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Volumn 28, Issue , 1999, Pages 101-128

DNA repair mechanisms for the recognition and removal of damaged DNA bases

Author keywords

DNA base excision repair; DNA glycosylases; Minor groove recognition; Nucleotide flipping

Indexed keywords

DNA BASE; DNA GLYCOSYLTRANSFERASE; ENDONUCLEASE; URACIL;

EID: 0032985826     PISSN: 10568700     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.biophys.28.1.101     Document Type: Article
Times cited : (172)

References (103)
  • 1
    • 0032498302 scopus 로고    scopus 로고
    • Crystal structure of a G:T/U mismatch-specific DNA glycosylase: Mismatch recognition by complementary-strand interactions
    • 1. Barrett TE, Savva R, Panayotou G, Barlow T, Brown T, Pearl LH. 1998. Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Cell 92:117-29
    • (1998) Cell , vol.92 , pp. 117-129
    • Barrett, T.E.1    Savva, R.2    Panayotou, G.3    Barlow, T.4    Brown, T.5    Pearl, L.H.6
  • 2
    • 0030839865 scopus 로고    scopus 로고
    • Oxidative decay of DNA
    • 2. Beckman KB, Ames BN. 1997. Oxidative decay of DNA. J. Biol. Chem. 272:19633-36
    • (1997) J. Biol. Chem. , vol.272 , pp. 19633-19636
    • Beckman, K.B.1    Ames, B.N.2
  • 3
    • 0030740948 scopus 로고    scopus 로고
    • Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathway
    • 3. Bennett RAO, Wilson DM III, Wong D, Demple B. 1997. Interaction of human apurinic endonuclease and DNA polymerase β in the base excision repair pathway. Proc. Natl. Acad. Sci. USA 94:7166-69
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7166-7169
    • Bennett, R.A.O.1    Wilson D.M. III2    Wong, D.3    Demple, B.4
  • 4
    • 0032518911 scopus 로고    scopus 로고
    • Release of normal bases from intact DNA by a native DNA repair enzyme
    • 4. Berdal KG, Johansen RF, Seeberg E. 1998. Release of normal bases from intact DNA by a native DNA repair enzyme. EMBO J. 15:363-67
    • (1998) EMBO J. , vol.15 , pp. 363-367
    • Berdal, K.G.1    Johansen, R.F.2    Seeberg, E.3
  • 5
    • 0027215935 scopus 로고
    • Excision of 3-methylguanine from alkylated DNA by 3-methyladenine DNA glycosylase I from Escherichia coli
    • 5. Bjelland S, Bjoras M, Seeberg E. 1993. Excision of 3-methylguanine from alkylated DNA by 3-methyladenine DNA glycosylase I from Escherichia coli. Nucleic Acids Res. 21:2041-49
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2041-2049
    • Bjelland, S.1    Bjoras, M.2    Seeberg, E.3
  • 6
    • 0024328839 scopus 로고
    • UV-induced pyrimidine hydrates in DNA are repaired by bacterial and mammalian DNA glycosylase activities
    • 6. Boorstein RJ, Hilbert TP, Cadet J, Cunningham RP, Teebor GW. 1989. UV-induced pyrimidine hydrates in DNA are repaired by bacterial and mammalian DNA glycosylase activities. Biochemistry 28:6164-70
    • (1989) Biochemistry , vol.28 , pp. 6164-6170
    • Boorstein, R.J.1    Hilbert, T.P.2    Cadet, J.3    Cunningham, R.P.4    Teebor, G.W.5
  • 8
    • 0028862933 scopus 로고
    • Characterization of the XRCCI-DNA ligase III complex in vitro and its absence from mutant hamster cells
    • 8. Caldecott KW, Tucker JD, Stanker LH, Thompson LH. 1995. Characterization of the XRCCI-DNA ligase III complex in vitro and its absence from mutant hamster cells. Nucleic Acids Res. 23:4836-43
    • (1995) Nucleic Acids Res. , vol.23 , pp. 4836-4843
    • Caldecott, K.W.1    Tucker, J.D.2    Stanker, L.H.3    Thompson, L.H.4
  • 9
    • 0029163078 scopus 로고
    • Structure and function of DNA methyltransferases
    • 9. Cheng X. 1995. Structure and function of DNA methyltransferases. Annu. Rev. Biophys. Biomol. Struct. 24:293-318
    • (1995) Annu. Rev. Biophys. Biomol. Struct. , vol.24 , pp. 293-318
    • Cheng, X.1
  • 10
    • 0030585418 scopus 로고    scopus 로고
    • Finding a basis for flipping bases
    • 10. Cheng X, Blumenthal RM. 1996. Finding a basis for flipping bases. Structure 4:639-45
    • (1996) Structure , vol.4 , pp. 639-645
    • Cheng, X.1    Blumenthal, R.M.2
  • 11
    • 0031025997 scopus 로고    scopus 로고
    • Defective transcription-coupled repair of oxidative damage in Cockayne syndrome patients from XP group G
    • 11. Cooper PK, Nouspikel T, Clarkson SG, Leadon SA. 1997. Defective transcription-coupled repair of oxidative damage in Cockayne syndrome patients from XP group G. Science 275:990-93
    • (1997) Science , vol.275 , pp. 990-993
    • Cooper, P.K.1    Nouspikel, T.2    Clarkson, S.G.3    Leadon, S.A.4
  • 13
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: Enzymology and biology
    • 13. Demple B, Harrison L. 1994. Repair of oxidative damage to DNA: enzymology and biology. Annu. Rev. Biochem. 63:915-48
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 15
    • 0018926091 scopus 로고
    • DNA N-glycosylases and UV repair
    • 15. Demple B, Linn S. 1980. DNA N-glycosylases and UV repair. Nature 287: 203-8
    • (1980) Nature , vol.287 , pp. 203-208
    • Demple, B.1    Linn, S.2
  • 16
    • 0025800612 scopus 로고
    • Preferential recognition of I-T base-pairs in the initiation of excision-repair by hypoxanthine-DNA glycosylase
    • 16. Dianov G, Lindahl T. 1991. Preferential recognition of I-T base-pairs in the initiation of excision-repair by hypoxanthine-DNA glycosylase. Nucleic Acids Res. 19: 3829-33
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3829-3833
    • Dianov, G.1    Lindahl, T.2
  • 17
    • 0028604549 scopus 로고
    • Unified catalytic mechanism for DNA glycosylases
    • 17. Dodson ML, Michaels ML, Lloyd RS. 1994. Unified catalytic mechanism for DNA glycosylases. J. Biol. Chem. 269: 32709-12
    • (1994) J. Biol. Chem. , vol.269 , pp. 32709-32712
    • Dodson, M.L.1    Michaels, M.L.2    Lloyd, R.S.3
  • 18
    • 0027301692 scopus 로고
    • Evidence for an imino intermediate in the T4 endonuclease V reaction
    • 18. Dodson ML, Schrock RD III, Lloyd RS. 1993. Evidence for an imino intermediate in the T4 endonuclease V reaction. Biochemistry 32:8284-90
    • (1993) Biochemistry , vol.32 , pp. 8284-8290
    • Dodson, M.L.1    Schrock R.D. III2    Lloyd, R.S.3
  • 19
    • 0025120572 scopus 로고
    • The enzymology of apurinic/apyrimidinic endonucleases
    • 19. Doetsch PW, Cunningham RP. 1990. The enzymology of apurinic/apyrimidinic endonucleases. Mutat. Res. 236:173-201
    • (1990) Mutat. Res. , vol.236 , pp. 173-201
    • Doetsch, P.W.1    Cunningham, R.P.2
  • 20
    • 0029929070 scopus 로고    scopus 로고
    • The helix-hairpin-helix DNA-binding motif: A structural basis for nonsequence-specific recognition of DNA
    • 20. Doherty AJ, Serpell LC, Ponting CP. 1996. The helix-hairpin-helix DNA-binding motif: a structural basis for nonsequence-specific recognition of DNA. Nucleic Acids Res. 24:2488-97
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2488-2497
    • Doherty, A.J.1    Serpell, L.C.2    Ponting, C.P.3
  • 21
    • 0023782193 scopus 로고
    • Purification and properties of mitochondrial uracil-DNA glycosylase from rat liver
    • 21. Domena JD, Timmer RT, Dicharry SA, Mosbaugh DW. 1988. Purification and properties of mitochondrial uracil-DNA glycosylase from rat liver. Biochemistry 27:6742-51
    • (1988) Biochemistry , vol.27 , pp. 6742-6751
    • Domena, J.D.1    Timmer, R.T.2    Dicharry, S.A.3    Mosbaugh, D.W.4
  • 22
    • 0025257431 scopus 로고
    • Biological significance of facilitated diffusion in protein-DNA interactions. Applications to T4 endonuclease V-initiated DNA repair
    • 22. Dowd DR, Lloyd RS. 1990. Biological significance of facilitated diffusion in protein-DNA interactions. Applications to T4 endonuclease V-initiated DNA repair. J. Biol. Chem. 265:3424-31
    • (1990) J. Biol. Chem. , vol.265 , pp. 3424-3431
    • Dowd, D.R.1    Lloyd, R.S.2
  • 23
    • 0023056224 scopus 로고
    • Synthesis and properties of oligonucleotides containing 2′-deoxynebularine and 2′-deoxyxanthosine
    • 23. Eritja R, Horowitz DM, Walker PA, Ziehler-Martin JP, Boosalis MS, et al. 1986. Synthesis and properties of oligonucleotides containing 2′-deoxynebularine and 2′-deoxyxanthosine. Nucleic Acids Res. 14:8135-53
    • (1986) Nucleic Acids Res. , vol.14 , pp. 8135-8153
    • Eritja, R.1    Horowitz, D.M.2    Walker, P.A.3    Ziehler-Martin, J.P.4    Boosalis, M.S.5
  • 24
    • 0030013201 scopus 로고    scopus 로고
    • Relationship between DNA repair and transcription
    • 24. Friedberg EC. 1996. Relationship between DNA repair and transcription. Annu. Rev. Biochem. 65:15-42
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 15-42
    • Friedberg, E.C.1
  • 26
    • 0017381612 scopus 로고
    • Endonuclease from Escherichia coli that acts specifically upon duplex DNA damaged by ultraviolet light, osmium, acid or X-rays
    • 26. Gates FT III, Linn S. 1977. Endonuclease from Escherichia coli that acts specifically upon duplex DNA damaged by ultraviolet light, osmium, acid or X-rays. J. Biol. Chem. 252:2802-7
    • (1977) J. Biol. Chem. , vol.252 , pp. 2802-2807
    • Gates F.T. III1    Linn, S.2
  • 27
    • 0030999894 scopus 로고    scopus 로고
    • Aging processes, DNA damage, and repair
    • 27. Gilchrest BA, Bohr VA. 1997. Aging processes, DNA damage, and repair. FASEB J. 11:322-30
    • (1997) FASEB J. , vol.11 , pp. 322-330
    • Gilchrest, B.A.1    Bohr, V.A.2
  • 28
    • 0030475264 scopus 로고    scopus 로고
    • Specific recognition of A/G and A/7,8-dihydro-8-oxoguanine (8-oxoG) mismatches by Escherichia coli MutY: Removal of the C-terminal domain preferentially affects A/8-oxoG recognition
    • 28. Gogos A, Cillo J, Clarke ND, Lu A-L. 1996. Specific recognition of A/G and A/7,8-dihydro-8-oxoguanine (8-oxoG) mismatches by Escherichia coli MutY: removal of the C-terminal domain preferentially affects A/8-oxoG recognition. Biochemistry 35:16665-71
    • (1996) Biochemistry , vol.35 , pp. 16665-16671
    • Gogos, A.1    Cillo, J.2    Clarke, N.D.3    Lu, A.-L.4
  • 29
    • 0030728449 scopus 로고    scopus 로고
    • The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites
    • 29. Gorman MA, Morera S, Rothwell DG, de La Fortelle E, Mol CD, et al. 1997. The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites. EMBO J. 16:6548-58
    • (1997) EMBO J. , vol.16 , pp. 6548-6558
    • Gorman, M.A.1    Morera, S.2    Rothwell, D.G.3    De La Fortelle, E.4    Mol, C.D.5
  • 30
    • 0027324378 scopus 로고
    • Mutagenesis by 8-oxoguanine: An enemy within
    • 30. Grollman AP, Moriya M. 1993. Mutagenesis by 8-oxoguanine: an enemy within. Trends Genet. 9:246-49
    • (1993) Trends Genet. , vol.9 , pp. 246-249
    • Grollman, A.P.1    Moriya, M.2
  • 31
    • 0031763884 scopus 로고    scopus 로고
    • MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily
    • 31. Guan Y, Manuel RC, Arvai AS, Parikh SS, Mol CD, et al. 1998. MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily. Nat. Struct. Biol. 5:1058-64
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1058-1064
    • Guan, Y.1    Manuel, R.C.2    Arvai, A.S.3    Parikh, S.S.4    Mol, C.D.5
  • 33
    • 0028596398 scopus 로고
    • Transcription-coupled repair and human disease
    • 33. Hanawalt PC. 1994. Transcription-coupled repair and human disease. Science 266:1957-58
    • (1994) Science , vol.266 , pp. 1957-1958
    • Hanawalt, P.C.1
  • 35
    • 0023857601 scopus 로고
    • Hypoxanthine-DNA glycosylase from Escherichia coli. Partial purification and properties
    • 35. Harosh I, Sperling J. 1988. Hypoxanthine-DNA glycosylase from Escherichia coli. Partial purification and properties. J. Biol. Chem. 263:3328-34
    • (1988) J. Biol. Chem. , vol.263 , pp. 3328-3334
    • Harosh, I.1    Sperling, J.2
  • 36
    • 0028305721 scopus 로고
    • New substrates for old enzymes. 5-hydroxy-2′-deoxycytidine and 5-hydroxy-2′-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA glycosylase, while 5-hydroxy-2′-deoxyuridine is a substrate for uracil DNA N-glycosylase
    • 36. Hatahet Z, Kow YW, Purmal AA, Cunningham RP, Wallace SS. 1994. New substrates for old enzymes. 5-hydroxy-2′-deoxycytidine and 5-hydroxy-2′-deoxyuridine are substrates for Escherichia coli endonuclease III and formamidopyrimidine DNA glycosylase, while 5-hydroxy-2′-deoxyuridine is a substrate for uracil DNA N-glycosylase. J. Biol. Chem. 269:18814-20
    • (1994) J. Biol. Chem. , vol.269 , pp. 18814-18820
    • Hatahet, Z.1    Kow, Y.W.2    Purmal, A.A.3    Cunningham, R.P.4    Wallace, S.S.5
  • 37
    • 0027304370 scopus 로고
    • Characterization of the effects of a thymine glycol residue on the structure, dynamics, and stability of duplex DNA by NMR
    • 37. Kao JY, Goljer I, Phan TA, Bolton PH. 1993. Characterization of the effects of a thymine glycol residue on the structure, dynamics, and stability of duplex DNA by NMR. J. Biol. Chem. 268:17787-93
    • (1993) J. Biol. Chem. , vol.268 , pp. 17787-17793
    • Kao, J.Y.1    Goljer, I.2    Phan, T.A.3    Bolton, P.H.4
  • 38
    • 0021106244 scopus 로고
    • Characterization of the Escherichia coli X-ray endonuclease, endonuclease III
    • 38. Katcher HL, Wallace SS. 1983. Characterization of the Escherichia coli X-ray endonuclease, endonuclease III. Biochemistry 22:4071-81
    • (1983) Biochemistry , vol.22 , pp. 4071-4081
    • Katcher, H.L.1    Wallace, S.S.2
  • 39
    • 0030035663 scopus 로고    scopus 로고
    • Excision of cytosine and thymine from DNA by mutants of human uracil-DNA glycosylase
    • 39. Kavli B, Slupphaug G, Mol CD, Arvai AS, Petersen SB, et al. 1996. Excision of cytosine and thymine from DNA by mutants of human uracil-DNA glycosylase. EMBO J. 15:3442-47
    • (1996) EMBO J. , vol.15 , pp. 3442-3447
    • Kavli, B.1    Slupphaug, G.2    Mol, C.D.3    Arvai, A.S.4    Petersen, S.B.5
  • 40
    • 0023641840 scopus 로고
    • Conformational changes in the oligonucleotide duplex d(GCGTTGCG)-d(CGCAACGC) induced by formation of a cis-syn thymine dimer
    • 40. Kemmick J, Boelens R, Koning TMG, Kaptein R, van der Marel GA, van Boom JH. 1987. Conformational changes in the oligonucleotide duplex d(GCGTTGCG)-d(CGCAACGC) induced by formation of a cis-syn thymine dimer. Eur. J. Biochem. 162:37-43
    • (1987) Eur. J. Biochem. , vol.162 , pp. 37-43
    • Kemmick, J.1    Boelens, R.2    Koning, T.M.G.3    Kaptein, R.4    Van Der Marel, G.A.5    Van Boom, J.H.6
  • 41
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase β and the XRCCI protein
    • 41. Kubota Y, Nash RA, Klungland A, Schär P, Barnes DE, Lindahl T. 1996. Reconstitution of DNA base excision-repair with purified human proteins: interaction between DNA polymerase β and the XRCCI protein. EMBO J. 15:6662-70
    • (1996) EMBO J. , vol.15 , pp. 6662-6670
    • Kubota, Y.1    Nash, R.A.2    Klungland, A.3    Schär, P.4    Barnes, D.E.5    Lindahl, T.6
  • 42
    • 0001195990 scopus 로고    scopus 로고
    • Structure of a duplex DNA containing a thymine glycol residue in solution
    • 42. Kung HC, Bolton PH. 1997. Structure of a duplex DNA containing a thymine glycol residue in solution. J. Biol. Chem. 272: 9227-36
    • (1997) J. Biol. Chem. , vol.272 , pp. 9227-9236
    • Kung, H.C.1    Bolton, P.H.2
  • 45
    • 0026354983 scopus 로고
    • DNase I-induced DNA conformation. 2 Å structure of a DNase I-octamer complex
    • 45. Lahm A, Suck D. 1991. DNase I-induced DNA conformation. 2 Å structure of a DNase I-octamer complex. J. Mol. Biol. 222:645-67
    • (1991) J. Mol. Biol. , vol.222 , pp. 645-667
    • Lahm, A.1    Suck, D.2
  • 46
    • 0029127485 scopus 로고
    • The interaction of T4 endonuclease V E23Q mutant with thymine dimer-and tetrahydrofuran-containing DNA
    • 46. Latham KA, Manuel RC, Lloyd RS. 1995. The interaction of T4 endonuclease V E23Q mutant with thymine dimer-and tetrahydrofuran-containing DNA. J. Bacteriol. 177:5166-68
    • (1995) J. Bacteriol. , vol.177 , pp. 5166-5168
    • Latham, K.A.1    Manuel, R.C.2    Lloyd, R.S.3
  • 47
    • 0028125823 scopus 로고
    • Nuclear magnetic resonance study of the interaction of T4 endonuclease V with DNA
    • 47. Lee BJ, Sakashita H, Ohkubo T, Ikehara M, Doi T, et al. 1994. Nuclear magnetic resonance study of the interaction of T4 endonuclease V with DNA. Biochemistry 33:57-64
    • (1994) Biochemistry , vol.33 , pp. 57-64
    • Lee, B.J.1    Sakashita, H.2    Ohkubo, T.3    Ikehara, M.4    Doi, T.5
  • 48
    • 0025342965 scopus 로고
    • Repair of intrinsic DNA lesions
    • 48. Lindahl T. 1990. Repair of intrinsic DNA lesions. Mutat. Res. 238.305-11
    • (1990) Mutat. Res. , vol.238 , pp. 305-311
    • Lindahl, T.1
  • 49
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • 49. Lindahl T. 1993. Instability and decay of the primary structure of DNA. Nature 362:709-15
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 50
    • 0023919219 scopus 로고
    • Regulation and expression of the adaptive response to alkylating agents
    • 50. Lindahl T, Sedgwick B, Sekiguchi M, Nakabeppu Y. 1988. Regulation and expression of the adaptive response to alkylating agents. Annu. Rev. Biochem. 57:133-57
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 133-157
    • Lindahl, T.1    Sedgwick, B.2    Sekiguchi, M.3    Nakabeppu, Y.4
  • 51
    • 0022037404 scopus 로고
    • Apurinic sites as mutagenic intermediates
    • 51. Loeb LA. 1985. Apurinic sites as mutagenic intermediates. Cell 40:483-84
    • (1985) Cell , vol.40 , pp. 483-484
    • Loeb, L.A.1
  • 52
    • 0030018681 scopus 로고    scopus 로고
    • Identification of the structural and functional domains of MutY, an Escherichia coli DNA mismatch repair enzyme
    • 52. Manuel RC, Czerwinski EW, Lloyd RS. 1996. Identification of the structural and functional domains of MutY, an Escherichia coli DNA mismatch repair enzyme. J. Biol. Chem. 271:16218-26
    • (1996) J. Biol. Chem. , vol.271 , pp. 16218-16226
    • Manuel, R.C.1    Czerwinski, E.W.2    Lloyd, R.S.3
  • 53
    • 0030987556 scopus 로고    scopus 로고
    • Cloning, overexpression, and biochemical characterization of the catalytic domain of MutY
    • 53. Manuel RC, Lloyd RS. 1997. Cloning, overexpression, and biochemical characterization of the catalytic domain of MutY. Biochemistry 36:11140-52
    • (1997) Biochemistry , vol.36 , pp. 11140-11152
    • Manuel, R.C.1    Lloyd, R.S.2
  • 54
    • 0027930608 scopus 로고
    • Crystal structure of a DNA duplex containing 8-hydroxyde-oxyguanine-adenine base-pairs
    • 54. McAuley-Hecht KE, Leonard GA, Gibson NJ, Thomson JB, Watson WP, et al. 1994. Crystal structure of a DNA duplex containing 8-hydroxyde-oxyguanine-adenine base-pairs. Biochemistry 33:10266-70
    • (1994) Biochemistry , vol.33 , pp. 10266-10270
    • McAuley-Hecht, K.E.1    Leonard, G.A.2    Gibson, N.J.3    Thomson, J.B.4    Watson, W.P.5
  • 55
    • 0026684849 scopus 로고
    • Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA
    • 55. Michaels ML, Cruz C, Grollman AP, Miller JH. 1992. Evidence that MutY and MutM combine to prevent mutations by an oxidatively damaged form of guanine in DNA. Proc. Natl. Acad. Sci. USA 89:7022-25
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 7022-7025
    • Michaels, M.L.1    Cruz, C.2    Grollman, A.P.3    Miller, J.H.4
  • 56
    • 0029943449 scopus 로고    scopus 로고
    • Mismatch repair in replication fidelity, genetic recombination, and cancer biology
    • 56. Modrich P, Lahue R. 1996. Mismatch repair in replication fidelity, genetic recombination, and cancer biology. Annu. Rev. Biochem. 65:101-33
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 101-133
    • Modrich, P.1    Lahue, R.2
  • 57
    • 0029084487 scopus 로고
    • Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: Protein mimicry of DNA
    • 57. Mol CD, Arvai AS, Sanderson RJ, Slupphaug G, Kavli B, et al. 1995a. Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA. Cell 82:701-8
    • (1995) Cell , vol.82 , pp. 701-708
    • Mol, C.D.1    Arvai, A.S.2    Sanderson, R.J.3    Slupphaug, G.4    Kavli, B.5
  • 58
    • 0028934537 scopus 로고
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: Structural basis for specificity and catalysis
    • 58. Mol CD, Arvai AS, Slupphaug G, Kavli B, Alseth I, et al. 1995b. Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis. Cell 80:869-78
    • (1995) Cell , vol.80 , pp. 869-878
    • Mol, C.D.1    Arvai, A.S.2    Slupphaug, G.3    Kavli, B.4    Alseth, I.5
  • 59
    • 0028923440 scopus 로고
    • Structure and function of the multifunctional DNA-repair enzyme exonuclease III
    • 59. Mol CD, Kuo C-F, Thayer MM, Cunningham RP, Tainer JA. 1995c. Structure and function of the multifunctional DNA-repair enzyme exonuclease III. Nature 374:381-86
    • (1995) Nature , vol.374 , pp. 381-386
    • Mol, C.D.1    Kuo, C.-F.2    Thayer, M.M.3    Cunningham, R.P.4    Tainer, J.A.5
  • 60
    • 0001882582 scopus 로고    scopus 로고
    • Structural phylogenetics of DNA base-excision repair
    • ed. F Eckstein, DMJ Lilley, Berlin: Springer-Verlag
    • 60. Mol CD, Parikh SS, Lo TP, Tainer JA. 1998. Structural phylogenetics of DNA base-excision repair. In Nucleic Acids & Molecular Biology, ed. F Eckstein, DMJ Lilley, 12:29-69. Berlin: Springer-Verlag
    • (1998) Nucleic Acids & Molecular Biology , vol.12 , pp. 29-69
    • Mol, C.D.1    Parikh, S.S.2    Lo, T.P.3    Tainer, J.A.4
  • 61
    • 0029013675 scopus 로고
    • Crystal structure of a pyrimidine dimer-specific excision repair enzyme from bacteriophage T4: Refinement at 1.45 Å and X-ray analysis of the three active site mutants
    • 61. Morikawa K, Ariyoshi M, Vassylyev DG, Matsumoto O, Katayanagi K, Ohtsuka E. 1995. Crystal structure of a pyrimidine dimer-specific excision repair enzyme from bacteriophage T4: refinement at 1.45 Å and X-ray analysis of the three active site mutants. J. Mol. Biol. 249:360-75
    • (1995) J. Mol. Biol. , vol.249 , pp. 360-375
    • Morikawa, K.1    Ariyoshi, M.2    Vassylyev, D.G.3    Matsumoto, O.4    Katayanagi, K.5    Ohtsuka, E.6
  • 62
    • 0026544541 scopus 로고
    • X-ray structure of T4 endonuclease V: An excision repair enzyme specific for a pyrimidine dimer
    • 62. Morikawa K, Matsumoto O, Tsujimoto M, Katayanagi K, Ariyoshi M, et al. 1992. X-ray structure of T4 endonuclease V: an excision repair enzyme specific for a pyrimidine dimer. Science 256:523-26
    • (1992) Science , vol.256 , pp. 523-526
    • Morikawa, K.1    Matsumoto, O.2    Tsujimoto, M.3    Katayanagi, K.4    Ariyoshi, M.5
  • 63
    • 0020490817 scopus 로고
    • Metabolism of dITP in HeLa cell extracts, incorporation into DNA by isolated nuclei and release of hypoxanthine from DNA by a hypoxanthine-DNA glycosylase activity
    • 63. Myrnes B, Guddal PH, Krokan H. 1982. Metabolism of dITP in HeLa cell extracts, incorporation into DNA by isolated nuclei and release of hypoxanthine from DNA by a hypoxanthine-DNA glycosylase activity. Nucleic Acids Res. 10:3693-701
    • (1982) Nucleic Acids Res. , vol.10 , pp. 3693-3701
    • Myrnes, B.1    Guddal, P.H.2    Krokan, H.3
  • 64
    • 0030220956 scopus 로고    scopus 로고
    • Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily
    • 64. Nash HM, Bruner SD, Scharer OD, Kawate T, Addona TA, et al. 1996. Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily. Curr. Biol. 6:968-80
    • (1996) Curr. Biol. , vol.6 , pp. 968-980
    • Nash, H.M.1    Bruner, S.D.2    Scharer, O.D.3    Kawate, T.4    Addona, T.A.5
  • 65
    • 0031239573 scopus 로고    scopus 로고
    • The critical active-site amine of the human 8-oxoguarine DNA glycosylase, hOggl: Direct identification, ablation and chemical reconstitution
    • 65. Nash HM, Lu R, Lane WS, Verdine GL. 1997. The critical active-site amine of the human 8-oxoguarine DNA glycosylase, hOggl: direct identification, ablation and chemical reconstitution. Chem. Biol. 4:693-702
    • (1997) Chem. Biol. , vol.4 , pp. 693-702
    • Nash, H.M.1    Lu, R.2    Lane, W.S.3    Verdine, G.L.4
  • 66
    • 0027383758 scopus 로고
    • The purification of a mismatch-specific thymine-DNA glycosylase from HeLa cells
    • 66. Neddermann P, Jirieny J. 1993. The purification of a mismatch-specific thymine-DNA glycosylase from HeLa cells. J. Biol. Chem. 268:21218-24
    • (1993) J. Biol. Chem. , vol.268 , pp. 21218-21224
    • Neddermann, P.1    Jirieny, J.2
  • 67
    • 0030999231 scopus 로고    scopus 로고
    • Role of specific amino acid residues in T4 endonuclease V that alter nontarget DNA binding
    • 67. Nyaga SG, Dodson ML, Lloyd RS. 1997. Role of specific amino acid residues in T4 endonuclease V that alter nontarget DNA binding. Biochemistry 36:4080-88
    • (1997) Biochemistry , vol.36 , pp. 4080-4088
    • Nyaga, S.G.1    Dodson, M.L.2    Lloyd, R.S.3
  • 68
    • 0031961907 scopus 로고    scopus 로고
    • Direct measurement of the substrate preference of uracil-DNA glycosylase
    • 68. Panayotou G, Brown T, Barlow T, Pearl LH, Savva R. 1998. Direct measurement of the substrate preference of uracil-DNA glycosylase. J. Biol. Chem. 273:45-50
    • (1998) J. Biol. Chem. , vol.273 , pp. 45-50
    • Panayotou, G.1    Brown, T.2    Barlow, T.3    Pearl, L.H.4    Savva, R.5
  • 69
    • 0032167424 scopus 로고    scopus 로고
    • Base-excision repair initiation revealed by crystal structures and DNA-binding kinetics of human uracil-DNA glycosylase bound to DNA
    • 69. Parikh SS, Mol CD, Slupphaug G, Bharati S, Krokan HE, Tainer JA. 1998. Base-excision repair initiation revealed by crystal structures and DNA-binding kinetics of human uracil-DNA glycosylase bound to DNA. EMBO J. 17:5214-26
    • (1998) EMBO J. , vol.17 , pp. 5214-5226
    • Parikh, S.S.1    Mol, C.D.2    Slupphaug, G.3    Bharati, S.4    Krokan, H.E.5    Tainer, J.A.6
  • 70
    • 0031574192 scopus 로고    scopus 로고
    • Base excision repair enzyme family portrait: Integrating the structure and chemistry of an entire DNA repair pathway
    • 70. Parikh SS, Mol CD, Tainer JA. 1997. Base excision repair enzyme family portrait: integrating the structure and chemistry of an entire DNA repair pathway. Structure 5:1543-50
    • (1997) Structure , vol.5 , pp. 1543-1550
    • Parikh, S.S.1    Mol, C.D.2    Tainer, J.A.3
  • 71
    • 0028812143 scopus 로고
    • Crystal structure of DNA photolyase from Escherichia coli
    • 71. Park H-W, Kim S-T, Sancar A, Deisenhofer J. 1995. Crystal structure of DNA photolyase from Escherichia coli. Science 268:1866-72
    • (1995) Science , vol.268 , pp. 1866-1872
    • Park, H.-W.1    Kim, S.-T.2    Sancar, A.3    Deisenhofer, J.4
  • 73
    • 0029817866 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase beta complexed with DNA: Implications for catalytic mechanism, processivity, and fidelity
    • 73. Pelletier H, Sawaya MR, Wolfe W, Wilson SH, Kraut J. 1996. Crystal structures of human DNA polymerase beta complexed with DNA: implications for catalytic mechanism, processivity, and fidelity. Biochemistry 35:12742-61
    • (1996) Biochemistry , vol.35 , pp. 12742-12761
    • Pelletier, H.1    Sawaya, M.R.2    Wolfe, W.3    Wilson, S.H.4    Kraut, J.5
  • 74
    • 0030018848 scopus 로고    scopus 로고
    • Specific interaction of DNA polymerase β and DNA ligase I in a multiprotein base excision repair complex from bovine testis
    • 74. Prasad R, Singhal RK, Srivastava DK, Molina JT, Tomkinson AE, Wilson SH. 1996. Specific interaction of DNA polymerase β and DNA ligase I in a multiprotein base excision repair complex from bovine testis. J. Biol. Chem. 271:16000-7
    • (1996) J. Biol. Chem. , vol.271 , pp. 16000-16007
    • Prasad, R.1    Singhal, R.K.2    Srivastava, D.K.3    Molina, J.T.4    Tomkinson, A.E.5    Wilson, S.H.6
  • 75
    • 0017236583 scopus 로고
    • An endonuclease from Escherichia coli that introduces single polynucleotide chain scissions in ultraviolet-irradiated DNA
    • 75. Radman M. 1976. An endonuclease from Escherichia coli that introduces single polynucleotide chain scissions in ultraviolet-irradiated DNA. J. Biol. Chem. 251:1438-45
    • (1976) J. Biol. Chem. , vol.251 , pp. 1438-1445
    • Radman, M.1
  • 76
    • 0032574770 scopus 로고    scopus 로고
    • Activation of apurinic/apyrimidinic endonuclease in human cells by reactive oxygen species and its correlation with their adaptive response to genotoxicity of free radicals
    • 76. Ramana CV, Boldogh I, Izumi T, Mitra S. 1998. Activation of apurinic/apyrimidinic endonuclease in human cells by reactive oxygen species and its correlation with their adaptive response to genotoxicity of free radicals. Proc. Natl. Acad. Sci. USA 95:5061-66
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5061-5066
    • Ramana, C.V.1    Boldogh, I.2    Izumi, T.3    Mitra, S.4
  • 77
    • 0028117141 scopus 로고
    • Structure and function of DNA photolyase
    • 77. Sancar A. 1994. Structure and function of DNA photolyase. Biochemistry 11:2-9
    • (1994) Biochemistry , vol.11 , pp. 2-9
    • Sancar, A.1
  • 78
    • 0028239225 scopus 로고
    • Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases
    • 78. Saparbaev M, Laval J. 1994. Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases. Proc. Natl. Acad. Sci. USA 91:5872-77
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 5872-5877
    • Saparbaev, M.1    Laval, J.2
  • 79
    • 0028959237 scopus 로고
    • The structural basis of specific base-excision repair by uracil-DNA glycosylase
    • 79. Savva R, McAuley-Hecht K, Brown T, Pearl L. 1995. The structural basis of specific base-excision repair by uracil-DNA glycosylase. Nature 373:487-93
    • (1995) Nature , vol.373 , pp. 487-493
    • Savva, R.1    McAuley-Hecht, K.2    Brown, T.3    Pearl, L.4
  • 80
    • 0029115366 scopus 로고
    • Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil glycosylase inhibitor protein complex
    • 80. Savva R, Pearl LH. 1995. Nucleotide mimicry in the crystal structure of the uracil-DNA glycosylase-uracil glycosylase inhibitor protein complex. Nat. Struct. Biol. 2:752-57
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 752-757
    • Savva, R.1    Pearl, L.H.2
  • 81
    • 0038342180 scopus 로고    scopus 로고
    • Specific binding of a designed abasic site analog to multiple DNA glycosylases
    • 81. Scharer OD, Nash HM, Jiricny J, Laval J, Verdine GL. 1998. Specific binding of a designed abasic site analog to multiple DNA glycosylases. J. Biol. Chem. 273:8592-97
    • (1998) J. Biol. Chem. , vol.273 , pp. 8592-8597
    • Scharer, O.D.1    Nash, H.M.2    Jiricny, J.3    Laval, J.4    Verdine, G.L.5
  • 82
    • 0026075807 scopus 로고
    • Reductive methylation of the amino terminus of endonuclease V eradicates catalytic activities. Evidence for an essential role of the amino terminus in the chemical mechanisms of catalysis
    • 82. Schrock RD III, Lloyd RS. 1991. Reductive methylation of the amino terminus of endonuclease V eradicates catalytic activities. Evidence for an essential role of the amino terminus in the chemical mechanisms of catalysis. J. Biol. Chem. 266:17631-39
    • (1991) J. Biol. Chem. , vol.266 , pp. 17631-17639
    • Schrock R.D. III1    Lloyd, R.S.2
  • 84
    • 0028933306 scopus 로고
    • Properties of a recombinant human uracil-DNA glycosylase from the UNG-gene and evidence that the UNG-gene encodes the major uracil-DNA glycosylase
    • 84. Slupphaug G, Eftedal I, Kavli B, Bharati S, Helle MM, et al. 1995. Properties of a recombinant human uracil-DNA glycosylase from the UNG-gene and evidence that the UNG-gene encodes the major uracil-DNA glycosylase. Biochemistry 34:128-38
    • (1995) Biochemistry , vol.34 , pp. 128-138
    • Slupphaug, G.1    Eftedal, I.2    Kavli, B.3    Bharati, S.4    Helle, M.M.5
  • 85
    • 0029904839 scopus 로고    scopus 로고
    • A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA
    • 85. Slupphaug G, Mol CD, Kavli B, Arvai AS, Krokan HE, Tainer JA. 1996. A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA. Nature 384:87-92
    • (1996) Nature , vol.384 , pp. 87-92
    • Slupphaug, G.1    Mol, C.D.2    Kavli, B.3    Arvai, A.S.4    Krokan, H.E.5    Tainer, J.A.6
  • 86
    • 0016692306 scopus 로고
    • Endonucleolytic incision of X-irradiated deoxyribonucleic acid by extracts of Escherichia coli
    • 86. Strniste GF, Wallace SS. 1975. Endonucleolytic incision of X-irradiated deoxyribonucleic acid by extracts of Escherichia coli. Proc. Natl. Acad. Sci. USA 72:1997-2001
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 1997-2001
    • Strniste, G.F.1    Wallace, S.S.2
  • 87
    • 0022476864 scopus 로고
    • Structure of DNase I at 2.0 Å resolution suggests a mechanism for binding to and cutting DNA
    • 87. Suck D, Oefner C. 1986. Structure of DNase I at 2.0 Å resolution suggests a mechanism for binding to and cutting DNA. Nature 321:620-25
    • (1986) Nature , vol.321 , pp. 620-625
    • Suck, D.1    Oefner, C.2
  • 89
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • 89. Thayer MM, Ahern H, Xing D, Cunningham RP, Tainer JA. 1995. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 14:4108-20
    • (1995) EMBO J. , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.3    Cunningham, R.P.4    Tainer, J.A.5
  • 90
    • 0031878710 scopus 로고    scopus 로고
    • Double-strand break repair mediated by DNA end-joining
    • 90. Tsukamoto Y, Ikeda H. 1998. Double-strand break repair mediated by DNA end-joining. Genes Cells 3:135-44
    • (1998) Genes Cells , vol.3 , pp. 135-144
    • Tsukamoto, Y.1    Ikeda, H.2
  • 91
    • 0029896229 scopus 로고    scopus 로고
    • Cloning and expression in E. coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine
    • 91. van der Kemp PA, Thomas D, Barbey R, de Oliveira R, Boiteux S. 1996. Cloning and expression in E. coli of the OGG1 gene of Saccharomyces cerevisiae, which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine. Proc. Natl. Acad. Sci. USA 93:5197-202
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 5197-5202
    • Van Der Kemp, P.A.1    Thomas, D.2    Barbey, R.3    De Oliveira, R.4    Boiteux, S.5
  • 93
    • 0028863468 scopus 로고
    • Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNA substrate: Structural basis for damaged DNA recognition
    • 93. Vassylyev DG, Kashiwagi T, Mikami Y, Ariyoshi M, Iwai S, et al. 1995. Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNA substrate: structural basis for damaged DNA recognition. Cell 83:773-82
    • (1995) Cell , vol.83 , pp. 773-782
    • Vassylyev, D.G.1    Kashiwagi, T.2    Mikami, Y.3    Ariyoshi, M.4    Iwai, S.5
  • 94
    • 0030589691 scopus 로고    scopus 로고
    • Precluding uracil from DNA
    • 94. Vassylyev DG, Morikawa K. 1996. Precluding uracil from DNA. Structure 4: 1381-85
    • (1996) Structure , vol.4 , pp. 1381-1385
    • Vassylyev, D.G.1    Morikawa, K.2
  • 95
    • 0031149139 scopus 로고    scopus 로고
    • How do DNA repair proteins locate damaged bases in the genome?
    • 95. Verdine GL, Bruner SD. 1997. How do DNA repair proteins locate damaged bases in the genome? Chem. Biol. 4:329-34
    • (1997) Chem. Biol. , vol.4 , pp. 329-334
    • Verdine, G.L.1    Bruner, S.D.2
  • 96
    • 0026495424 scopus 로고
    • Uracil-DNA glycosylases preferentially excise mispaired uracil
    • 96. Verri A, Mazzarello P, Spadari S, Focher F. 1992. Uracil-DNA glycosylases preferentially excise mispaired uracil. Biochem. J. 287:1007-10
    • (1992) Biochem. J. , vol.287 , pp. 1007-1010
    • Verri, A.1    Mazzarello, P.2    Spadari, S.3    Focher, F.4
  • 99
    • 0030839750 scopus 로고    scopus 로고
    • Abasic site binding by the human apurinic endonuclease, Ape, and determination of the DNA contact sites
    • 99. Wilson DM III, Takeshita M, Demple B. 1997. Abasic site binding by the human apurinic endonuclease, Ape, and determination of the DNA contact sites. Nucleic Acids Res. 25:933-39
    • (1997) Nucleic Acids Res. , vol.25 , pp. 933-939
    • Wilson D.M. III1    Takeshita, M.2    Demple, B.3
  • 100
    • 0029001186 scopus 로고
    • Incision activity of human apurinic endonuclease (Ape) at abasic site analogs in DNA
    • 100. Wilson DM III, Takeshita M, Grollman AP, Demple B. 1995. Incision activity of human apurinic endonuclease (Ape) at abasic site analogs in DNA. J. Biol. Chem. 270:16002-7
    • (1995) J. Biol. Chem. , vol.270 , pp. 16002-16007
    • Wilson D.M. III1    Takeshita, M.2    Grollman, A.P.3    Demple, B.4
  • 101
    • 0030768038 scopus 로고    scopus 로고
    • Nucleotide excision repair in mammalian cells
    • 101. Wood RD. 1997. Nucleotide excision repair in mammalian cells. J. Biol. Chem. 272:23465-68
    • (1997) J. Biol. Chem. , vol.272 , pp. 23465-23468
    • Wood, R.D.1
  • 102
    • 16044372779 scopus 로고    scopus 로고
    • Three-dimensional structure of a DNA repair enzyme, 3-methyladenine DNA glycosylase II, from Escherichia coli
    • 102. Yamagata Y, Kato M, Odawara K, Tokuno Y, Nakashima Y, et al. 1996. Three-dimensional structure of a DNA repair enzyme, 3-methyladenine DNA glycosylase II, from Escherichia coli. Cell 86:311-19
    • (1996) Cell , vol.86 , pp. 311-319
    • Yamagata, Y.1    Kato, M.2    Odawara, K.3    Tokuno, Y.4    Nakashima, Y.5


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