicism
    • K.L. Ying, J. Oizumi, and C.J. Curry Rothmund-Thomson syndrome associated with trisomy 8 mosaicism J. Med. Genet. 27 1990 258 260
    • (1990) J. Med. Genet. , vol.27 , pp. 258-260
    • Ying, K.L.1    Oizumi, J.2    Curry, C.J.3
  • 20
    • 15544389502 scopus 로고    scopus 로고
    • Defective sister-chromatid cohesion, aneuploidy and cancer predisposition in a mouse model of type II Rothmund-Thomson syndrome
    • M.B. Mann, C.A. Hodges, E. Barnes, H. Vogel, T.J. Hassold, and G Luo Defective sister-chromatid cohesion, aneuploidy and cancer predisposition in a mouse model of type II Rothmund-Thomson syndrome Hum. Mol. Genet. 14 2005 813 825
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 813-825
    • Mann, M.B.1    Hodges, C.A.2    Barnes, E.3    Vogel, H.4    Hassold, T.J.5    Luo, G.6
  • 22
    • 10944232673 scopus 로고    scopus 로고
    • Postreplicative recruitment of cohesin to double-strand breaks is required for DNA repair
    • L. Strom, H.B. Lindroos, K. Shirahige, and C. Sjogren Postreplicative recruitment of cohesin to double-strand breaks is required for DNA repair Mol. Cell 16 2004 1003 1015
    • (2004) Mol. Cell , vol.16 , pp. 1003-1015
    • Strom, L.1    Lindroos, H.B.2    Shirahige, K.3    Sjogren, C.4
  • 23
    • 10944262393 scopus 로고    scopus 로고
    • DNA damage response pathway uses histone modification to assemble a double-strand break-specific cohesin domain
    • E. Unal, A. Arbel-Eden, U. Sattler, R. Shroff, M. Lichten, J.E. Haber, and D. Koshland DNA damage response pathway uses histone modification to assemble a double-strand break-specific cohesin domain Mol. Cell 16 2004 991 1002
    • (2004) Mol. Cell , vol.16 , pp. 991-1002
    • Unal, E.1    Arbel-Eden, A.2    Sattler, U.3    Shroff, R.4    Lichten, M.5    Haber, J.E.6    Koshland, D.7
  • 24
    • 0034164070 scopus 로고    scopus 로고
    • Human RecQ5beta, a large isomer of RecQ5 DNA helicase, localizes in the nucleoplasm and interacts with topoisomerases 3alpha and 3beta
    • A. Shimamoto, K. Nishikawa, S. Kitao, and Y. Furuichi Human RecQ5beta, a large isomer of RecQ5 DNA helicase, localizes in the nucleoplasm and interacts with topoisomerases 3alpha and 3beta 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
  • 25
  • 27
    • 0034231844 scopus 로고    scopus 로고
    • Werner's syndrome protein (WRN) migrates Holliday junctions and co-localizes with RPA upon replication arrest
    • A. Constantinou, M. Tarsounas, J.K. Karow, R.M. Brosh, V.A. Bohr, I.D. Hickson, and S.C. West Werner's syndrome protein (WRN) migrates Holliday junctions and co-localizes with RPA upon replication arrest EMBO Rep. 1 2000 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
  • 28
    • 2342487313 scopus 로고    scopus 로고
    • Analysis of the unwinding activity of the dimeric RECQ1 helicase in the presence of human replication protein a
    • S. Cui, D. Arosio, K.M. Doherty, R.M. Brosh Jr., A. Falaschi, and A. Vindigni Analysis of the unwinding activity of the dimeric RECQ1 helicase in the presence of human replication protein A Nucl. Acids Res. 32 2004 2158 2170
    • (2004) Nucl. Acids Res. , vol.32 , pp. 2158-2170
    • Cui, S.1    Arosio, D.2    Doherty, K.M.3    Brosh Jr., R.M.4    Falaschi, A.5    Vindigni, A.6
  • 29
    • 3543007196 scopus 로고    scopus 로고
    • Human RECQ5beta, a protein with DNA helicase and strand-annealing activities in a single polypeptide
    • P.L. Garcia, Y. Liu, J. Jiricny, S.C. West, and P. Janscak Human RECQ5beta, 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
  • 30
    • 0035937811 scopus 로고    scopus 로고
    • Basis for avid homologous DNA strand exchange by human Rad51 and RPA
    • S. Sigurdsson, K. Trujillo, B. Song, S. Stratton, and P. Sung Basis for avid homologous DNA strand exchange by human Rad51 and RPA J. Biol. Chem. 276 2001 8798 8806
    • (2001) J. Biol. Chem. , vol.276 , pp. 8798-8806
    • Sigurdsson, S.1    Trujillo, K.2    Song, B.3    Stratton, S.4    Sung, P.5
  • 31
    • 0030686496 scopus 로고    scopus 로고
    • The Bloom's syndrome gene product is a 3′-5′ DNA helicase
    • J.K. Karow, R.K. Chakraverty, and I.D. Hickson The Bloom's syndrome gene product is a 3′-5′ DNA helicase J. Biol. Chem. 272 1997 30611 30614
    • (1997) J. Biol. Chem. , vol.272 , pp. 30611-30614
    • Karow, J.K.1    Chakraverty, R.K.2    Hickson, I.D.3
  • 33
    • 0141707817 scopus 로고    scopus 로고
    • Generating crossovers by resolution of nicked Holliday junctions: A role for Mus81-Eme1 in meiosis
    • F. Osman, J. Dixon, C.L. Doe, and M.C. Whitby Generating crossovers by resolution of nicked Holliday junctions: a role for Mus81-Eme1 in meiosis Mol. Cell 12 2003 761 774
    • (2003) Mol. Cell , vol.12 , pp. 761-774
    • Osman, F.1    Dixon, J.2    Doe, C.L.3    Whitby, M.C.4
  • 34
    • 0032492853 scopus 로고    scopus 로고
    • Catalysis of homologous DNA pairing by yeast Rad51 and Rad54 proteins
    • G. Petukhova, S. Stratton, and P. Sung Catalysis of homologous DNA pairing by yeast Rad51 and Rad54 proteins Nature 393 1998 91 94
    • (1998) Nature , vol.393 , pp. 91-94
    • Petukhova, G.1    Stratton, S.2    Sung, P.3
  • 35
  • 37
    • 0040436076 scopus 로고    scopus 로고
    • Functional and physical interaction between WRN helicase and human replication protein a
    • R.M.J. Brosh Functional and physical interaction between WRN helicase and human replication protein A J. Biol. Chem. 275 1999 18341 18350
    • (1999) J. Biol. Chem. , vol.275 , pp. 18341-18350
    • Brosh, R.M.J.1
  • 40
    • 0037137177 scopus 로고    scopus 로고
    • The Werner syndrome helicase/exonuclease (WRN) disrupts and degrades D-loops in vitro
    • D.K. Orren, S. Theodore, and A. Machwe The Werner syndrome helicase/exonuclease (WRN) disrupts and degrades D-loops in vitro Biochemistry 41 2002 13483 13488
    • (2002) Biochemistry , vol.41 , pp. 13483-13488
    • Orren, D.K.1    Theodore, S.2    MacHwe, A.3
  • 41
    • 0347987856 scopus 로고    scopus 로고
    • The Bloom's syndrome helicase suppresses crossing over during homologous recombination
    • L. Wu, and I.D. Hickson 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
  • 42
    • 20744437108 scopus 로고    scopus 로고
    • RECQ family members combine strand pairing and unwinding activities to catalyze strand exchange
    • A. Machwe, L. Xiao, J. Groden, S.W. Matson, and D.K. Orren RECQ family members combine strand pairing and unwinding activities to catalyze strand exchange J. Biol. Chem. 2005
    • (2005) J. Biol. Chem.
    • MacHwe, A.1    Xiao, L.2    Groden, J.3    Matson, S.W.4    Orren, D.K.5
  • 43
    • 0242666387 scopus 로고    scopus 로고
    • ATPase and DNA helicase activities of the Saccharomyces cerevisiae anti-recombinase Srs2
    • S. Van Komen, M.S. Reddy, L. Krejci, H. Klein, and P. Sung ATPase and DNA helicase activities of the Saccharomyces cerevisiae anti-recombinase Srs2 J. Biol. Chem. 278 2003 44331 44337
    • (2003) J. Biol. Chem. , vol.278 , pp. 44331-44337
    • Van Komen, S.1    Reddy, M.S.2    Krejci, L.3    Klein, H.4    Sung, P.5
  • 44
    • 0032568595 scopus 로고    scopus 로고
    • DNA annealing by RAD52 protein is stimulated by specific interaction with the complex of replication protein a and single-stranded DNA
    • T. Sugiyama, J.H. New, and S.C. Kowalczykowski DNA annealing by RAD52 protein is stimulated by specific interaction with the complex of replication protein A and single-stranded DNA Proc. Natl. Acad. Sci. U.S.A. 95 1998 6049 6054
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 6049-6054
    • Sugiyama, T.1    New, J.H.2    Kowalczykowski, S.C.3
  • 45
    • 0031902872 scopus 로고    scopus 로고
    • Rad52 forms ring structures and co-operates with RPA in single-strand DNA annealing
    • A. Shinohara, M. Shinohara, T. Ohta, S. Matsuda, and T. Ogawa Rad52 forms ring structures and co-operates with RPA in single-strand DNA annealing Genes Cells 3 1998 145 156
    • (1998) Genes Cells , vol.3 , pp. 145-156
    • Shinohara, A.1    Shinohara, M.2    Ohta, T.3    Matsuda, S.4    Ogawa, T.5
  • 46
    • 0037449803 scopus 로고    scopus 로고
    • Characterization of the DNA-unwinding activity of human RECQ1, a helicase specifically stimulated by human replication protein a
    • S. Cui, R. Klima, A. Ochem, D. Arosio, A. Falaschi, and A. Vindigni Characterization of the DNA-unwinding activity of human RECQ1, a helicase specifically stimulated by human replication protein A J. Biol. Chem. 278 2003 1424 1432
    • (2003) J. Biol. Chem. , vol.278 , pp. 1424-1432
    • Cui, S.1    Klima, R.2    Ochem, A.3    Arosio, D.4    Falaschi, A.5    Vindigni, A.6
  • 47
    • 0035902524 scopus 로고    scopus 로고
    • The architecture of the human Rad54-DNA complex provides evidence for protein translocation along DNA
    • D. Ristic, C. Wyman, C. Paulusma, and R. Kanaar The architecture of the human Rad54-DNA complex provides evidence for protein translocation along DNA Proc. Natl. Acad. Sci. U.S.A. 98 2001 8454 8460
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 8454-8460
    • Ristic, D.1    Wyman, C.2    Paulusma, C.3    Kanaar, R.4
  • 48
    • 0033635247 scopus 로고    scopus 로고
    • Superhelicity-driven homologous DNA pairing by yeast recombination factors Rad51 and Rad54
    • S. Van Komen, G. Petukhova, S. Sigurdsson, S. Stratton, and P. Sung Superhelicity-driven homologous DNA pairing by yeast recombination factors Rad51 and Rad54 Mol. Cell 6 2000 563 572
    • (2000) Mol. Cell , vol.6 , pp. 563-572
    • Van Komen, S.1    Petukhova, G.2    Sigurdsson, S.3    Stratton, S.4    Sung, P.5
  • 49
    • 0036864703 scopus 로고    scopus 로고
    • Rad54, a Swi2/Snf2-like recombinational repair protein, disassembles Rad51:dsDNA filaments
    • J.A. Solinger, K. Kiianitsa, and W.D. Heyer Rad54, a Swi2/Snf2-like recombinational repair protein, disassembles Rad51:dsDNA filaments Mol. Cell 10 2002 1175 1188
    • (2002) Mol. Cell , vol.10 , pp. 1175-1188
    • Solinger, J.A.1    Kiianitsa, K.2    Heyer, W.D.3
  • 51
    • 0037673943 scopus 로고    scopus 로고
    • The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments
    • X. Veaute, J. Jeusset, C. Soustelle, S.C. Kowalczykowski, E. Le Cam, and F. Fabre The Srs2 helicase prevents recombination by disrupting Rad51 nucleoprotein filaments Nature 423 2003 309 312
    • (2003) Nature , vol.423 , pp. 309-312
    • Veaute, X.1    Jeusset, J.2    Soustelle, C.3    Kowalczykowski, S.C.4    Le Cam, E.5    Fabre, F.6
  • 52
    • 13244252309 scopus 로고    scopus 로고
    • UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli
    • X. Veaute, S. Delmas, M. Selva, J. Jeusset, E. Le Cam, I. Matic, F. Fabre, and M.A. Petit UvrD helicase, unlike Rep helicase, dismantles RecA nucleoprotein filaments in Escherichia coli EMBO J. 24 2005 180 189
    • (2005) EMBO J. , vol.24 , pp. 180-189
    • Veaute, X.1    Delmas, S.2    Selva, M.3    Jeusset, J.4    Le Cam, E.5    Matic, I.6    Fabre, F.7    Petit, M.A.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.