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Volumn 13, Issue 8, 2005, Pages 1173-1182

Conferring substrate specificity to DNA helicases: Role of the RecQ HRDC domain

Author keywords

[No Author keywords available]

Indexed keywords

RECQ HELICASE;

EID: 23444440610     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2005.04.018     Document Type: Article
Times cited : (79)

References (44)
  • 1
    • 0141567744 scopus 로고    scopus 로고
    • RecQ helicases: Suppressors of tumorigenesis and premature aging
    • C.Z. Bachrati, and I.D. Hickson 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
  • 3
    • 0032540283 scopus 로고    scopus 로고
    • Purification and characterization of the Sgs1 DNA helicase activity of Saccharomyces cerevisiae
    • R.J. Bennett, J.A. Sharp, and J.C. Wang Purification and characterization of the Sgs1 DNA helicase activity of Saccharomyces cerevisiae J. Biol. Chem. 273 1998 9644 9650
    • (1998) J. Biol. Chem. , vol.273 , pp. 9644-9650
    • Bennett, R.J.1    Sharp, J.A.2    Wang, J.C.3
  • 4
    • 0037930738 scopus 로고    scopus 로고
    • Domain mapping of Escherichia coli RecQ defines the roles of conserved N- and C-terminal regions in the RecQ family
    • D.A. Bernstein, and J.L. Keck Domain mapping of Escherichia coli RecQ defines the roles of conserved N- and C-terminal regions in the RecQ family Nucleic Acids Res. 31 2003 2778 2785
    • (2003) Nucleic Acids Res. , vol.31 , pp. 2778-2785
    • Bernstein, D.A.1    Keck, J.L.2
  • 5
    • 0141865522 scopus 로고    scopus 로고
    • High-resolution structure of the E. coli RecQ helicase catalytic core
    • D.A. Bernstein, M.C. Zittel, and J.L. Keck 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
  • 6
    • 0032740855 scopus 로고    scopus 로고
    • RecQ and RecJ process blocked replication forks prior to the resumption of replication in UV-irradiated Escherichia coli
    • J. Courcelle, and P.C. Hanawalt RecQ and RecJ process blocked replication forks prior to the resumption of replication in UV-irradiated Escherichia coli Mol. Gen. Genet. 262 1999 543 551
    • (1999) Mol. Gen. Genet. , vol.262 , pp. 543-551
    • Courcelle, J.1    Hanawalt, P.C.2
  • 9
    • 1342346600 scopus 로고    scopus 로고
    • The DNA binding properties of the Escherichia coli RecQ helicase
    • S.X. Dou, P.Y. Wang, H.Q. Xu, and X.G. Xi The DNA binding properties of the Escherichia coli RecQ helicase J. Biol. Chem. 279 2004 6354 6363
    • (2004) J. Biol. Chem. , vol.279 , pp. 6354-6363
    • Dou, S.X.1    Wang, P.Y.2    Xu, H.Q.3    X G. Xi4
  • 10
    • 0014109212 scopus 로고
    • Spectroscopic determination of tryptophan and tyrosine in proteins
    • H. Edelhoch Spectroscopic determination of tryptophan and tyrosine in proteins Biochemistry 6 1967 1948 1954
    • (1967) Biochemistry , vol.6 , pp. 1948-1954
    • Edelhoch, H.1
  • 12
    • 0030888233 scopus 로고    scopus 로고
    • RecQ DNA helicase is a suppressor of illegitimate recombination in Escherichia coli
    • K. Hanada, T. Ukita, Y. Kohno, K. Saito, J. Kato, and H. Ikeda RecQ DNA helicase is a suppressor of illegitimate recombination in Escherichia coli Proc. Natl. Acad. Sci. USA 94 1997 3860 3865
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3860-3865
    • Hanada, K.1    Ukita, T.2    Kohno, Y.3    Saito, K.4    Kato, J.5    Ikeda, H.6
  • 13
    • 0032522789 scopus 로고    scopus 로고
    • RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination
    • F.G. Harmon, and S.C. Kowalczykowski RecQ helicase, in concert with RecA and SSB proteins, initiates and disrupts DNA recombination Genes Dev. 12 1998 1134 1144
    • (1998) Genes Dev. , vol.12 , pp. 1134-1144
    • Harmon, F.G.1    Kowalczykowski, S.C.2
  • 14
    • 0035808456 scopus 로고    scopus 로고
    • Biochemical characterization of the DNA helicase activity of the Escherichia coli RecQ helicase
    • F.G. Harmon, and S.C. Kowalczykowski Biochemical characterization of the DNA helicase activity of the Escherichia coli RecQ helicase J. Biol. Chem. 276 2001 232 243
    • (2001) J. Biol. Chem. , vol.276 , pp. 232-243
    • Harmon, F.G.1    Kowalczykowski, S.C.2
  • 15
    • 0033031935 scopus 로고    scopus 로고
    • RecQ helicase and topoisomerase III comprise a novel DNA strand passage function: A conserved mechanism for control of DNA recombination
    • F.G. Harmon, R.J. DiGate, and S.C. Kowalczykowski RecQ helicase and topoisomerase III comprise a novel DNA strand passage function: a conserved mechanism for control of DNA recombination Mol. Cell 3 1999 611 620
    • (1999) Mol. Cell , vol.3 , pp. 611-620
    • Harmon, F.G.1    Digate, R.J.2    Kowalczykowski, S.C.3
  • 16
    • 3543089707 scopus 로고    scopus 로고
    • Role of the Escherichia coli RecQ DNA helicase in SOS signaling and genome stabilization at stalled replication forks
    • T. Hishida, Y.W. Han, T. Shibata, Y. Kubota, Y. Ishino, H. Iwasaki, and H. Shinagawa Role of the Escherichia coli RecQ DNA helicase in SOS signaling and genome stabilization at stalled replication forks Genes Dev. 18 2004 1886 1897
    • (2004) Genes Dev. , vol.18 , pp. 1886-1897
    • Hishida, T.1    Han, Y.W.2    Shibata, T.3    Kubota, Y.4    Ishino, Y.5    Iwasaki, H.6    Shinagawa, H.7
  • 17
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • L. Holm, and C. Sander Protein structure comparison by alignment of distance matrices J. Mol. Biol. 233 1993 123 138
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 18
    • 0015817690 scopus 로고
    • Genetic analysis of the recF pathway to genetic recombination in Escherichia coli K12: Isolation and characterization of mutants
    • Z. Horii, and A.J. Clark Genetic analysis of the recF pathway to genetic recombination in Escherichia coli K12: isolation and characterization of mutants J. Mol. Biol. 80 1973 327 344
    • (1973) J. Mol. Biol. , vol.80 , pp. 327-344
    • Horii, Z.1    Clark, A.J.2
  • 20
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.Y. Zou, and S.W. Cowan Improved methods for binding protein models in electron density maps and the location of errors in these models Acta Crystallogr. A 47 (Pt 2) 1991 110 119
    • (1991) Acta Crystallogr. a , vol.472 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3
  • 22
    • 0021962878 scopus 로고
    • Genetic recombination of bacterial plasmid DNA: Effect of RecF pathway mutations on plasmid recombination in Escherichia coli
    • R. Kolodner, R.A. Fishel, and M. Howard Genetic recombination of bacterial plasmid DNA: effect of RecF pathway mutations on plasmid recombination in Escherichia coli J. Bacteriol. 163 1985 1060 1066
    • (1985) J. Bacteriol. , vol.163 , pp. 1060-1066
    • Kolodner, R.1    Fishel, R.A.2    Howard, M.3
  • 23
    • 0030740262 scopus 로고    scopus 로고
    • Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP
    • S. Korolev, J. Hsieh, G.H. Gauss, T.M. Lohman, and G. Waksman Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP Cell 90 1997 635 647
    • (1997) Cell , vol.90 , pp. 635-647
    • Korolev, S.1    Hsieh, J.2    Gauss, G.H.3    Lohman, T.M.4    Waksman, G.5
  • 26
  • 28
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • B.W. Matthews Solvent content of protein crystals J. Mol. Biol. 33 1968 491 497
    • (1968) J. Mol. Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 29
    • 0030697336 scopus 로고    scopus 로고
    • A putative nucleic acid-binding domain in Bloom's and Werner's syndrome helicases
    • V. Morozov, A.R. Mushegian, E.V. Koonin, and P. Bork 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
  • 30
    • 0021185614 scopus 로고
    • Isolation and genetic characterization of a thymineless death-resistant mutant of Escherichia coli K12: Identification of a new mutation (recQ1) that blocks the RecF recombination pathway
    • H. Nakayama, K. Nakayama, R. Nakayama, N. Irino, Y. Nakayama, and P.C. Hanawalt Isolation and genetic characterization of a thymineless death-resistant mutant of Escherichia coli K12: identification of a new mutation (recQ1) that blocks the RecF recombination pathway Mol. Gen. Genet. 195 1984 474 480
    • (1984) Mol. Gen. Genet. , vol.195 , pp. 474-480
    • Nakayama, H.1    Nakayama, K.2    Nakayama, R.3    Irino, N.4    Nakayama, Y.5    Hanawalt, P.C.6
  • 31
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • A. Nicholls, K.A. Sharp, and B. Honig Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons Proteins 11 1991 281 296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 33
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • C.W. Carter R.M. Sweet Academic Press New York
    • Z. Otwinowski, and W. Minor Processing of X-ray diffraction data collected in oscillation mode C.W. Carter R.M. Sweet Methods in Enzymology 1997 Academic Press New York 307 326
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 34
    • 0028049441 scopus 로고
    • Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP
    • H. Pelletier, M.R. Sawaya, A. Kumar, S.H. Wilson, and J. Kraut Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP Science 264 1994 1891 1903
    • (1994) Science , vol.264 , pp. 1891-1903
    • Pelletier, H.1    Sawaya, M.R.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 38
    • 0027439390 scopus 로고
    • Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin
    • G.D. Van Duyne, R.F. Standaert, P.A. Karplus, S.L. Schreiber, and J. Clardy Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin J. Mol. Biol. 229 1993 105 124
    • (1993) J. Mol. Biol. , vol.229 , pp. 105-124
    • Van Duyne, G.D.1    Standaert, R.F.2    Karplus, P.A.3    Schreiber, S.L.4    Clardy, J.5
  • 39
    • 0033515425 scopus 로고    scopus 로고
    • Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism
    • S.S. Velankar, P. Soultanas, M.S. Dillingham, H.S. Subramanya, and D.B. Wigley Crystal structures of complexes of PcrA DNA helicase with a DNA substrate indicate an inchworm mechanism Cell 97 1999 75 84
    • (1999) Cell , vol.97 , pp. 75-84
    • Velankar, S.S.1    Soultanas, P.2    Dillingham, M.S.3    Subramanya, H.S.4    Wigley, D.B.5
  • 40
    • 0347362703 scopus 로고    scopus 로고
    • Werner syndrome protein contains three structure-specific DNA binding domains
    • C. von Kobbe, N.H. Thoma, B.K. Czyzewski, N.P. Pavletich, and V.A. Bohr Werner syndrome protein contains three structure-specific DNA binding domains J. Biol. Chem. 278 2003 52997 53006
    • (2003) J. Biol. Chem. , vol.278 , pp. 52997-53006
    • Von Kobbe, C.1    Thoma, N.H.2    Czyzewski, B.K.3    Pavletich, N.P.4    Bohr, V.A.5
  • 41
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • M.D. Winn, M.N. Isupov, and G.N. Murshudov Use of TLS parameters to model anisotropic displacements in macromolecular refinement Acta Crystallogr. D Biol. Crystallogr. 57 2001 122 133
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 44
    • 0031919820 scopus 로고    scopus 로고
    • Binding to four-way junction DNA: A common property of architectural proteins?
    • J. Zlatanova, and K. van Holde Binding to four-way junction DNA: a common property of architectural proteins? FASEB J. 12 1998 421 431
    • (1998) FASEB J. , vol.12 , pp. 421-431
    • Zlatanova, J.1    Van Holde, K.2


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