메뉴 건너뛰기




Volumn 4, Issue 8, 2005, Pages 855-869

Repair of UV lesions in nucleosomes - Intrinsic properties and remodeling

Author keywords

Chromatin; Nucleosomes; Nucleotide excision repair; Photolyase

Indexed keywords

DEOXYRIBODIPYRIMIDINE PHOTOLYASE; DNA;

EID: 21844442362     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2005.04.005     Document Type: Review
Times cited : (58)

References (163)
  • 1
    • 0033529565 scopus 로고    scopus 로고
    • Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome
    • R.D. Kornberg, and Y. Lorch Twenty-five years of the nucleosome, fundamental particle of the eukaryote chromosome Cell 98 1999 285 294
    • (1999) Cell , vol.98 , pp. 285-294
    • Kornberg, R.D.1    Lorch, Y.2
  • 2
    • 0030726678 scopus 로고    scopus 로고
    • Gene activation at a distance and telomeric silencing are not affected by yeast histone H1
    • D. Escher, and W. Schaffner Gene activation at a distance and telomeric silencing are not affected by yeast histone H1 Mol. Gen. Genet. 256 1997 456 461
    • (1997) Mol. Gen. Genet. , vol.256 , pp. 456-461
    • Escher, D.1    Schaffner, W.2
  • 3
    • 0032571258 scopus 로고    scopus 로고
    • The biochemical and phenotypic characterization of Hhoip, the putative linker histone H1 of Saccharomyces cerevisiae
    • H.G. Patterton, C.C. Landel, D. Landsman, C.L. Peterson, and R.T. Simpson The biochemical and phenotypic characterization of Hhoip, the putative linker histone H1 of Saccharomyces cerevisiae J. Biol. Chem. 273 1998 7268 7276
    • (1998) J. Biol. Chem. , vol.273 , pp. 7268-7276
    • Patterton, H.G.1    Landel, C.C.2    Landsman, D.3    Peterson, C.L.4    Simpson, R.T.5
  • 4
    • 0037490067 scopus 로고    scopus 로고
    • Suppression of homologous recombination by the Saccharomyces cerevisiae linker histone
    • J.A. Downs, E. Kosmidou, A. Morgan, and S.P. Jackson Suppression of homologous recombination by the Saccharomyces cerevisiae linker histone Mol. Cell 11 2003 1685 1692
    • (2003) Mol. Cell , vol.11 , pp. 1685-1692
    • Downs, J.A.1    Kosmidou, E.2    Morgan, A.3    Jackson, S.P.4
  • 5
    • 0242407193 scopus 로고    scopus 로고
    • Phylogenomics of the nucleosome
    • H.S. Malik, and S. Henikoff Phylogenomics of the nucleosome Nat. Struct. Biol. 10 2003 882 891
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 882-891
    • Malik, H.S.1    Henikoff, S.2
  • 6
    • 0037383755 scopus 로고    scopus 로고
    • Anti-silencing from the core: A histone H2A variant protects euchromatin
    • M. Hild, and R. Paro Anti-silencing from the core: a histone H2A variant protects euchromatin Nat. Cell. Biol. 5 2003 278 280
    • (2003) Nat. Cell. Biol. , vol.5 , pp. 278-280
    • Hild, M.1    Paro, R.2
  • 7
    • 0034610814 scopus 로고    scopus 로고
    • The language of covalent histone modifications
    • B.D. Strahl, and C.D. Allis The language of covalent histone modifications Nature 403 2000 41 45
    • (2000) Nature , vol.403 , pp. 41-45
    • Strahl, B.D.1    Allis, C.D.2
  • 9
    • 0031831516 scopus 로고    scopus 로고
    • Structure, dynamics, and function of chromatin in vitro
    • J. Widom Structure, dynamics, and function of chromatin in vitro Annu. Rev. Biophys. Biomol. Struct. 27 1998 285 327
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 285-327
    • Widom, J.1
  • 10
    • 0037154963 scopus 로고    scopus 로고
    • Cooperation between complexes that regulate chromatin structure and transcription
    • G.J. Narlikar, H.Y. Fan, and R.E. Kingston Cooperation between complexes that regulate chromatin structure and transcription Cell 108 2002 475 487
    • (2002) Cell , vol.108 , pp. 475-487
    • Narlikar, G.J.1    Fan, H.Y.2    Kingston, R.E.3
  • 11
  • 12
  • 13
    • 0033486110 scopus 로고    scopus 로고
    • Light and dark in chromatin repair: Repair of UV-induced DNA lesions by photolyase and nucleotide excision repair
    • F. Thoma Light and dark in chromatin repair: repair of UV-induced DNA lesions by photolyase and nucleotide excision repair EMBO J. 18 1999 6585 6598
    • (1999) EMBO J. , vol.18 , pp. 6585-6598
    • Thoma, F.1
  • 14
    • 0942300667 scopus 로고    scopus 로고
    • Repairing DNA damage in chromatin
    • A.M. Gontijo, C.M. Green, and G. Almouzni Repairing DNA damage in chromatin Biochimie 85 2003 1133 1147
    • (2003) Biochimie , vol.85 , pp. 1133-1147
    • Gontijo, A.M.1    Green, C.M.2    Almouzni, G.3
  • 15
    • 11144357255 scopus 로고    scopus 로고
    • Cellular machineries for chromosomal DNA repair
    • C.L. Peterson, and J. Cote Cellular machineries for chromosomal DNA repair Genes Dev. 18 2004 602 616
    • (2004) Genes Dev. , vol.18 , pp. 602-616
    • Peterson, C.L.1    Cote, J.2
  • 16
    • 0038557114 scopus 로고    scopus 로고
    • Who's on first in the cellular response to DNA damage?
    • S.D. Cline, and P.C. Hanawalt Who's on first in the cellular response to DNA damage? Nat. Rev. Mol. Cell Biol. 4 2003 361 372
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 361-372
    • Cline, S.D.1    Hanawalt, P.C.2
  • 18
    • 0021760689 scopus 로고
    • Structure of the nucleosome core particle at 7 a resolution
    • T.J. Richmond, J.T. Finch, B. Rushton, D. Rhodes, and A. Klug Structure of the nucleosome core particle at 7 A resolution Nature 311 1984 532 537
    • (1984) Nature , vol.311 , pp. 532-537
    • Richmond, T.J.1    Finch, J.T.2    Rushton, B.3    Rhodes, D.4    Klug, A.5
  • 19
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 a resolution
    • K. Luger, A.W. Mader, R.K. Richmond, D.F. Sargent, and T.J. Richmond Crystal structure of the nucleosome core particle at 2.8 A resolution Nature 389 1997 251 260
    • (1997) Nature , vol.389 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 20
    • 0037992395 scopus 로고    scopus 로고
    • The structure of DNA in the nucleosome core
    • T.J. Richmond, and C.A. Davey The structure of DNA in the nucleosome core Nature 423 2003 145 150
    • (2003) Nature , vol.423 , pp. 145-150
    • Richmond, T.J.1    Davey, C.A.2
  • 22
    • 0035903534 scopus 로고    scopus 로고
    • Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions
    • C.L. White, R.K. Suto, and K. Luger Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions EMBO J. 20 2001 5207 5218
    • (2001) EMBO J. , vol.20 , pp. 5207-5218
    • White, C.L.1    Suto, R.K.2    Luger, K.3
  • 23
    • 0033664380 scopus 로고    scopus 로고
    • Crystal structure of a nucleosome core particle containing the variant histone H2A.Z
    • R.K. Suto, M.J. Clarkson, D.J. Tremethick, and K. Luger Crystal structure of a nucleosome core particle containing the variant histone H2A.Z Nat. Struct. Biol. 7 2000 1121 1124
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 1121-1124
    • Suto, R.K.1    Clarkson, M.J.2    Tremethick, D.J.3    Luger, K.4
  • 24
    • 0037423930 scopus 로고    scopus 로고
    • Conserved Histone Variant H2A.Z Protects Euchromatin from the Ectopic Spread of Silent Heterochromatin
    • M.D. Meneghini, M. Wu, and H.D. Madhani Conserved Histone Variant H2A.Z Protects Euchromatin from the Ectopic Spread of Silent Heterochromatin Cell 112 2003 725 736
    • (2003) Cell , vol.112 , pp. 725-736
    • Meneghini, M.D.1    Wu, M.2    Madhani, H.D.3
  • 25
    • 0028801404 scopus 로고
    • Amino acid substitutions in the structured domains of histones H3 and H4 partially relieve the requirement of the yeast SWI/SNF complex for transcription
    • W. Kruger, C.L. Peterson, A. Sil, C. Coburn, G. Arents, E.N. Moudrianakis, and I. Herskowitz Amino acid substitutions in the structured domains of histones H3 and H4 partially relieve the requirement of the yeast SWI/SNF complex for transcription Genes Dev. 9 1995 2770 2779
    • (1995) Genes Dev. , vol.9 , pp. 2770-2779
    • Kruger, W.1    Peterson, C.L.2    Sil, A.3    Coburn, C.4    Arents, G.5    Moudrianakis, E.N.6    Herskowitz, I.7
  • 28
    • 0018801479 scopus 로고
    • Mechanism of a reversible, thermally induced conformational change in chromatin core particles
    • R.T. Simpson Mechanism of a reversible, thermally induced conformational change in chromatin core particles J. Biol. Chem. 254 1979 10123 10127
    • (1979) J. Biol. Chem. , vol.254 , pp. 10123-10127
    • Simpson, R.T.1
  • 29
    • 0021101211 scopus 로고
    • Periodicity of exonuclease III digestion of chromatin and the pitch of deoxyribonucleic acid on the nucleosome
    • A. Prunell Periodicity of exonuclease III digestion of chromatin and the pitch of deoxyribonucleic acid on the nucleosome Biochemistry 22 1983 4887 4894
    • (1983) Biochemistry , vol.22 , pp. 4887-4894
    • Prunell, A.1
  • 30
    • 0028850059 scopus 로고
    • Overcoming a nucleosomal barrier to transcription
    • V.M. Studitsky, D.J. Clark, and G. Felsenfeld Overcoming a nucleosomal barrier to transcription Cell 83 1995 19 27
    • (1995) Cell , vol.83 , pp. 19-27
    • Studitsky, V.M.1    Clark, D.J.2    Felsenfeld, G.3
  • 31
    • 0034598944 scopus 로고    scopus 로고
    • Sequence and position-dependence of the equilibrium accessibility of nucleosomal DNA target sites
    • J.D. Anderson, and J. Widom Sequence and position-dependence of the equilibrium accessibility of nucleosomal DNA target sites J. Mol. Biol. 296 2000 979 987
    • (2000) J. Mol. Biol. , vol.296 , pp. 979-987
    • Anderson, J.D.1    Widom, J.2
  • 32
    • 4344662581 scopus 로고    scopus 로고
    • A 'one-pot' assay for the accessibility of DNA in a nucleosome core particle
    • C. Wu, and A. Travers A 'one-pot' assay for the accessibility of DNA in a nucleosome core particle Nucl. Acids Res. 32 2004 e122
    • (2004) Nucl. Acids Res. , vol.32 , pp. 122
    • Wu, C.1    Travers, A.2
  • 33
    • 3542998667 scopus 로고    scopus 로고
    • Nucleosomes facilitate their own invasion
    • G. Li, and J. Widom Nucleosomes facilitate their own invasion Nat. Struct. Mol. Biol. 11 2004 763 769
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 763-769
    • Li, G.1    Widom, J.2
  • 34
    • 0018036889 scopus 로고
    • Mobility of histones on the chromosome of simian virus 40
    • P. Beard Mobility of histones on the chromosome of simian virus 40 Cell 15 1978 955 967
    • (1978) Cell , vol.15 , pp. 955-967
    • Beard, P.1
  • 35
    • 0020695571 scopus 로고
    • Structural features of a phased nucleosome core particle
    • R.T. Simpson, and D.W. Stafford Structural features of a phased nucleosome core particle Proc. Natl. Acad. Sci. U.S.A. 80 1983 51 55
    • (1983) Proc. Natl. Acad. Sci. U.S.A. , vol.80 , pp. 51-55
    • Simpson, R.T.1    Stafford, D.W.2
  • 36
  • 37
    • 0032559424 scopus 로고    scopus 로고
    • Positioning and stability of nucleosomes on MMTV 3′LTR sequences
    • A. Flaus, and T.J. Richmond Positioning and stability of nucleosomes on MMTV 3′LTR sequences J. Mol. Biol. 275 1998 427 441
    • (1998) J. Mol. Biol. , vol.275 , pp. 427-441
    • Flaus, A.1    Richmond, T.J.2
  • 38
    • 0026642219 scopus 로고
    • Mobile nucleosomes-a general behavior
    • G. Meersseman, S. Pennings, and E.M. Bradbury Mobile nucleosomes-a general behavior EMBO J. 11 1992 2951 2959
    • (1992) EMBO J. , vol.11 , pp. 2951-2959
    • Meersseman, G.1    Pennings, S.2    Bradbury, E.M.3
  • 39
    • 0024261880 scopus 로고
    • Statistical positioning of nucleosomes by specific protein-binding to an upstream activating sequence in yeast
    • M.J. Fedor, N.F. Lue, and R.D. Kornberg Statistical positioning of nucleosomes by specific protein-binding to an upstream activating sequence in yeast J. Mol. Biol. 204 1988 109 127
    • (1988) J. Mol. Biol. , vol.204 , pp. 109-127
    • Fedor, M.J.1    Lue, N.F.2    Kornberg, R.D.3
  • 40
    • 0021813437 scopus 로고
    • Local protein-DNA interactions may determine nucleosome positions on yeast plasmids
    • F. Thoma, and R.T. Simpson Local protein-DNA interactions may determine nucleosome positions on yeast plasmids Nature 315 1985 250 252
    • (1985) Nature , vol.315 , pp. 250-252
    • Thoma, F.1    Simpson, R.T.2
  • 41
    • 0023053638 scopus 로고
    • Protein-DNA interactions and nuclease-sensitive regions determine nucleosome positions on yeast plasmid chromatin
    • F. Thoma Protein-DNA interactions and nuclease-sensitive regions determine nucleosome positions on yeast plasmid chromatin J. Mol. Biol. 190 1986 177 190
    • (1986) J. Mol. Biol. , vol.190 , pp. 177-190
    • Thoma, F.1
  • 42
    • 0024207256 scopus 로고
    • Chromatin folding modulates nucleosome positioning in yeast minichromosomes
    • F. Thoma, and M. Zatchej Chromatin folding modulates nucleosome positioning in yeast minichromosomes Cell 55 1988 945 953
    • (1988) Cell , vol.55 , pp. 945-953
    • Thoma, F.1    Zatchej, M.2
  • 43
    • 0026561427 scopus 로고
    • Artificial nucleosome positioning sequences tested in yeast minichromosomes: A strong rotational setting is not sufficient to position nucleosomes in vivo
    • S. Tanaka, M. Zatchej, and F. Thoma Artificial nucleosome positioning sequences tested in yeast minichromosomes: a strong rotational setting is not sufficient to position nucleosomes in vivo EMBO J. 11 1992 1187 1193
    • (1992) EMBO J. , vol.11 , pp. 1187-1193
    • Tanaka, S.1    Zatchej, M.2    Thoma, F.3
  • 44
    • 0021613776 scopus 로고
    • Nucleosomes are positioned on mouse satellite DNA in multiple highly specific frames that are correlated with a diverged subrepeat of nine base-pairs
    • X.-Y. Zhang, and W. Hörz Nucleosomes are positioned on mouse satellite DNA in multiple highly specific frames that are correlated with a diverged subrepeat of nine base-pairs J. Mol. Biol. 176 1984 105 129
    • (1984) J. Mol. Biol. , vol.176 , pp. 105-129
    • Zhang, X.-Y.1    Hörz, W.2
  • 45
    • 0027360535 scopus 로고
    • Multiple nucleosome positioning with unique rotational setting for the Saccharomyces cerevisiae 5S rRNA gene in vitro and in vivo
    • M. Buttinelli, E. Di Mauro, and R. Negri Multiple nucleosome positioning with unique rotational setting for the Saccharomyces cerevisiae 5S rRNA gene in vitro and in vivo Proc. Natl. Acad. Sci. U.S.A. 90 1993 9315 9319
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 9315-9319
    • Buttinelli, M.1    Di Mauro, E.2    Negri, R.3
  • 46
    • 0029115016 scopus 로고
    • Nucleosome positioning on the MMTV LTR results from the frequency-biased occupancy of multiple frames
    • G. Fragoso, S. John, M.S. Roberts, and G.L. Hager Nucleosome positioning on the MMTV LTR results from the frequency-biased occupancy of multiple frames Genes Dev. 9 1995 1933 1947
    • (1995) Genes Dev. , vol.9 , pp. 1933-1947
    • Fragoso, G.1    John, S.2    Roberts, M.S.3    Hager, G.L.4
  • 47
    • 0029871340 scopus 로고    scopus 로고
    • Chromatin structure of the yeast URA3 gene at high resolution provides insight into structure and positioning of nucleosomes in the chromosomal context
    • S. Tanaka, M. Livingstone-Zatchej, and F. Thoma Chromatin structure of the yeast URA3 gene at high resolution provides insight into structure and positioning of nucleosomes in the chromosomal context J. Mol. Biol. 257 1996 919 934
    • (1996) J. Mol. Biol. , vol.257 , pp. 919-934
    • Tanaka, S.1    Livingstone-Zatchej, M.2    Thoma, F.3
  • 48
    • 0035997356 scopus 로고    scopus 로고
    • ATP-dependent nucleosome remodeling
    • P.B. Becker, and W. Horz ATP-dependent nucleosome remodeling Annu. Rev. Biochem. 71 2002 247 273
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 247-273
    • Becker, P.B.1    Horz, W.2
  • 49
    • 11144355550 scopus 로고    scopus 로고
    • SWRred not shaken; Mixing the histones
    • P. Korber, and W. Horz SWRred not shaken; mixing the histones Cell 117 2004 5 7
    • (2004) Cell , vol.117 , pp. 5-7
    • Korber, P.1    Horz, W.2
  • 50
    • 1942439629 scopus 로고    scopus 로고
    • Mechanisms for ATP-dependent chromatin remodelling: Farewell to the tuna-can octamer?
    • A. Flaus, and T. Owen-Hughes Mechanisms for ATP-dependent chromatin remodelling: farewell to the tuna-can octamer? Curr. Opin. Genet. Dev. 14 2004 165 173
    • (2004) Curr. Opin. Genet. Dev. , vol.14 , pp. 165-173
    • Flaus, A.1    Owen-Hughes, T.2
  • 51
    • 85015069067 scopus 로고    scopus 로고
    • Controlling the double helix
    • G. Felsenfeld, and M. Groudine Controlling the double helix Nature 421 2003 448 453
    • (2003) Nature , vol.421 , pp. 448-453
    • Felsenfeld, G.1    Groudine, M.2
  • 53
    • 0002541170 scopus 로고
    • Nucleosome motion: Evidence and models
    • C. Nicolini P.O.P. Ts'o Plenum Press New York, NY
    • K.E. Van Holde, and T.D. Yager Nucleosome motion: evidence and models C. Nicolini P.O.P. Ts'o Structure and Function of the Genetic Apparatus 1985 Plenum Press New York, NY 35 53
    • (1985) Structure and Function of the Genetic Apparatus , pp. 35-53
    • Van Holde, K.E.1    Yager, T.D.2
  • 54
    • 0037119967 scopus 로고    scopus 로고
    • Nucleosome sliding: Facts and fiction
    • P.B. Becker Nucleosome sliding: facts and fiction EMBO J. 21 2002 4749 4753
    • (2002) EMBO J. , vol.21 , pp. 4749-4753
    • Becker, P.B.1
  • 56
    • 0028927254 scopus 로고
    • The solution structure of DNA duplex- decamer containing the (6-4) photoproduct of thymidylyl(3′->5′)thymidine by NMR and relaxation matrix refinement
    • J.K. Kim, and B.S. Choi The solution structure of DNA duplex- decamer containing the (6-4) photoproduct of thymidylyl(3′->5′)thymidine by NMR and relaxation matrix refinement Eur. J. Biochem. 228 1995 849 854
    • (1995) Eur. J. Biochem. , vol.228 , pp. 849-854
    • Kim, J.K.1    Choi, B.S.2
  • 57
    • 0024844259 scopus 로고
    • Origin of ultraviolet damage in DNA
    • M.M. Becker, and Z. Wang Origin of ultraviolet damage in DNA J. Mol. Biol. 210 1989 429 438
    • (1989) J. Mol. Biol. , vol.210 , pp. 429-438
    • Becker, M.M.1    Wang, Z.2
  • 58
    • 0021190168 scopus 로고
    • Use of light for footprinting DNA in vivo
    • M.M. Becker, and J.C. Wang Use of light for footprinting DNA in vivo Nature 309 1984 682 687
    • (1984) Nature , vol.309 , pp. 682-687
    • Becker, M.M.1    Wang, J.C.2
  • 59
    • 0023135193 scopus 로고
    • Photofootprinting in vivo detects transcription-dependent changes in yeast TATA boxes
    • S.B. Selleck, and J. Majors Photofootprinting in vivo detects transcription-dependent changes in yeast TATA boxes Nature 325 1987 173 177
    • (1987) Nature , vol.325 , pp. 173-177
    • Selleck, S.B.1    Majors, J.2
  • 60
    • 0026566518 scopus 로고
    • Binding of transcription factors creates hot spots for UV photoproducts in vivo
    • G.P. Pfeifer, R. Drouin, A.D. Riggs, and G.P. Holmquist Binding of transcription factors creates hot spots for UV photoproducts in vivo Mol. Cell. Biol. 12 1992 1798 1804
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1798-1804
    • Pfeifer, G.P.1    Drouin, R.2    Riggs, A.D.3    Holmquist, G.P.4
  • 61
    • 0029058984 scopus 로고
    • UV light as a footprinting agent: Modulation of UV-induced DNA damage by transcription factors bound at the promoters of three human genes
    • S. Tornaletti, and G.P. Pfeifer UV light as a footprinting agent: modulation of UV-induced DNA damage by transcription factors bound at the promoters of three human genes J. Mol. Biol. 249 1995 714 728
    • (1995) J. Mol. Biol. , vol.249 , pp. 714-728
    • Tornaletti, S.1    Pfeifer, G.P.2
  • 62
    • 0023867502 scopus 로고
    • Selective visualization of gene structure with ultraviolet light
    • Z. Wang, and M.M. Becker Selective visualization of gene structure with ultraviolet light Proc. Natl. Acad. Sci. U.S.A. 85 1988 654 658
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 654-658
    • Wang, Z.1    Becker, M.M.2
  • 63
    • 0029939655 scopus 로고    scopus 로고
    • Modulation of cydobutane pyrimidine dimer formation in a positioned nucleosome containing poly(dA.dT) tracts
    • U. Schieferstein, and F. Thoma Modulation of cydobutane pyrimidine dimer formation in a positioned nucleosome containing poly(dA.dT) tracts Biochemistry 35 1996 7705 7714
    • (1996) Biochemistry , vol.35 , pp. 7705-7714
    • Schieferstein, U.1    Thoma, F.2
  • 64
    • 0032472378 scopus 로고    scopus 로고
    • Site-specific repair of cydobutane pyrimidine dimers in a positioned nucleosome by photolyase and T4 endonuclease V in vitro
    • U. Schieferstein, and F. Thoma Site-specific repair of cydobutane pyrimidine dimers in a positioned nucleosome by photolyase and T4 endonuclease V in vitro EMBO J. 17 1998 306 316
    • (1998) EMBO J. , vol.17 , pp. 306-316
    • Schieferstein, U.1    Thoma, F.2
  • 65
    • 0038381469 scopus 로고    scopus 로고
    • Chromatin remodeling activities act on UV-damaged nucleosomes and modulate DNA damage accessibility to photolyase
    • H. Gaillard, D.J. Fitzgerald, C.L. Smith, C.L. Peterson, T.J. Richmond, and F. Thoma Chromatin remodeling activities act on UV-damaged nucleosomes and modulate DNA damage accessibility to photolyase J. Biol. Chem. 278 2003 17655 17663
    • (2003) J. Biol. Chem. , vol.278 , pp. 17655-17663
    • Gaillard, H.1    Fitzgerald, D.J.2    Smith, C.L.3    Peterson, C.L.4    Richmond, T.J.5    Thoma, F.6
  • 66
    • 0005001210 scopus 로고
    • UV-induced formation of pyrimidine dimers in nucleosome core DNA is strongly modulated with a period of 10.3 bases
    • J.M. Gale, K.A. Nissen, and M.J. Smerdon UV-induced formation of pyrimidine dimers in nucleosome core DNA is strongly modulated with a period of 10.3 bases Proc. Natl. Acad. Sci. U.S.A. 84 1987 6644 6648
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 6644-6648
    • Gale, J.M.1    Nissen, K.A.2    Smerdon, M.J.3
  • 67
    • 0025410310 scopus 로고
    • UV induced (6-4) photoproducts are distributed differently than cydobutane dimers in nucleosomes
    • J.M. Gale, and M.J. Smerdon UV induced (6-4) photoproducts are distributed differently than cydobutane dimers in nucleosomes Photochem. Photobiol. 51 1990 411 417
    • (1990) Photochem. Photobiol. , vol.51 , pp. 411-417
    • Gale, J.M.1    Smerdon, M.J.2
  • 68
    • 0024380891 scopus 로고
    • Thymine dimer formation as a probe of the path of DNA in and between nucleosomes in intact chromatin
    • J.R. Pehrson Thymine dimer formation as a probe of the path of DNA in and between nucleosomes in intact chromatin Proc. Natl. Acad. Sci. U.S.A. 86 1989 9149 9153
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 9149-9153
    • Pehrson, J.R.1
  • 69
    • 0029115144 scopus 로고
    • Probing the conformation of nucleosome linker DNA in situ with pyrimidine dimer formation
    • J.R. Pehrson Probing the conformation of nucleosome linker DNA in situ with pyrimidine dimer formation J. Biol. Chem. 270 1995 22440 22444
    • (1995) J. Biol. Chem. , vol.270 , pp. 22440-22444
    • Pehrson, J.R.1
  • 70
    • 0027378279 scopus 로고
    • Unfolding of nucleosome cores dramatically changes the distribution of ultraviolet photoproducts in DNA
    • D.W. Brown, L.J. Libertini, C. Suquet, E.W. Small, and M.J. Smerdon Unfolding of nucleosome cores dramatically changes the distribution of ultraviolet photoproducts in DNA Biochemistry 32 1993 10527 10531
    • (1993) Biochemistry , vol.32 , pp. 10527-10531
    • Brown, D.W.1    Libertini, L.J.2    Suquet, C.3    Small, E.W.4    Smerdon, M.J.5
  • 71
    • 0027484148 scopus 로고
    • UV damage to DNA strongly influences its rotational setting on the histone surface of reconstituted nucleosomes
    • C. Suquet, and M.J. Smerdon UV damage to DNA strongly influences its rotational setting on the histone surface of reconstituted nucleosomes J. Biol. Chem. 268 1993 23755 23757
    • (1993) J. Biol. Chem. , vol.268 , pp. 23755-23757
    • Suquet, C.1    Smerdon, M.J.2
  • 72
    • 0030960760 scopus 로고    scopus 로고
    • DNA damage can alter the stability of nucleosomes: Effects are dependent on damage type
    • D.B. Mann, D.L. Springer, and M.J. Smerdon DNA damage can alter the stability of nucleosomes: effects are dependent on damage type Proc. Natl. Acad. Sci. U.S.A. 94 1997 2215 2220
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 2215-2220
    • Mann, D.B.1    Springer, D.L.2    Smerdon, M.J.3
  • 73
    • 0037126597 scopus 로고    scopus 로고
    • Nucleosome positioning at the replication fork
    • R. Lucchini, R.E. Wellinger, and J.M. Sogo Nucleosome positioning at the replication fork EMBO J. 20 2001 7294 7302
    • (2001) EMBO J. , vol.20 , pp. 7294-7302
    • Lucchini, R.1    Wellinger, R.E.2    Sogo, J.M.3
  • 74
    • 0030941116 scopus 로고    scopus 로고
    • Chromatin structure modulates DNA repair by photolyase in vivo
    • B. Suter, M. Livingstone-Zatchej, and F. Thoma Chromatin structure modulates DNA repair by photolyase in vivo EMBO J. 16 1997 2150 2160
    • (1997) EMBO J. , vol.16 , pp. 2150-2160
    • Suter, B.1    Livingstone-Zatchej, M.2    Thoma, F.3
  • 77
    • 0032717346 scopus 로고    scopus 로고
    • The discovery of enzymatic photoreactivation and the question of priority: The letters of Salvador Luria and Albert Kelner
    • E.C. Friedberg The discovery of enzymatic photoreactivation and the question of priority: the letters of Salvador Luria and Albert Kelner Biochimie 81 1999 7 13
    • (1999) Biochimie , vol.81 , pp. 7-13
    • Friedberg, E.C.1
  • 78
    • 0038305458 scopus 로고    scopus 로고
    • Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors
    • A. Sancar Structure and function of DNA photolyase and cryptochrome blue-light photoreceptors Chem. Rev. 103 2003 2203 2238
    • (2003) Chem. Rev. , vol.103 , pp. 2203-2238
    • Sancar, A.1
  • 79
    • 1942536615 scopus 로고    scopus 로고
    • Intraprotein electron transfer and proton dynamics during photoactivation of DNA photolyase from E. coli: Review and new insights from an "inverse" deuterium isotope effect
    • M. Byrdin, V. Sartor, A.P. Eker, M.H. Vos, C. Aubert, K. Brettel, and P. Mathis Intraprotein electron transfer and proton dynamics during photoactivation of DNA photolyase from E. coli: review and new insights from an "inverse" deuterium isotope effect Biochim. Biophys. Acta 1655 2004 64 70
    • (2004) Biochim. Biophys. Acta , vol.1655 , pp. 64-70
    • Byrdin, M.1    Sartor, V.2    Eker, A.P.3    Vos, M.H.4    Aubert, C.5    Brettel, K.6    Mathis, P.7
  • 81
    • 0024325453 scopus 로고
    • Interactions between yeast photolyase and nucleotide excision repair proteins in Saccharomyces cerevisiae and Escherichia coli
    • G.B. Sancar, and F.W. Smith Interactions between yeast photolyase and nucleotide excision repair proteins in Saccharomyces cerevisiae and Escherichia coli Mol. Cell. Biol. 9 1989 4767 4776
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 4767-4776
    • Sancar, G.B.1    Smith, F.W.2
  • 83
    • 0019285806 scopus 로고
    • Comparison of the cleavage of pyrimidine dimers by the bacteriophage T4 and Micrococcus luteus UV-specific endonucleases
    • L.K. Gordon, and W.A. Haseltine Comparison of the cleavage of pyrimidine dimers by the bacteriophage T4 and Micrococcus luteus UV-specific endonucleases J. Biol. Chem. 255 1980 12047 12050
    • (1980) J. Biol. Chem. , vol.255 , pp. 12047-12050
    • Gordon, L.K.1    Haseltine, W.A.2
  • 84
    • 0028863468 scopus 로고
    • Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNA substrate: Structural basis for damaged DNA recognition
    • D.G. Vassylyev, T. Kashiwagi, Y. Mikami, M. Ariyoshi, S. Iwai, E. Ohtsuka, and K. Morikawa Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNA substrate: structural basis for damaged DNA recognition Cell 83 1995 773 782
    • (1995) Cell , vol.83 , pp. 773-782
    • Vassylyev, D.G.1    Kashiwagi, T.2    Mikami, Y.3    Ariyoshi, M.4    Iwai, S.5    Ohtsuka, E.6    Morikawa, K.7
  • 85
    • 0024385267 scopus 로고
    • Photolyases from Saccharomyces cerevisiae and Escherichia coli recognize common binding determinants in DNA containing pyrimidine dimers
    • M. Baer, and G.B. Sancar Photolyases from Saccharomyces cerevisiae and Escherichia coli recognize common binding determinants in DNA containing pyrimidine dimers Mol. Cell. Biol. 9 1989 4777 4788
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 4777-4788
    • Baer, M.1    Sancar, G.B.2
  • 86
    • 0034733494 scopus 로고    scopus 로고
    • Enzymatic photoreactivation: 50 years and counting
    • G.B. Sancar Enzymatic photoreactivation: 50 years and counting Mutat. Res. 451 2000 25 37
    • (2000) Mutat. Res. , vol.451 , pp. 25-37
    • Sancar, G.B.1
  • 87
    • 0035977005 scopus 로고    scopus 로고
    • Cyclobutane pyrimidine dimers are responsible for the vast majority of mutations induced by UVB irradiation in mammalian cells
    • Y.H. You, D.H. Lee, J.H. Yoon, S. Nakajima, A. Yasui, and G.P. Pfeifer Cyclobutane pyrimidine dimers are responsible for the vast majority of mutations induced by UVB irradiation in mammalian cells J. Biol. Chem. 276 2001 44688 44694
    • (2001) J. Biol. Chem. , vol.276 , pp. 44688-44694
    • You, Y.H.1    Lee, D.H.2    Yoon, J.H.3    Nakajima, S.4    Yasui, A.5    Pfeifer, G.P.6
  • 88
    • 0345306615 scopus 로고    scopus 로고
    • In vivo recruitment of XPC to UV-induced cyclobutane pyrimidine dimers by the DDB2 gene product
    • M.E. Fitch, S. Nakajima, A. Yasui, and J.M. Ford In vivo recruitment of XPC to UV-induced cyclobutane pyrimidine dimers by the DDB2 gene product J. Biol. Chem. 278 2003 46906 46910
    • (2003) J. Biol. Chem. , vol.278 , pp. 46906-46910
    • Fitch, M.E.1    Nakajima, S.2    Yasui, A.3    Ford, J.M.4
  • 90
    • 0034733496 scopus 로고    scopus 로고
    • Nucleotide excision repair in yeast
    • S. Prakash, and L. Prakash Nucleotide excision repair in yeast Mutat. Res. 451 2000 13 24
    • (2000) Mutat. Res. , vol.451 , pp. 13-24
    • Prakash, S.1    Prakash, L.2
  • 91
    • 0036301403 scopus 로고    scopus 로고
    • DNA-repair by photolyase reveals dynamic properties of nucleosome positioning in vivo
    • B. Suter, and F. Thoma DNA-repair by photolyase reveals dynamic properties of nucleosome positioning in vivo J. Mol. Biol. 319 2002 395 406
    • (2002) J. Mol. Biol. , vol.319 , pp. 395-406
    • Suter, B.1    Thoma, F.2
  • 92
    • 0032005792 scopus 로고    scopus 로고
    • Nucleotide excision repair and photolyase preferentially repair the nontranscribed strand of RNA polymerase Ill-transcribed genes in Saccharomyces cerevisiae
    • A. Aboussekhra, and F. Thoma Nucleotide excision repair and photolyase preferentially repair the nontranscribed strand of RNA polymerase Ill-transcribed genes in Saccharomyces cerevisiae Genes Dev. 12 1998 411 421
    • (1998) Genes Dev. , vol.12 , pp. 411-421
    • Aboussekhra, A.1    Thoma, F.2
  • 93
    • 0034310723 scopus 로고    scopus 로고
    • Poly(dA.dT) sequences exist as rigid DNA structures in nucleosome-free yeast promoters in vivo
    • B. Suter, G. Schnappauf, and F. Thoma Poly(dA.dT) sequences exist as rigid DNA structures in nucleosome-free yeast promoters in vivo Nucl. Acids Res. 28 2000 4083 4089
    • (2000) Nucl. Acids Res. , vol.28 , pp. 4083-4089
    • Suter, B.1    Schnappauf, G.2    Thoma, F.3
  • 94
    • 0037089137 scopus 로고    scopus 로고
    • Photoreactivation of UV-induced cyclobutane pyrimidine dimers in the MFA2 gene of Saccharomyces cerevisiae
    • N.R. Morse, V. Meniel, and R. Waters Photoreactivation of UV-induced cyclobutane pyrimidine dimers in the MFA2 gene of Saccharomyces cerevisiae Nucl. Acids Res. 30 2002 1799 1807
    • (2002) Nucl. Acids Res. , vol.30 , pp. 1799-1807
    • Morse, N.R.1    Meniel, V.2    Waters, R.3
  • 95
    • 0034658426 scopus 로고    scopus 로고
    • DNA repair in a yeast origin of replication: Contributions of photolyase and nucleotide excision repair
    • B. Suter, R.E. Wellinger, and F. Thoma DNA repair in a yeast origin of replication: contributions of photolyase and nucleotide excision repair Nucl. Acids Res. 28 2000 2060 2068
    • (2000) Nucl. Acids Res. , vol.28 , pp. 2060-2068
    • Suter, B.1    Wellinger, R.E.2    Thoma, F.3
  • 96
    • 3543041827 scopus 로고    scopus 로고
    • Kinetochores prevent repair of UV damage in Saccharomyces cerevisiae centromeres
    • C. Capiaghi, T.V. Ho, and F. Thoma Kinetochores prevent repair of UV damage in Saccharomyces cerevisiae centromeres Mol. Cell. Biol. 24 2004 6907 6918
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6907-6918
    • Capiaghi, C.1    Ho, T.V.2    Thoma, F.3
  • 97
    • 0141509951 scopus 로고    scopus 로고
    • Repair of UV lesions in silenced chromatin provides in vivo evidence for a compact chromatin structure
    • M. Livingstone-Zatchej, R. Marcionelli, K. Moller, R. De Pril, and F. Thoma Repair of UV lesions in silenced chromatin provides in vivo evidence for a compact chromatin structure J. Biol. Chem. 278 2003 37471 37479
    • (2003) J. Biol. Chem. , vol.278 , pp. 37471-37479
    • Livingstone-Zatchej, M.1    Marcionelli, R.2    Moller, K.3    De Pril, R.4    Thoma, F.5
  • 98
    • 0030964608 scopus 로고    scopus 로고
    • RNA polymerase II transcription inhibits DNA repair by photolyase in the transcribed strand of active yeast genes
    • M. Livingstone-Zatchej, A. Meier, B. Suter, and F. Thoma RNA polymerase II transcription inhibits DNA repair by photolyase in the transcribed strand of active yeast genes Nucl. Acids Res. 25 1997 3795 3800
    • (1997) Nucl. Acids Res. , vol.25 , pp. 3795-3800
    • Livingstone-Zatchej, M.1    Meier, A.2    Suter, B.3    Thoma, F.4
  • 99
    • 0037023774 scopus 로고    scopus 로고
    • Repair of active and silenced rDNA in yeast: The contributions of photolyase and transcription-coupled nucleotide excision repair
    • A. Meier, M. Livingstone-Zatchej, and F. Thoma Repair of active and silenced rDNA in yeast: the contributions of photolyase and transcription- coupled nucleotide excision repair J. Biol. Chem. 277 2002 11845 11852
    • (2002) J. Biol. Chem. , vol.277 , pp. 11845-11852
    • Meier, A.1    Livingstone-Zatchej, M.2    Thoma, F.3
  • 100
    • 0026757373 scopus 로고
    • Transcription, nucleosome stability, and DNA repair in a yeast minichromosome
    • J. Bedoyan, R. Gupta, F. Thoma, and M.J. Smerdon Transcription, nucleosome stability, and DNA repair in a yeast minichromosome J. Biol. Chem. 267 1992 5996 6005
    • (1992) J. Biol. Chem. , vol.267 , pp. 5996-6005
    • Bedoyan, J.1    Gupta, R.2    Thoma, F.3    Smerdon, M.J.4
  • 101
    • 0034611785 scopus 로고    scopus 로고
    • High mobility of proteins in the mammalian cell nucleus
    • R.D. Phair, and T. Misteli High mobility of proteins in the mammalian cell nucleus Nature 404 2000 604 609
    • (2000) Nature , vol.404 , pp. 604-609
    • Phair, R.D.1    Misteli, T.2
  • 102
    • 0037450761 scopus 로고    scopus 로고
    • P53 is a chromatin accessibility factor for nucleotide excision repair of DNA damage
    • C.P. Rubbi, and J. Milner p53 is a chromatin accessibility factor for nucleotide excision repair of DNA damage EMBO J. 22 2003 975 986
    • (2003) EMBO J. , vol.22 , pp. 975-986
    • Rubbi, C.P.1    Milner, J.2
  • 103
    • 0034601464 scopus 로고    scopus 로고
    • A chromatin remodelling complex involved in transcription and DNA processing
    • X. Shen, G. Mizuguchi, A. Hamiche, and C. Wu A chromatin remodelling complex involved in transcription and DNA processing Nature 406 2000 541 544
    • (2000) Nature , vol.406 , pp. 541-544
    • Shen, X.1    Mizuguchi, G.2    Hamiche, A.3    Wu, C.4
  • 104
    • 0037032422 scopus 로고    scopus 로고
    • Abundance of the RSC nucleosome-remodeling complex is important for the cells to tolerate DNA damage in Saccharomyces cerevisiae
    • H. Koyama, M. Itoh, K. Miyahara, and E. Tsuchiya Abundance of the RSC nucleosome-remodeling complex is important for the cells to tolerate DNA damage in Saccharomyces cerevisiae FEBS Lett. 531 2002 215 221
    • (2002) FEBS Lett. , vol.531 , pp. 215-221
    • Koyama, H.1    Itoh, M.2    Miyahara, K.3    Tsuchiya, E.4
  • 105
    • 0035281586 scopus 로고    scopus 로고
    • In vivo chromatin remodeling by yeast ISWI homologs Isw1p and Isw2p
    • N.A. Kent, N. Karabetsou, P.K. Politis, and J. Mellor In vivo chromatin remodeling by yeast ISWI homologs Isw1p and Isw2p Genes Dev. 15 2001 619 626
    • (2001) Genes Dev. , vol.15 , pp. 619-626
    • Kent, N.A.1    Karabetsou, N.2    Politis, P.K.3    Mellor, J.4
  • 106
    • 0345276461 scopus 로고    scopus 로고
    • Chromatin remodeling in vivo: Evidence for a nucleosome sliding mechanism
    • T.G. Fazzio, and T. Tsukiyama Chromatin remodeling in vivo: evidence for a nucleosome sliding mechanism Mol. Cell 12 2003 1333 1340
    • (2003) Mol. Cell , vol.12 , pp. 1333-1340
    • Fazzio, T.G.1    Tsukiyama, T.2
  • 107
    • 0033558873 scopus 로고    scopus 로고
    • Characterization of the imitation switch subfamily of ATP-dependent chromatin-remodeling factors in Saccharomyces cerevisiae
    • T. Tsukiyama, J. Palmer, C.C. Landel, J. Shiloach, and C. Wu Characterization of the imitation switch subfamily of ATP-dependent chromatin-remodeling factors in Saccharomyces cerevisiae Genes Dev. 13 1999 686 697
    • (1999) Genes Dev. , vol.13 , pp. 686-697
    • Tsukiyama, T.1    Palmer, J.2    Landel, C.C.3    Shiloach, J.4    Wu, C.5
  • 109
    • 0035902108 scopus 로고    scopus 로고
    • Genome maintenance mechanisms for preventing cancer
    • J.H. Hoeijmakers Genome maintenance mechanisms for preventing cancer Nature 411 2001 366 374
    • (2001) Nature , vol.411 , pp. 366-374
    • Hoeijmakers, J.H.1
  • 110
    • 0037115936 scopus 로고    scopus 로고
    • Subpathways of nucleotide excision repair and their regulation
    • P.C. Hanawalt Subpathways of nucleotide excision repair and their regulation Oncogene 21 2002 8949 8956
    • (2002) Oncogene , vol.21 , pp. 8949-8956
    • Hanawalt, P.C.1
  • 111
    • 0033118354 scopus 로고    scopus 로고
    • Molecular mechanism of nucleotide excision repair
    • W.L. de Laat, N.G. Jaspers, and J.H. Hoeijmakers Molecular mechanism of nucleotide excision repair Genes Dev. 13 1999 768 785
    • (1999) Genes Dev. , vol.13 , pp. 768-785
    • De Laat, W.L.1    Jaspers, N.G.2    Hoeijmakers, J.H.3
  • 112
    • 0033603338 scopus 로고    scopus 로고
    • Order of assembly of human DNA repair excision nuclease
    • M. Wakasugi, and A. Sancar Order of assembly of human DNA repair excision nuclease J. Biol. Chem. 274 1999 18759 18768
    • (1999) J. Biol. Chem. , vol.274 , pp. 18759-18768
    • Wakasugi, M.1    Sancar, A.2
  • 113
    • 0030732132 scopus 로고    scopus 로고
    • Mechanism of open complex and dual incision formation by human nucleotide excision repair factors
    • E. Evans, J.G. Moggs, J.R. Hwang, J.M. Egly, and R.D. Wood Mechanism of open complex and dual incision formation by human nucleotide excision repair factors EMBO J. 16 1997 6559 6573
    • (1997) EMBO J. , vol.16 , pp. 6559-6573
    • Evans, E.1    Moggs, J.G.2    Hwang, J.R.3    Egly, J.M.4    Wood, R.D.5
  • 115
    • 4544242205 scopus 로고    scopus 로고
    • Mechanisms of DNA damage recognition and strand discrimination in human nucleotide excision repair
    • R. Dip, U. Camenisch, and H. Naegeli Mechanisms of DNA damage recognition and strand discrimination in human nucleotide excision repair DNA Rep. (Amsterdam) 3 2004 1409 1423
    • (2004) DNA Rep. (Amsterdam) , vol.3 , pp. 1409-1423
    • Dip, R.1    Camenisch, U.2    Naegeli, H.3
  • 116
    • 0018125018 scopus 로고
    • Nucleosome rearrangement in human chromatin during UV-induced DNA-reapir synthesis
    • M.J. Smerdon, and M.W. Lieberman Nucleosome rearrangement in human chromatin during UV-induced DNA-reapir synthesis Proc. Natl. Acad. Sci. U.S.A. 75 1978 4238 4241
    • (1978) Proc. Natl. Acad. Sci. U.S.A. , vol.75 , pp. 4238-4241
    • Smerdon, M.J.1    Lieberman, M.W.2
  • 117
    • 0019132228 scopus 로고
    • Distribution within chromatin of deoxyribonucleic acid repair synthesis occurring at different times after ultraviolet radiation
    • M.J. Smerdon, and M.W. Lieberman Distribution within chromatin of deoxyribonucleic acid repair synthesis occurring at different times after ultraviolet radiation Biochemistry 19 1980 2992 3000
    • (1980) Biochemistry , vol.19 , pp. 2992-3000
    • Smerdon, M.J.1    Lieberman, M.W.2
  • 118
    • 0022972433 scopus 로고
    • Stability of nucleosome placement in newly repaired regions of DNA
    • K.A. Nissen, S.Y. Lan, and M.J. Smerdon Stability of nucleosome placement in newly repaired regions of DNA J. Biol. Chem. 261 1986 8585 8588
    • (1986) J. Biol. Chem. , vol.261 , pp. 8585-8588
    • Nissen, K.A.1    Lan, S.Y.2    Smerdon, M.J.3
  • 119
    • 0025340988 scopus 로고
    • DNA repair within nucleosome cores of UV-irradiated human cells
    • K.A. Jensen, and M.J. Smerdon DNA repair within nucleosome cores of UV-irradiated human cells Biochemistry 29 1990 4773 4782
    • (1990) Biochemistry , vol.29 , pp. 4773-4782
    • Jensen, K.A.1    Smerdon, M.J.2
  • 120
    • 0028242355 scopus 로고
    • Determination of minimum substrate size for human excinuclease
    • J.C. Huang, and A. Sancar Determination of minimum substrate size for human excinuclease J. Biol. Chem. 269 1994 19034 19040
    • (1994) J. Biol. Chem. , vol.269 , pp. 19034-19040
    • Huang, J.C.1    Sancar, A.2
  • 121
    • 0026508487 scopus 로고
    • Human nucleotide excision nuclease removes thymine dimers from DNA by incising the 22nd phosphodiester bond 5′ and the 6th phosphodiester bond 3′ to the photodimer
    • J.C. Huang, D.L. Svoboda, J.T. Reardon, and A. Sancar Human nucleotide excision nuclease removes thymine dimers from DNA by incising the 22nd phosphodiester bond 5′ and the 6th phosphodiester bond 3′ to the photodimer Proc. Natl. Acad. Sci. U.S.A. 89 1992 3664 3668
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 3664-3668
    • Huang, J.C.1    Svoboda, D.L.2    Reardon, J.T.3    Sancar, A.4
  • 122
  • 123
    • 0030710190 scopus 로고    scopus 로고
    • Initiation and bidirectional propagation of chromatin assembly from a target site for nucleotide excision repair
    • P.H. Gaillard, J.G. Moggs, D.M. Roche, J.P. Quivy, P.B. Becker, R.D. Wood, and G. Almouzni Initiation and bidirectional propagation of chromatin assembly from a target site for nucleotide excision repair EMBO J. 16 1997 6281 6289
    • (1997) EMBO J. , vol.16 , pp. 6281-6289
    • Gaillard, P.H.1    Moggs, J.G.2    Roche, D.M.3    Quivy, J.P.4    Becker, P.B.5    Wood, R.D.6    Almouzni, G.7
  • 124
    • 0141530885 scopus 로고    scopus 로고
    • Local action of the chromatin assembly factor CAF-1 at sites of nucleotide excision repair in vivo
    • C.M. Green, and G. Almouzni Local action of the chromatin assembly factor CAF-1 at sites of nucleotide excision repair in vivo EMBO J. 22 2003 5163 5174
    • (2003) EMBO J. , vol.22 , pp. 5163-5174
    • Green, C.M.1    Almouzni, G.2
  • 125
    • 0031043134 scopus 로고    scopus 로고
    • Ultraviolet radiation sensitivity and reduction of telomeric silencing Saccharomyces cerevisiae cells lacking chromatin assembly factor-I
    • P.D. Kaufman, R. Kobayashi, and B. Stillman Ultraviolet radiation sensitivity and reduction of telomeric silencing Saccharomyces cerevisiae cells lacking chromatin assembly factor-I Gene Dev. 11 1997 345 357
    • (1997) Gene Dev. , vol.11 , pp. 345-357
    • Kaufman, P.D.1    Kobayashi, R.2    Stillman, B.3
  • 128
    • 0037127293 scopus 로고    scopus 로고
    • DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair
    • M. Wakasugi, A. Kawashima, H. Morioka, S. Linn, A. Sancar, T. Mori, O. Nikaido, and T. Matsunaga DDB accumulates at DNA damage sites immediately after UV irradiation and directly stimulates nucleotide excision repair J. Biol. Chem. 277 2002 1637 1640
    • (2002) J. Biol. Chem. , vol.277 , pp. 1637-1640
    • Wakasugi, M.1    Kawashima, A.2    Morioka, H.3    Linn, S.4    Sancar, A.5    Mori, T.6    Nikaido, O.7    Matsunaga, T.8
  • 132
    • 0025719346 scopus 로고
    • Nucleotide excision repair of DNA by human cell extracts is suppressed in reconstituted nucleosomes
    • Z.G. Wang, X.H. Wu, and E.C. Friedberg Nucleotide excision repair of DNA by human cell extracts is suppressed in reconstituted nucleosomes J. Biol. Chem. 266 1991 22472 22478
    • (1991) J. Biol. Chem. , vol.266 , pp. 22472-22478
    • Wang, Z.G.1    Wu, X.H.2    Friedberg, E.C.3
  • 134
    • 0034604708 scopus 로고    scopus 로고
    • Nucleotide excision repair of the 5 S ribosomal RNA gene assembled into a nucleosome
    • X. Liu, and M.J. Smerdon Nucleotide excision repair of the 5 S ribosomal RNA gene assembled into a nucleosome J. Biol. Chem. 275 2000 23729 23735
    • (2000) J. Biol. Chem. , vol.275 , pp. 23729-23735
    • Liu, X.1    Smerdon, M.J.2
  • 135
    • 0035901558 scopus 로고    scopus 로고
    • ATP-dependent chromatin remodeling facilitates nucleotide excision repair of UV-induced DNA lesions in synthetic dinucleosomes
    • K. Ura, M. Araki, H. Saeki, C. Masutani, T. Ito, S. Iwai, T. Mizukoshi, Y. Kaneda, and F. Hanaoka ATP-dependent chromatin remodeling facilitates nucleotide excision repair of UV-induced DNA lesions in synthetic dinucleosomes EMBO J. 20 2001 2004 2014
    • (2001) EMBO J. , vol.20 , pp. 2004-2014
    • Ura, K.1    Araki, M.2    Saeki, H.3    Masutani, C.4    Ito, T.5    Iwai, S.6    Mizukoshi, T.7    Kaneda, Y.8    Hanaoka, F.9
  • 136
    • 0034461931 scopus 로고    scopus 로고
    • DNA damage in the nucleosome core is refractory to repair by human excision nuclease
    • R. Hara, J. Mo, and A. Sancar DNA damage in the nucleosome core is refractory to repair by human excision nuclease Mol. Cell Biol. 20 2000 9173 9181
    • (2000) Mol. Cell Biol. , vol.20 , pp. 9173-9181
    • Hara, R.1    Mo, J.2    Sancar, A.3
  • 137
    • 0038656433 scopus 로고    scopus 로고
    • Effect of damage type on stimulation of human excision nuclease by SWI/SNF chromatin remodeling factor
    • R. Hara, and A. Sancar Effect of damage type on stimulation of human excision nuclease by SWI/SNF chromatin remodeling factor Mol. Cell Biol. 23 2003 4121 4125
    • (2003) Mol. Cell Biol. , vol.23 , pp. 4121-4125
    • Hara, R.1    Sancar, A.2
  • 138
    • 0036785614 scopus 로고    scopus 로고
    • The SWI/SNF chromatin-remodeling factor stimulates repair by human excision nuclease in the mononucleosome core particle
    • R. Hara, and A. Sancar The SWI/SNF chromatin-remodeling factor stimulates repair by human excision nuclease in the mononucleosome core particle Mol. Cell. Biol. 22 2002 6779 6787
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6779-6787
    • Hara, R.1    Sancar, A.2
  • 139
    • 0030798002 scopus 로고    scopus 로고
    • Nucleosome structure and positioning modulate nucleotide excision repair in the non-transcribed strand of an active gene
    • R.E. Wellinger, and F. Thoma Nucleosome structure and positioning modulate nucleotide excision repair in the non-transcribed strand of an active gene EMBO J. 16 1997 5046 5056
    • (1997) EMBO J. , vol.16 , pp. 5046-5056
    • Wellinger, R.E.1    Thoma, F.2
  • 140
    • 0032963791 scopus 로고    scopus 로고
    • RNA polymerase II transcription suppresses nucleosomal modulation of UV-induced (6-4) photoproduct and cyclobutane pyrimidine dimer repair in yeast
    • M. Tijsterman, R. de Pril, J.G. Tasseron-de Jong, and J. Brouwer RNA polymerase II transcription suppresses nucleosomal modulation of UV-induced (6-4) photoproduct and cyclobutane pyrimidine dimer repair in yeast Mol. Cell. Biol. 19 1999 934 940
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 934-940
    • Tijsterman, M.1    De Pril, R.2    Tasseron-De Jong, J.G.3    Brouwer, J.4
  • 141
    • 3042624480 scopus 로고    scopus 로고
    • Cbf1p modulates chromatin structure, transcription and repair at the Saccharomyces cerevisiae MET16 locus
    • J.A. Ferreiro, N.G. Powell, N. Karabetsou, N.A. Kent, J. Mellor, and R. Waters Cbf1p modulates chromatin structure, transcription and repair at the Saccharomyces cerevisiae MET16 locus Nucl. Acids Res. 32 2004 1617 1626
    • (2004) Nucl. Acids Res. , vol.32 , pp. 1617-1626
    • Ferreiro, J.A.1    Powell, N.G.2    Karabetsou, N.3    Kent, N.A.4    Mellor, J.5    Waters, R.6
  • 142
    • 0037414332 scopus 로고    scopus 로고
    • Transcription, nucleosome positioning and protein binding modulate nucleotide excision repair of the Saccharomyces cerevisiae MET17 promoter
    • N.G. Powell, J. Ferreiro, N. Karabetsou, J. Mellor, and R. Waters Transcription, nucleosome positioning and protein binding modulate nucleotide excision repair of the Saccharomyces cerevisiae MET17 promoter DNA Rep. (Amsterdam) 2 2003 375 386
    • (2003) DNA Rep. (Amsterdam) , vol.2 , pp. 375-386
    • Powell, N.G.1    Ferreiro, J.2    Karabetsou, N.3    Mellor, J.4    Waters, R.5
  • 143
    • 0037160120 scopus 로고    scopus 로고
    • Nucleosome structure and repair of N- methylpurines in the GAL1-10 genes of Saccharomyces cerevisiae
    • S. Li, and M.J. Smerdon Nucleosome structure and repair of N- methylpurines in the GAL1-10 genes of Saccharomyces cerevisiae J. Biol. Chem. 277 2002 44651 44659
    • (2002) J. Biol. Chem. , vol.277 , pp. 44651-44659
    • Li, S.1    Smerdon, M.J.2
  • 144
    • 0033199871 scopus 로고    scopus 로고
    • Nucleotide excision repair in a constitutive and inducible gene of a yeast minichromosome in intact cells
    • S. Li, M. Livingstone-Zatchej, R. Gupta, M. Meijer, F. Thoma, and M.J. Smerdon Nucleotide excision repair in a constitutive and inducible gene of a yeast minichromosome in intact cells Nucl. Acids Res. 27 1999 3610 3620
    • (1999) Nucl. Acids Res. , vol.27 , pp. 3610-3620
    • Li, S.1    Livingstone-Zatchej, M.2    Gupta, R.3    Meijer, M.4    Thoma, F.5    Smerdon, M.J.6
  • 148
    • 0025787384 scopus 로고
    • Yeast nucleosomal particles: Structural and transcriptional properties
    • M. Pineiro, C. Puerta, and E. Palacian Yeast nucleosomal particles: structural and transcriptional properties Biochemistry 30 1991 5805 5810
    • (1991) Biochemistry , vol.30 , pp. 5805-5810
    • Pineiro, M.1    Puerta, C.2    Palacian, E.3
  • 149
    • 0018581187 scopus 로고
    • Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin
    • F. Thoma, T. Koller, and A. Klug Involvement of histone H1 in the organization of the nucleosome and of the salt-dependent superstructures of chromatin J. Cell. Biol. 83 1979 403 427
    • (1979) J. Cell. Biol. , vol.83 , pp. 403-427
    • Thoma, F.1    Koller, T.2    Klug, A.3
  • 150
    • 0028130301 scopus 로고
    • Linker histones H1 and H5 prevent the mobility of positioned nucleosomes
    • S. Pennings, G. Meersseman, and E.M. Bradbury Linker histones H1 and H5 prevent the mobility of positioned nucleosomes Proc. Natl. Acad. Sci. U.S.A. 91 1994 10275 10279
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 10275-10279
    • Pennings, S.1    Meersseman, G.2    Bradbury, E.M.3
  • 151
    • 0020356008 scopus 로고
    • Sodium butyrate stimulates DNA repair in UV-irradiated normal and xeroderma pigmentosum human fibroblasts
    • M.J. Smerdon, S.Y. Lan, R.E. Calza, and R. Reeves Sodium butyrate stimulates DNA repair in UV-irradiated normal and xeroderma pigmentosum human fibroblasts J. Biol. Chem. 257 1982 13441 13447
    • (1982) J. Biol. Chem. , vol.257 , pp. 13441-13447
    • Smerdon, M.J.1    Lan, S.Y.2    Calza, R.E.3    Reeves, R.4
  • 152
    • 0036300514 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae histone acetyltransferase Gcn5 has a role in the photoreactivation and nucleotide excision repair of UV-induced cyclobutane pyrimidine dimers in the MFA2 gene
    • Y. Teng, Y. Yu, and R. Waters The Saccharomyces cerevisiae histone acetyltransferase Gcn5 has a role in the photoreactivation and nucleotide excision repair of UV-induced cyclobutane pyrimidine dimers in the MFA2 gene J. Mol. Biol. 316 2002 489 499
    • (2002) J. Mol. Biol. , vol.316 , pp. 489-499
    • Teng, Y.1    Yu, Y.2    Waters, R.3
  • 153
    • 10044280323 scopus 로고    scopus 로고
    • Crystal structure of a photolyase bound to a CPD-like DNA lesion after in situ repair
    • A. Mees, T. Klar, P. Gnau, U. Hennecke, A.P. Eker, T. Carell, and L.O. Essen Crystal structure of a photolyase bound to a CPD-like DNA lesion after in situ repair Science 306 2004 1789 1793
    • (2004) Science , vol.306 , pp. 1789-1793
    • Mees, A.1    Klar, T.2    Gnau, P.3    Hennecke, U.4    Eker, A.P.5    Carell, T.6    Essen, L.O.7
  • 154
    • 0020357694 scopus 로고
    • Defective excision of pyrimidine dimers and interstrand DNA crosslinks in rad7 and rad23 mutants of Saccharomyces cerevisiae
    • R.D. Miller, L. Prakash, and S. Prakash Defective excision of pyrimidine dimers and interstrand DNA crosslinks in rad7 and rad23 mutants of Saccharomyces cerevisiae Mol. Gen. Genet. 188 1982 235 239
    • (1982) Mol. Gen. Genet. , vol.188 , pp. 235-239
    • Miller, R.D.1    Prakash, L.2    Prakash, S.3
  • 155
    • 0027999206 scopus 로고
    • The RAD7 and RAD16 genes, which are essential for pyrimidine dimer removal from the silent mating type loci, are also required for repair of the nontranscribed strand of an active gene in Saccharomyces cerevisiae
    • R. Verhage, A.M. Zeeman, N. de Groot, F. Gleig, D.D. Bang, P. van de Putte, and J. Brouwer The RAD7 and RAD16 genes, which are essential for pyrimidine dimer removal from the silent mating type loci, are also required for repair of the nontranscribed strand of an active gene in Saccharomyces cerevisiae Mol. Cell. Biol. 14 1994 6135 6142
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6135-6142
    • Verhage, R.1    Zeeman, A.M.2    De Groot, N.3    Gleig, F.4    Bang, D.D.5    Van De Putte, P.6    Brouwer, J.7
  • 156
    • 0030050644 scopus 로고    scopus 로고
    • Analysis of gene- and strand-specific repair in the moderately UV- sensitive Saccharomyces cerevisiae rad23 mutant
    • R.A. Verhage, A.M. Zeeman, M. Lombaerts, P. van de Putte, and J. Brouwer Analysis of gene- and strand-specific repair in the moderately UV- sensitive Saccharomyces cerevisiae rad23 mutant Mutat. Res. 362 1996 155 165
    • (1996) Mutat. Res. , vol.362 , pp. 155-165
    • Verhage, R.A.1    Zeeman, A.M.2    Lombaerts, M.3    Van De Putte, P.4    Brouwer, J.5
  • 157
    • 0029026826 scopus 로고
    • Repair of plasmid and genomic DNA in a rad7 delta mutant of yeast
    • J.P. Mueller, and M.J. Smerdon Repair of plasmid and genomic DNA in a rad7 delta mutant of yeast Nucl. Acids Res. 23 1995 3457 3464
    • (1995) Nucl. Acids Res. , vol.23 , pp. 3457-3464
    • Mueller, J.P.1    Smerdon, M.J.2
  • 158
    • 0031588941 scopus 로고    scopus 로고
    • Excision repair at the level of the nucleotide in the Saccharomyces cerevisiae MFA2 gene: Mapping of where enhanced repair in the transcribed strand begins or ends and identification of only a partial rad16 requisite for repairing upstream control sequences
    • Y. Teng, S. Li, R. Waters, and S.H. Reed Excision repair at the level of the nucleotide in the Saccharomyces cerevisiae MFA2 gene: mapping of where enhanced repair in the transcribed strand begins or ends and identification of only a partial rad16 requisite for repairing upstream control sequences J. Mol. Biol. 267 1997 324 337
    • (1997) J. Mol. Biol. , vol.267 , pp. 324-337
    • Teng, Y.1    Li, S.2    Waters, R.3    Reed, S.H.4
  • 159
    • 0842281646 scopus 로고    scopus 로고
    • The yeast Rad7/Rad16/ABf1 complex generates superhelical torsion in DNA that is required for nucleotide excision repair
    • S. Yu, T. Owen-Hughes, E.C. Friedberg, R. Waters, and S.H. Reed The yeast Rad7/Rad16/ABf1 complex generates superhelical torsion in DNA that is required for nucleotide excision repair DNA Rep. 3 2004 277 287
    • (2004) DNA Rep. , vol.3 , pp. 277-287
    • Yu, S.1    Owen-Hughes, T.2    Friedberg, E.C.3    Waters, R.4    Reed, S.H.5
  • 160
    • 0036318818 scopus 로고    scopus 로고
    • Molecular anatomy of the human excision nuclease assembled at sites of DNA damage
    • J.T. Reardon, and A. Sancar Molecular anatomy of the human excision nuclease assembled at sites of DNA damage Mol. Cell. Biol. 22 2002 5938 5945
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5938-5945
    • Reardon, J.T.1    Sancar, A.2
  • 161
    • 0142059994 scopus 로고    scopus 로고
    • Recognition and repair of the cyclobutane thymine dimer, a major cause of skin cancers, by the human excision nuclease
    • J.T. Reardon, and A. Sancar Recognition and repair of the cyclobutane thymine dimer, a major cause of skin cancers, by the human excision nuclease Genes Dev. 17 2003 2539 2551
    • (2003) Genes Dev. , vol.17 , pp. 2539-2551
    • Reardon, J.T.1    Sancar, A.2
  • 162
    • 0033636515 scopus 로고    scopus 로고
    • Xeroderma pigmentosum p48 gene enhances global genomic repair and suppresses UV-induced mutagenesis
    • J.Y. Tang, B.J. Hwang, J.M. Ford, P.C. Hanawalt, and G. Chu Xeroderma pigmentosum p48 gene enhances global genomic repair and suppresses UV-induced mutagenesis Mol. Cell 5 2000 737 744
    • (2000) Mol. Cell , vol.5 , pp. 737-744
    • Tang, J.Y.1    Hwang, B.J.2    Ford, J.M.3    Hanawalt, P.C.4    Chu, G.5
  • 163
    • 0037031210 scopus 로고    scopus 로고
    • Xeroderma pigmentosum complementation group e and UV-damaged DNA-binding protein
    • J. Tang, and G. Chu Xeroderma pigmentosum complementation group E and UV-damaged DNA-binding protein DNA Rep. (Amsterdam) 1 2002 601 616
    • (2002) DNA Rep. (Amsterdam) , vol.1 , pp. 601-616
    • Tang, J.1    Chu, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.