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Volumn 20, Issue 4, 2012, Pages 667-675

The structure of the XPF-ssDNA complex underscores the distinct roles of the XPF and ERCC1 helix-hairpin-helix domains in ss/ds DNA recognition

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBONUCLEASE; DEOXYRIBONUCLEOPROTEIN; EXCISION REPAIR CROSS COMPLEMENTING PROTEIN 1; HETERODIMER; HOMODIMER; PROTEIN XPF; UNCLASSIFIED DRUG;

EID: 84859377849     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2012.02.009     Document Type: Article
Times cited : (22)

References (54)
  • 2
    • 38349098477 scopus 로고    scopus 로고
    • The ERCC1/XPF endonuclease is required for efficient single-strand annealing and gene conversion in mammalian cells
    • A.Z. Al-Minawi, N. Saleh-Gohari, and T. Helleday The ERCC1/XPF endonuclease is required for efficient single-strand annealing and gene conversion in mammalian cells Nucleic Acids Res. 36 2008 1 9
    • (2008) Nucleic Acids Res. , vol.36 , pp. 1-9
    • Al-Minawi, A.Z.1    Saleh-Gohari, N.2    Helleday, T.3
  • 4
    • 0031023182 scopus 로고    scopus 로고
    • Reconstitution of human excision nuclease with recombinant XPF-ERCC1 complex
    • T. Bessho, A. Sancar, L.H. Thompson, and M.P. Thelen Reconstitution of human excision nuclease with recombinant XPF-ERCC1 complex J. Biol. Chem. 272 1997 3833 3837
    • (1997) J. Biol. Chem. , vol.272 , pp. 3833-3837
    • Bessho, T.1    Sancar, A.2    Thompson, L.H.3    Thelen, M.P.4
  • 5
    • 0031030449 scopus 로고    scopus 로고
    • Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
    • A. Bochkarev, R.A. Pfuetzner, A.M. Edwards, and L. Frappier Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA Nature 385 1997 176 181
    • (1997) Nature , vol.385 , pp. 176-181
    • Bochkarev, A.1    Pfuetzner, R.A.2    Edwards, A.M.3    Frappier, L.4
  • 6
    • 0036646504 scopus 로고    scopus 로고
    • Molecular basis of sequence-specific single-stranded DNA recognition by KH domains: Solution structure of a complex between hnRNP K KH3 and single-stranded DNA
    • D.T. Braddock, J.L. Baber, D. Levens, and G.M. Clore Molecular basis of sequence-specific single-stranded DNA recognition by KH domains: solution structure of a complex between hnRNP K KH3 and single-stranded DNA EMBO J. 21 2002 3476 3485
    • (2002) EMBO J. , vol.21 , pp. 3476-3485
    • Braddock, D.T.1    Baber, J.L.2    Levens, D.3    Clore, G.M.4
  • 7
    • 0037186549 scopus 로고    scopus 로고
    • Structure and dynamics of KH domains from FBP bound to single-stranded DNA
    • D.T. Braddock, J.M. Louis, J.L. Baber, D. Levens, and G.M. Clore Structure and dynamics of KH domains from FBP bound to single-stranded DNA Nature 415 2002 1051 1056
    • (2002) Nature , vol.415 , pp. 1051-1056
    • Braddock, D.T.1    Louis, J.M.2    Baber, J.L.3    Levens, D.4    Clore, G.M.5
  • 10
    • 44349162159 scopus 로고    scopus 로고
    • Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures
    • 489-4
    • Z. Chen, H. Yang, and N.P. Pavletich Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures Nature 453 2008 489-4
    • (2008) Nature , vol.453
    • Chen, Z.1    Yang, H.2    Pavletich, N.P.3
  • 11
    • 23344452570 scopus 로고    scopus 로고
    • Biophysical characterization of the interaction domains and mapping of the contact residues in the XPF-ERCC1 complex
    • Y.J. Choi, K.S. Ryu, Y.M. Ko, Y.K. Chae, J.G. Pelton, D.E. Wemmer, and B.S. Choi Biophysical characterization of the interaction domains and mapping of the contact residues in the XPF-ERCC1 complex J. Biol. Chem. 280 2005 28644 28652
    • (2005) J. Biol. Chem. , vol.280 , pp. 28644-28652
    • Choi, Y.J.1    Ryu, K.S.2    Ko, Y.M.3    Chae, Y.K.4    Pelton, J.G.5    Wemmer, D.E.6    Choi, B.S.7
  • 12
    • 20844442267 scopus 로고    scopus 로고
    • The XPF-ERCC1 endonuclease and homologous recombination contribute to the repair of minor groove DNA interstrand crosslinks in mammalian cells produced by the pyrrolo[2,1-c][1,4]benzodiazepine dimer SJG-136
    • P.H. Clingen, I.U. De Silva, P.J. McHugh, F.J. Ghadessy, M.J. Tilby, D.E. Thurston, and J.A. Hartley The XPF-ERCC1 endonuclease and homologous recombination contribute to the repair of minor groove DNA interstrand crosslinks in mammalian cells produced by the pyrrolo[2,1-c][1,4]benzodiazepine dimer SJG-136 Nucleic Acids Res. 33 2005 3283 3291
    • (2005) Nucleic Acids Res. , vol.33 , pp. 3283-3291
    • Clingen, P.H.1    De Silva, I.U.2    McHugh, P.J.3    Ghadessy, F.J.4    Tilby, M.J.5    Thurston, D.E.6    Hartley, J.A.7
  • 14
  • 15
    • 0032529167 scopus 로고    scopus 로고
    • DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair
    • W.L. de Laat, E. Appeldoorn, K. Sugasawa, E. Weterings, N.G. Jaspers, and J.H. Hoeijmakers DNA-binding polarity of human replication protein A positions nucleases in nucleotide excision repair Genes Dev. 12 1998 2598 2609
    • (1998) Genes Dev. , vol.12 , pp. 2598-2609
    • De Laat, W.L.1    Appeldoorn, E.2    Sugasawa, K.3    Weterings, E.4    Jaspers, N.G.5    Hoeijmakers, J.H.6
  • 19
    • 0037090816 scopus 로고    scopus 로고
    • The active site of the DNA repair endonuclease XPF-ERCC1 forms a highly conserved nuclease motif
    • J.H. Enzlin, and O.D. Schärer The active site of the DNA repair endonuclease XPF-ERCC1 forms a highly conserved nuclease motif EMBO J. 21 2002 2045 2053
    • (2002) EMBO J. , vol.21 , pp. 2045-2053
    • Enzlin, J.H.1    Schärer, O.D.2
  • 20
    • 0035865927 scopus 로고    scopus 로고
    • Activity of individual ERCC1 and XPF subunits in DNA nucleotide excision repair
    • P.H. Gaillard, and R.D. Wood Activity of individual ERCC1 and XPF subunits in DNA nucleotide excision repair Nucleic Acids Res. 29 2001 872 879
    • (2001) Nucleic Acids Res. , vol.29 , pp. 872-879
    • Gaillard, P.H.1    Wood, R.D.2
  • 21
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • T. Herrmann, P. Güntert, and K. Wüthrich Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA J. Mol. Biol. 319 2002 209 227
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 22
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • J.H.J. Hoeijmakers Genome maintenance mechanisms for preventing cancer Nature 411 2001 366 374
    • (2001) Nature , vol.411 , pp. 366-374
    • Hoeijmakers, J.H.J.1
  • 25
    • 0037526104 scopus 로고    scopus 로고
    • Insights into ssDNA recognition by the OB fold from a structural and thermodynamic study of Sulfolobus SSB protein
    • I.D. Kerr, R.I. Wadsworth, L. Cubeddu, W. Blankenfeldt, J.H. Naismith, and M.F. White Insights into ssDNA recognition by the OB fold from a structural and thermodynamic study of Sulfolobus SSB protein EMBO J. 22 2003 2561 2570
    • (2003) EMBO J. , vol.22 , pp. 2561-2570
    • Kerr, I.D.1    Wadsworth, R.I.2    Cubeddu, L.3    Blankenfeldt, W.4    Naismith, J.H.5    White, M.F.6
  • 26
    • 0034714401 scopus 로고    scopus 로고
    • Repair of an interstrand DNA cross-link initiated by ERCC1-XPF repair/recombination nuclease
    • I. Kuraoka, W.R. Kobertz, R.R. Ariza, M. Biggerstaff, J.M. Essigmann, and R.D. Wood Repair of an interstrand DNA cross-link initiated by ERCC1-XPF repair/recombination nuclease J. Biol. Chem. 275 2000 26632 26636
    • (2000) J. Biol. Chem. , vol.275 , pp. 26632-26636
    • Kuraoka, I.1    Kobertz, W.R.2    Ariza, R.R.3    Biggerstaff, M.4    Essigmann, J.M.5    Wood, R.D.6
  • 27
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R.A. Laskowski, J.A. Rullmannn, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 28
    • 0027378895 scopus 로고
    • Mice with DNA repair gene (ERCC-1) deficiency have elevated levels of p53, liver nuclear abnormalities and die before weaning
    • J. McWhir, J. Selfridge, D.J. Harrison, S. Squires, and D.W. Melton Mice with DNA repair gene (ERCC-1) deficiency have elevated levels of p53, liver nuclear abnormalities and die before weaning Nat. Genet. 5 1993 217 224
    • (1993) Nat. Genet. , vol.5 , pp. 217-224
    • McWhir, J.1    Selfridge, J.2    Harrison, D.J.3    Squires, S.4    Melton, D.W.5
  • 31
    • 27144515686 scopus 로고    scopus 로고
    • XPF nuclease-dependent telomere loss and increased DNA damage in mice overexpressing TRF2 result in premature aging and cancer
    • P. Muñoz, R. Blanco, J.M. Flores, and M.A. Blasco XPF nuclease-dependent telomere loss and increased DNA damage in mice overexpressing TRF2 result in premature aging and cancer Nat. Genet. 37 2005 1063 1071
    • (2005) Nat. Genet. , vol.37 , pp. 1063-1071
    • Muñoz, P.1    Blanco, R.2    Flores, J.M.3    Blasco, M.A.4
  • 35
    • 77950487121 scopus 로고    scopus 로고
    • The XPA-binding domain of ERCC1 is required for nucleotide excision repair but not other DNA repair pathways
    • B. Orelli, T.B. McClendon, O.V. Tsodikov, T. Ellenberger, L.J. Niedernhofer, and O.D. Scharer The XPA-binding domain of ERCC1 is required for nucleotide excision repair but not other DNA repair pathways J. Biol. Chem. 285 2009 3705 3712
    • (2009) J. Biol. Chem. , vol.285 , pp. 3705-3712
    • Orelli, B.1    McClendon, T.B.2    Tsodikov, O.V.3    Ellenberger, T.4    Niedernhofer, L.J.5    Scharer, O.D.6
  • 36
    • 0029095693 scopus 로고
    • Purification and characterization of the XPF-ERCC1 complex of human DNA repair excision nuclease
    • C.H. Park, T. Bessho, T. Matsunaga, and A. Sancar Purification and characterization of the XPF-ERCC1 complex of human DNA repair excision nuclease J. Biol. Chem. 270 1995 22657 22660
    • (1995) J. Biol. Chem. , vol.270 , pp. 22657-22660
    • Park, C.H.1    Bessho, T.2    Matsunaga, T.3    Sancar, A.4
  • 37
    • 0141753120 scopus 로고    scopus 로고
    • The comings and goings of nucleotide excision repair factors on damaged DNA
    • T. Riedl, F. Hanaoka, and J.M. Egly The comings and goings of nucleotide excision repair factors on damaged DNA EMBO J. 22 2003 5293 5303
    • (2003) EMBO J. , vol.22 , pp. 5293-5303
    • Riedl, T.1    Hanaoka, F.2    Egly, J.M.3
  • 38
    • 67449102263 scopus 로고    scopus 로고
    • Specificity and affinity of Lac repressor for the auxiliary operators O2 and O3 are explained by the structures of their protein-DNA complexes
    • J. Romanuka, G.E. Folkers, N. Biris, E. Tishchenko, H. Wienk, A.M. Bonvin, R. Kaptein, and R. Boelens Specificity and affinity of Lac repressor for the auxiliary operators O2 and O3 are explained by the structures of their protein-DNA complexes J. Mol. Biol. 390 2009 478 489
    • (2009) J. Mol. Biol. , vol.390 , pp. 478-489
    • Romanuka, J.1    Folkers, G.E.2    Biris, N.3    Tishchenko, E.4    Wienk, H.5    Bonvin, A.M.6    Kaptein, R.7    Boelens, R.8
  • 39
    • 24744447497 scopus 로고    scopus 로고
    • Altered specificity in DNA binding by the lac repressor: A mutant lac headpiece that mimics the gal repressor
    • R. Kopke Salinas, G.E. Folkers, A.M.J.J. Bonvin, D. Das, R. Boelens, and R. Kaptein Altered specificity in DNA binding by the lac repressor: a mutant lac headpiece that mimics the gal repressor Chem. Bio. Chem. 6 2005 1628 1637
    • (2005) Chem. Bio. Chem. , vol.6 , pp. 1628-1637
    • Kopke Salinas, R.1    Folkers, G.E.2    Bonvin, A.M.J.J.3    Das, D.4    Boelens, R.5    Kaptein, R.6
  • 40
    • 35348954826 scopus 로고    scopus 로고
    • Achieving broad substrate specificity in damage recognition by binding accessible nondamaged DNA
    • O.D. Schärer Achieving broad substrate specificity in damage recognition by binding accessible nondamaged DNA Mol. Cell 28 2007 184 186
    • (2007) Mol. Cell , vol.28 , pp. 184-186
    • Schärer, O.D.1
  • 41
    • 0034661711 scopus 로고    scopus 로고
    • Common fold in helix-hairpin-helix proteins
    • X. Shao, and N.V. Grishin Common fold in helix-hairpin-helix proteins Nucleic Acids Res. 28 2000 2643 2650
    • (2000) Nucleic Acids Res. , vol.28 , pp. 2643-2650
    • Shao, X.1    Grishin, N.V.2
  • 44
    • 1542309071 scopus 로고    scopus 로고
    • Growth retardation, early death, and DNA repair defects in mice deficient for the nucleotide excision repair enzyme XPF
    • M. Tian, R. Shinkura, N. Shinkura, and F.W. Alt Growth retardation, early death, and DNA repair defects in mice deficient for the nucleotide excision repair enzyme XPF Mol. Cell. Biol. 24 2004 1200 1205
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 1200-1205
    • Tian, M.1    Shinkura, R.2    Shinkura, N.3    Alt, F.W.4
  • 45
    • 28844480409 scopus 로고    scopus 로고
    • The structure of the human ERCC1/XPF interaction domains reveals a complementary role for the two proteins in nucleotide excision repair
    • K. Tripsianes, G. Folkers, E. Ab, D. Das, H. Odijk, N.G. Jaspers, J.H. Hoeijmakers, R. Kaptein, and R. Boelens The structure of the human ERCC1/XPF interaction domains reveals a complementary role for the two proteins in nucleotide excision repair Structure 13 2005 1849 1858
    • (2005) Structure , vol.13 , pp. 1849-1858
    • Tripsianes, K.1    Folkers, G.2    Ab, E.3    Das, D.4    Odijk, H.5    Jaspers, N.G.6    Hoeijmakers, J.H.7    Kaptein, R.8    Boelens, R.9
  • 46
    • 34848864364 scopus 로고    scopus 로고
    • Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization
    • K. Tripsianes, G.E. Folkers, C. Zheng, D. Das, J.S. Grinstead, R. Kaptein, and R. Boelens Analysis of the XPA and ssDNA-binding surfaces on the central domain of human ERCC1 reveals evidence for subfunctionalization Nucleic Acids Res. 35 2007 5789 5798
    • (2007) Nucleic Acids Res. , vol.35 , pp. 5789-5798
    • Tripsianes, K.1    Folkers, G.E.2    Zheng, C.3    Das, D.4    Grinstead, J.S.5    Kaptein, R.6    Boelens, R.7
  • 47
    • 23844548251 scopus 로고    scopus 로고
    • Crystal structure and DNA binding functions of ERCC1, a subunit of the DNA structure-specific endonuclease XPF-ERCC1
    • O.V. Tsodikov, J.H. Enzlin, O.D. Schärer, and T. Ellenberger Crystal structure and DNA binding functions of ERCC1, a subunit of the DNA structure-specific endonuclease XPF-ERCC1 Proc. Natl. Acad. Sci. USA 102 2005 11236 11241
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 11236-11241
    • Tsodikov, O.V.1    Enzlin, J.H.2    Schärer, O.D.3    Ellenberger, T.4
  • 49
    • 33746285812 scopus 로고    scopus 로고
    • Information-driven protein-DNA docking using HADDOCK: It is a matter of flexibility
    • M. van Dijk, A.D.J. van Dijk, V. Hsu, R. Boelens, and A.M.J.J. Bonvin Information-driven protein-DNA docking using HADDOCK: it is a matter of flexibility Nucleic Acids Res. 34 2006 3317 3325
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3317-3325
    • Van Dijk, M.1    Van Dijk, A.D.J.2    Hsu, V.3    Boelens, R.4    Bonvin, A.M.J.J.5
  • 52
    • 32244438507 scopus 로고    scopus 로고
    • A global transcription cofactor bound to juxtaposed strands of unwound DNA
    • S. Werten, and D. Moras A global transcription cofactor bound to juxtaposed strands of unwound DNA Nat. Struct. Mol. Biol. 13 2006 181 182
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 181-182
    • Werten, S.1    Moras, D.2
  • 53
    • 0035830457 scopus 로고    scopus 로고
    • Novel functional interactions between nucleotide excision DNA repair proteins influencing the enzymatic activities of TFIIH, XPG, and ERCC1-XPF
    • G.S. Winkler, K. Sugasawa, A.P. Eker, W.L. de Laat, and J.H.J. Hoeijmakers Novel functional interactions between nucleotide excision DNA repair proteins influencing the enzymatic activities of TFIIH, XPG, and ERCC1-XPF Biochemistry 40 2001 160 165
    • (2001) Biochemistry , vol.40 , pp. 160-165
    • Winkler, G.S.1    Sugasawa, K.2    Eker, A.P.3    De Laat, W.L.4    Hoeijmakers, J.H.J.5
  • 54
    • 54249112218 scopus 로고    scopus 로고
    • Human XPF controls TRF2 and telomere length maintenance through distinctive mechanisms
    • Y. Wu, T.R. Mitchell, and X.D. Zhu Human XPF controls TRF2 and telomere length maintenance through distinctive mechanisms Mech. Ageing Dev. 129 2008 602 610
    • (2008) Mech. Ageing Dev. , vol.129 , pp. 602-610
    • Wu, Y.1    Mitchell, T.R.2    Zhu, X.D.3


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