메뉴 건너뛰기




Volumn 407, Issue 3, 1998, Pages 203-215

Mammalian base excision repair and DNA polymerase beta

Author keywords

Abasic site; Apurinic apyrimidinic site; Base excision repair; DNA polymerase beta; DNA polymerase delta; DNA polymerase epsilon; DNA repair

Indexed keywords

DNA DIRECTED DNA POLYMERASE BETA;

EID: 0032100860     PISSN: 09218777     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0921-8777(98)00002-0     Document Type: Article
Times cited : (268)

References (97)
  • 2
    • 0020016636 scopus 로고
    • DNA repair enzymes
    • [2] T. Lindahl, DNA repair enzymes, Annu. Rev. Biochem. 51 (1982) 61-87.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 61-87
    • Lindahl, T.1
  • 3
    • 0026620267 scopus 로고
    • The repair of DNA alkylation damage by methyltransferases and glycosylases
    • [3] L.D. Samson, The repair of DNA alkylation damage by methyltransferases and glycosylases, Essays Biochem. 27 (1992) 69-78.
    • (1992) Essays Biochem. , vol.27 , pp. 69-78
    • Samson, L.D.1
  • 6
    • 0029347105 scopus 로고
    • Structure and function of apurinic/apyrimidinic endonucleases
    • [6] G. Barzilay, I.D. Hickson, Structure and function of apurinic/apyrimidinic endonucleases, Bioessays 17 (1995) 713-719.
    • (1995) Bioessays , vol.17 , pp. 713-719
    • Barzilay, G.1    Hickson, I.D.2
  • 8
    • 0024161399 scopus 로고
    • AP endonucleases and DNA glycosylases that recognize oxidative DNA damage
    • [8] S.S. Wallace, AP endonucleases and DNA glycosylases that recognize oxidative DNA damage, Environ. Mol. Mutagen. 12 (1988) 431-477.
    • (1988) Environ. Mol. Mutagen. , vol.12 , pp. 431-477
    • Wallace, S.S.1
  • 9
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: Enzymology and biology
    • [9] B. Demple, L. Harrison, Repair of oxidative damage to DNA: enzymology and biology, Annu. Rev. Biochem. 63 (1994) 915-948.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915-948
    • Demple, B.1    Harrison, L.2
  • 10
    • 0025718595 scopus 로고
    • cDNA and deduced amino acid sequence of a mouse DNA repair enzyme (APEX nuclease) with significant homology to Escherichia coli exonuclease III
    • [10] S. Seki, K. Akiyama, S. Watanabe, M. Hatsushika, S. Ikeda, K. Tsutsui, cDNA and deduced amino acid sequence of a mouse DNA repair enzyme (APEX nuclease) with significant homology to Escherichia coli exonuclease III, J. Biol. Chem. 266 (1991) 20797-20802.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20797-20802
    • Seki, S.1    Akiyama, K.2    Watanabe, S.3    Hatsushika, M.4    Ikeda, S.5    Tsutsui, K.6
  • 11
    • 0025120572 scopus 로고
    • The enzymology of apurinic/apyrimidinic endonucleases
    • [11] P.W. Doetsch, R.P. Cunningham, The enzymology of apurinic/apyrimidinic endonucleases, Mutat. Res. 236 (1990) 173-201
    • (1990) Mutat. Res. , vol.236 , pp. 173-201
    • Doetsch, P.W.1    Cunningham, R.P.2
  • 12
    • 0026583944 scopus 로고
    • Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity
    • [12] S. Xanthoudakis, T. Curran, Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity, EMBO J. 11 (1992) 653-665.
    • (1992) EMBO J. , vol.11 , pp. 653-665
    • Xanthoudakis, S.1    Curran, T.2
  • 13
    • 0025936119 scopus 로고
    • Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants
    • [13] C.N. Robson, I.D. Hickson, Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants, Nucleic Acids Res. 19 (1991) 5519-5523.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5519-5523
    • Robson, C.N.1    Hickson, I.D.2
  • 14
    • 0026323008 scopus 로고
    • Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: Definition of a family of DNA repair enzymes
    • [14] B. Demple, T. Herman, D.S. Chen, Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes, Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 11450-11454.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 11450-11454
    • Demple, B.1    Herman, T.2    Chen, D.S.3
  • 15
    • 0026683715 scopus 로고
    • cDNA cloning, sequencing, expression and possible domain structure of human APEX nuclease homologous to Escherichia coli exonuclease III
    • [15] S. Seki, M. Hatsushika, S. Watanabe, K. Akiyama, K. Nagao, K. Tsutsui, cDNA cloning, sequencing, expression and possible domain structure of human APEX nuclease homologous to Escherichia coli exonuclease III, Biochim. Biophys. Acta 1131 (1992) 287-299.
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 287-299
    • Seki, S.1    Hatsushika, M.2    Watanabe, S.3    Akiyama, K.4    Nagao, K.5    Tsutsui, K.6
  • 16
    • 0029028964 scopus 로고
    • Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair
    • [16] Y. Matsumoto, L. Kim, Excision of deoxyribose phosphate residues by DNA polymerase beta during DNA repair, Science 269 (1995) 699-702.
    • (1995) Science , vol.269 , pp. 699-702
    • Matsumoto, Y.1    Kim, L.2
  • 18
    • 0025314841 scopus 로고
    • Mismatch-specific thymine DNA glycosylase and DNA polymerase β mediate the correction of G · T mispairs in nuclear extracts from human cells
    • [18] K. Wiebauer, J. Jiricny, Mismatch-specific thymine DNA glycosylase and DNA polymerase β mediate the correction of G · T mispairs in nuclear extracts from human cells, Proc. Natl. Acad. Sci. U.S.A. 87 (1990) 5842-5845.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 5842-5845
    • Wiebauer, K.1    Jiricny, J.2
  • 19
    • 0026589375 scopus 로고
    • Generation of single-nucleotide repair patches following excision of uracil residues from DNA
    • [19] G. Dianov, A. Price, T. Lindahl, Generation of single-nucleotide repair patches following excision of uracil residues from DNA, Mol. Cell. Biol. 12 (1992) 1605-1612.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 1605-1612
    • Dianov, G.1    Price, A.2    Lindahl, T.3
  • 20
    • 0030957997 scopus 로고    scopus 로고
    • Second pathway for completion of human DNA base excision repair: Reconstitution with purified proteins and requirement for DNase IV (FEN I)
    • [20] A. Klungland, T. Lindahl, Second pathway for completion of human DNA base excision repair: reconstitution with purified proteins and requirement for DNase IV (FEN I), EMBO J. 26 (1997) 3341-3348.
    • (1997) EMBO J. , vol.26 , pp. 3341-3348
    • Klungland, A.1    Lindahl, T.2
  • 21
    • 0030018848 scopus 로고    scopus 로고
    • Specific interaction of DNA polymerase beta and DNA ligase I in a multiprotein base excision repair complex from bovine testis
    • [21] R. Prasad, R.K. Singhal, D.K. Srivastava, J.T. Molina, A.E. Tomkinson, S.H. Wilson, Specific interaction of DNA polymerase beta and DNA ligase I in a multiprotein base excision repair complex from bovine testis, J. Biol. Chem. 271 (1996) 16000-16007.
    • (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
  • 22
    • 0025054962 scopus 로고
    • Nucleotide excision repair in Escherichia coli
    • [22] B. Van Houten, Nucleotide excision repair in Escherichia coli, Microbiol. Rev. 54 (1990) 18-51.
    • (1990) Microbiol. Rev. , vol.54 , pp. 18-51
    • Van Houten, B.1
  • 23
    • 0029892790 scopus 로고    scopus 로고
    • DNA excision repair
    • [23] A. Sancar, DNA excision repair, Annu. Rev. Biochem. 65 (1996) 43-81.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 43-81
    • Sancar, A.1
  • 24
    • 0028606403 scopus 로고
    • Mechanisms of DNA excision repair
    • [24] A. Sancar, Mechanisms of DNA excision repair, Science 266 (1994) 1954-1956.
    • (1994) Science , vol.266 , pp. 1954-1956
    • Sancar, A.1
  • 25
    • 0023664684 scopus 로고
    • Oligodeoxynucleotides containing synthetic abasic sites: Model substrates for DNA polymerases and apurinic/apyrimidinic endonucleases
    • [25] M. Takeshita, C.N. Chang, F. Johnson, S. Will, A.P. Grollman, Oligodeoxynucleotides containing synthetic abasic sites: model substrates for DNA polymerases and apurinic/apyrimidinic endonucleases, J. Biol. Chem. 262 (1987) 10171-10179.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10171-10179
    • Takeshita, M.1    Chang, C.N.2    Johnson, F.3    Will, S.4    Grollman, A.P.5
  • 26
    • 0028151464 scopus 로고
    • DNA damages processed by base excision repair: Biological consequences
    • [26] S.S. Wallace, DNA damages processed by base excision repair: biological consequences, Int. J. Radiat. Biol. 66 (1994) 579-589.
    • (1994) Int. J. Radiat. Biol. , vol.66 , pp. 579-589
    • Wallace, S.S.1
  • 27
    • 0028799991 scopus 로고
    • Recognition and processing of damaged DNA
    • [27] T. Lindahl, Recognition and processing of damaged DNA, J. Cell Sci. 19 (1995) 73-77.
    • (1995) J. Cell Sci. , vol.19 , pp. 73-77
    • Lindahl, T.1
  • 29
    • 0027965229 scopus 로고
    • Proliferating cell nuclear antigen-dependent abasic site repair in Xenopus laevis oocytes: An alternative pathway of base excision DNA repair
    • [29] Y. Matsumoto, K. Kim, D.F. Bogenhage, Proliferating cell nuclear antigen-dependent abasic site repair in Xenopus laevis oocytes: an alternative pathway of base excision DNA repair, Cell. Biol. 14 (1994) 6187-6189.
    • (1994) Cell. Biol. , vol.14 , pp. 6187-6189
    • Matsumoto, Y.1    Kim, K.2    Bogenhage, D.F.3
  • 30
    • 0030787013 scopus 로고    scopus 로고
    • What structural features determine repair enzyme specificity and mechanism in chemically modified DNA?
    • [30] B. Singer, B. Hang, What structural features determine repair enzyme specificity and mechanism in chemically modified DNA?, Chem. Res. Toxicol. 10 (1997) 713-732.
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 713-732
    • Singer, B.1    Hang, B.2
  • 31
    • 0030881789 scopus 로고    scopus 로고
    • Repair of oxidative damage to nuclear and mitochondrial DNA in mammalian cells
    • [31] D.L. Croteau, V.A. Bohr, Repair of oxidative damage to nuclear and mitochondrial DNA in mammalian cells, J. Biol. Chem. 272 (1997) 25409-25412.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25409-25412
    • Croteau, D.L.1    Bohr, V.A.2
  • 32
    • 0031172802 scopus 로고    scopus 로고
    • A mammalian DNA repair enzyme that excises oxidatively damaged guanine maps to a locus frequently lost in lung cancer
    • [32] R. Lu, H.M. Nash, G.L. Verdine, A mammalian DNA repair enzyme that excises oxidatively damaged guanine maps to a locus frequently lost in lung cancer, Curr. Biol. 7 (1997) 397-407.
    • (1997) Curr. Biol. , vol.7 , pp. 397-407
    • Lu, R.1    Nash, H.M.2    Verdine, G.L.3
  • 34
    • 0028966181 scopus 로고
    • DNA polymerase β conducts the gap filling step in uracil-initiated base excision repair in a bovine testis nuclear extract
    • [34] R.K. Singhal, R. Prasad, S.H. Wilson, DNA polymerase β conducts the gap filling step in uracil-initiated base excision repair in a bovine testis nuclear extract, J. Biol. Chem. 270 (1995) 949-957.
    • (1995) J. Biol. Chem. , vol.270 , pp. 949-957
    • Singhal, R.K.1    Prasad, R.2    Wilson, S.H.3
  • 36
    • 0023651476 scopus 로고
    • Nicks 3′ or 5′ to AP sites or to mispaired bases, and one-nucleotide gaps can be sealed by T4 DNA ligase
    • [36] C. Goffin, V. Bailly, W.G. Venly, Nicks 3′ or 5′ to AP sites or to mispaired bases, and one-nucleotide gaps can be sealed by T4 DNA ligase, Nucleic Acids Res. 15 (1987) 8711-8755.
    • (1987) Nucleic Acids Res. , vol.15 , pp. 8711-8755
    • Goffin, C.1    Bailly, V.2    Venly, W.G.3
  • 37
    • 0026323008 scopus 로고
    • Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: Definition of a family of DNA repair enzymes
    • [37] B. Demple, T. Herman, D.S. Chen, Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes, Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 11450-11454.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 11450-11454
    • Demple, B.1    Herman, T.2    Chen, D.S.3
  • 38
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision repair with purified human proteins: Interaction between DNA polymerase beta and the XRCC1 protein
    • [38] Y. Kubota, R.A. Nash, A. Klungland, P. Schar, D.E. Barnes, T. Lindahl, Reconstitution of DNA base excision repair with purified human proteins: interaction between DNA polymerase beta and the XRCC1 protein, EMBO J. 15 (1996) 6662-6670.
    • (1996) EMBO J. , vol.15 , pp. 6662-6670
    • Kubota, Y.1    Nash, R.A.2    Klungland, A.3    Schar, P.4    Barnes, D.E.5    Lindahl, T.6
  • 40
    • 0025088519 scopus 로고
    • Studies of the domain structure of mammalian DNA polymerase β: Identification of a discrete template binding domain
    • [40] A. Kumar, S.G. Widen, K.R. Williams, P. Kedar, R.L. Karpel, S.H. Wilson, Studies of the domain structure of mammalian DNA polymerase β: identification of a discrete template binding domain, J. Biol. Chem. 265 (1990) 2124-2131.
    • (1990) J. Biol. Chem. , vol.265 , pp. 2124-2131
    • Kumar, A.1    Widen, S.G.2    Williams, K.R.3    Kedar, P.4    Karpel, R.L.5    Wilson, S.H.6
  • 41
    • 0025333457 scopus 로고
    • Identification and properties of the catalytic domain of mammalian DNA polymerase beta
    • [41] A. Kumar, J. Abbotts, E. Karawya, S.H. Wilson, Identification and properties of the catalytic domain of mammalian DNA polymerase beta, Biochemistry 29 (1990) 7156-7159.
    • (1990) Biochemistry , vol.29 , pp. 7156-7159
    • Kumar, A.1    Abbotts, J.2    Karawya, E.3    Wilson, S.H.4
  • 42
    • 0026002415 scopus 로고
    • Spectroscopic studies of the structural domains of mammalian DNA β-polymerase
    • [42] J.R. Casas-Finet, A. Kumar, G. Morris, S.H. Wilson, R.L. Karpel, Spectroscopic studies of the structural domains of mammalian DNA β-polymerase, J. Biol. Chem. 266 (1991) 19618-19625.
    • (1991) J. Biol. Chem. , vol.266 , pp. 19618-19625
    • Casas-Finet, J.R.1    Kumar, A.2    Morris, G.3    Wilson, S.H.4    Karpel, R.L.5
  • 43
    • 0026457493 scopus 로고
    • Mammalian DNA polymerase β: Characterization of a 16-kDa transdomain fragment containing the nucleic acid-binding activities of the native enzyme
    • [43] J.R. Casas-Finet, A. Kumar, R.L. Karpel, S.H. Wilson, Mammalian DNA polymerase β: characterization of a 16-kDa transdomain fragment containing the nucleic acid-binding activities of the native enzyme, Biochemistry 31 (1992) 10272-10280.
    • (1992) Biochemistry , vol.31 , pp. 10272-10280
    • Casas-Finet, J.R.1    Kumar, A.2    Karpel, R.L.3    Wilson, S.H.4
  • 44
    • 0027374513 scopus 로고
    • Identification of residues in the single-stranded DNA-binding site of the 8-kDa domain of the 8-kDa domain of rat DNA polymerase β by UV crosslinking
    • [44] R. Prasad, A. Kumar, S.G. Widen, J.R. Casas-Finet, S.H. Wilson, Identification of residues in the single-stranded DNA-binding site of the 8-kDa domain of the 8-kDa domain of rat DNA polymerase β by UV crosslinking, J. Biol. Chem. 268 (1993) 22746-22755.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22746-22755
    • Prasad, R.1    Kumar, A.2    Widen, S.G.3    Casas-Finet, J.R.4    Wilson, S.H.5
  • 45
    • 0028338562 scopus 로고
    • Studies of gapped DNA substrate binding by mammalian DNA polymerase β: Dependence on 5′-phosphate group
    • [45] R. Prasad, W.A. Beard, S.H. Wilson, Studies of gapped DNA substrate binding by mammalian DNA polymerase β: dependence on 5′-phosphate group, J. Biol. Chem. 269 (1994) 18096-18101.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18096-18101
    • Prasad, R.1    Beard, W.A.2    Wilson, S.H.3
  • 46
    • 0029892846 scopus 로고    scopus 로고
    • Evidence for an imino intermediate in the DNA polymerase β deoxyribose phosphate excision reaction
    • [46] C.E. Piersen, R. Prasad, S.H. Wilson, R.S. Lloyd, Evidence for an imino intermediate in the DNA polymerase β deoxyribose phosphate excision reaction, J. Biol. Chem. 271 (1996) 17811-17815.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17811-17815
    • Piersen, C.E.1    Prasad, R.2    Wilson, S.H.3    Lloyd, R.S.4
  • 47
    • 0027179827 scopus 로고
    • Short gap-filling synthesis by DNA polymerase β is processive
    • [47] R.K. Singhal, S.H. Wilson, Short gap-filling synthesis by DNA polymerase β is processive, J. Biol. Chem. 268 (1993) 15906-15911.
    • (1993) J. Biol. Chem. , vol.268 , pp. 15906-15911
    • Singhal, R.K.1    Wilson, S.H.2
  • 48
    • 0031038053 scopus 로고    scopus 로고
    • Abasic translesion synthesis by DNA polymerase β violates the 'A-Rule': Novel types of nucleotide incorporation by human DNA polymerase β at an abasic lesion in different sequence contexts
    • [48] E. Efrati, G. Tocco, R. Eritja, S.H. Wilson, M.F. Goodman, Abasic translesion synthesis by DNA polymerase β violates the 'A-Rule': novel types of nucleotide incorporation by human DNA polymerase β at an abasic lesion in different sequence contexts, J. Biol. Chem. 272 (1997) 2559-2569.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2559-2569
    • Efrati, E.1    Tocco, G.2    Eritja, R.3    Wilson, S.H.4    Goodman, M.F.5
  • 49
    • 0030783515 scopus 로고    scopus 로고
    • Increased activity and fidelity of DNA polymerase β on single-nucleotide gapped DNA
    • [49] A.M. Chagovetz, J.B. Sweasy, B.D. Preston, Increased activity and fidelity of DNA polymerase β on single-nucleotide gapped DNA, J. Biol. Chem. 272 (1997) 27501-27504.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27501-27504
    • Chagovetz, A.M.1    Sweasy, J.B.2    Preston, B.D.3
  • 50
    • 0028062807 scopus 로고
    • Characterization of the tryptophan fluorescence and hydrodynamic properties of rat DNA polymerase β: Molecular asymmetry and metal-induced conformational change
    • [50] S.-J. Kim, M.S. Lewis, J.R. Knutson, D. Porter, A. Kumar, S.H. Wilson, Characterization of the tryptophan fluorescence and hydrodynamic properties of rat DNA polymerase β: molecular asymmetry and metal-induced conformational change, J. Mol. Biol. 244 (1994) 224-235.
    • (1994) J. Mol. Biol. , vol.244 , pp. 224-235
    • Kim, S.-J.1    Lewis, M.S.2    Knutson, J.R.3    Porter, D.4    Kumar, A.5    Wilson, S.H.6
  • 51
    • 0027974928 scopus 로고
    • A crystal structure of the catalytic domain of DNA polymerase beta
    • [51] J.F. Davies, R.J. Almassy, Z. Hostomska, R.A. Ferre, Z. Hostomsky, A crystal structure of the catalytic domain of DNA polymerase beta, Cell 76 (1994) 1123-1133.
    • (1994) Cell , vol.76 , pp. 1123-1133
    • Davies, J.F.1    Almassy, R.J.2    Hostomska, Z.3    Ferre, R.A.4    Hostomsky, Z.5
  • 52
    • 0028136070 scopus 로고
    • Crystal structure of rat DNA polymerase β reveals a conserved polymerase catalytic site
    • [52] M.R. Sawaya, H. Pelletier, A. Kumar, S.H. Wilson, J. Kraut, Crystal structure of rat DNA polymerase β reveals a conserved polymerase catalytic site, Science 264 (1994) 2930-2935.
    • (1994) Science , vol.264 , pp. 2930-2935
    • Sawaya, M.R.1    Pelletier, H.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 53
    • 0028049441 scopus 로고
    • Structures of ternary complexes of rat DNA polymerase β, a DNA template · primer, and ddCTP
    • [53] H. Pelletier, M.R. Sawaya, A. Kumar, S.H. Wilson, J. Kraut, Structures of ternary complexes of rat DNA polymerase β, a DNA template · primer, and ddCTP, Science 264 (1994) 1891-1903.
    • (1994) Science , vol.264 , pp. 1891-1903
    • Pelletier, H.1    Sawaya, M.R.2    Kumar, A.3    Wilson, S.H.4    Kraut, J.5
  • 54
    • 0029817866 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase β complexed with DNA, implications for catalytic mechanism, processivity, and fidelity
    • [54] H. Pelletier, M.R. Sawaya, W. Wolfle, S.H. Wilson, J. Kraut, Crystal structures of human DNA polymerase β complexed with DNA, implications for catalytic mechanism, processivity, and fidelity, Biochemistry 35 (1996) 12742-12761.
    • (1996) Biochemistry , vol.35 , pp. 12742-12761
    • Pelletier, H.1    Sawaya, M.R.2    Wolfle, W.3    Wilson, S.H.4    Kraut, J.5
  • 55
    • 0029843045 scopus 로고    scopus 로고
    • A structural basis for metal ion mutagenicity and nucleotide selectivity in human DNA polymerase
    • [55] H. Pelletier, M.R. Sawaya, W. Wolfle, S.H. Wilson, J. Kraut, A structural basis for metal ion mutagenicity and nucleotide selectivity in human DNA polymerase, Biochemistry 35 (1996) 12762-12777.
    • (1996) Biochemistry , vol.35 , pp. 12762-12777
    • Pelletier, H.1    Sawaya, M.R.2    Wolfle, W.3    Wilson, S.H.4    Kraut, J.5
  • 56
    • 0030930760 scopus 로고    scopus 로고
    • Crystal structures of human DNA polymerase β complexed with gapped and nicked DNA: Evidence for an induced fit mechanism
    • [56] M.R. Sawaya, R. Prasad, S.H. Wilson, J. Kraut, H. Pelletier, Crystal structures of human DNA polymerase β complexed with gapped and nicked DNA: evidence for an induced fit mechanism, Biochemistry 36 (1997) 11205-11215.
    • (1997) Biochemistry , vol.36 , pp. 11205-11215
    • Sawaya, M.R.1    Prasad, R.2    Wilson, S.H.3    Kraut, J.4    Pelletier, H.5
  • 57
    • 0031985891 scopus 로고    scopus 로고
    • Impairment of proliferating cell nuclear antigen-dependent apurinic/apyrimidinic site repair on linear DNA
    • [57] S. Biade, R.W. Sobol, S.H. Wilson, Y. Matsumoto, Impairment of proliferating cell nuclear antigen-dependent apurinic/apyrimidinic site repair on linear DNA, J. Biol. Chem. 273 (1998) 898-902.
    • (1998) J. Biol. Chem. , vol.273 , pp. 898-902
    • Biade, S.1    Sobol, R.W.2    Wilson, S.H.3    Matsumoto, Y.4
  • 58
    • 0028934537 scopus 로고
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: Structural basis for specificity and catalysis
    • [58] C.D. Mol, A.S. Arvai, G. Slupphaug, B. Kavli, I. Alseth, H.E. Krokan, J.A. Tainer, Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis, Cell 80 (1995) 869-878.
    • (1995) Cell , vol.80 , pp. 869-878
    • Mol, C.D.1    Arvai, A.S.2    Slupphaug, G.3    Kavli, B.4    Alseth, I.5    Krokan, H.E.6    Tainer, J.A.7
  • 59
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • [59] M.M. Thayer, H. Ahern, D. Xing, R.P. Cunningham, J.A. Tainer, Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure, EMBO J. 14 (1995) 4108-4120.
    • (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
  • 60
    • 0024349250 scopus 로고
    • Active-site modification of mammalian DNA polymerase beta with pyridoxal 5′-phosphate: Mechanism of inhibition and identification of lysine 71 in the deoxynucleoside triphosphate-binding pocket
    • [60] A. Basu, P. Kedar, S.H. Wilson, M.J. Modak, Active-site modification of mammalian DNA polymerase beta with pyridoxal 5′-phosphate: mechanism of inhibition and identification of lysine 71 in the deoxynucleoside triphosphate-binding pocket, Biochemistry 28 (1989) 6305-6309.
    • (1989) Biochemistry , vol.28 , pp. 6305-6309
    • Basu, A.1    Kedar, P.2    Wilson, S.H.3    Modak, M.J.4
  • 61
    • 0030804836 scopus 로고    scopus 로고
    • Insights into the mechanism of the β-elimination catalyzed by the N-terminal domain of DNA polymerase β
    • [61] G.P. Mullen, W. Antuch, M.W. Maciejewski, R. Prasad, S.H. Wilson, Insights into the mechanism of the β-elimination catalyzed by the N-terminal domain of DNA polymerase β, Tetrahedron 53 (1997) 12057-12066.
    • (1997) Tetrahedron , vol.53 , pp. 12057-12066
    • Mullen, G.P.1    Antuch, W.2    Maciejewski, M.W.3    Prasad, R.4    Wilson, S.H.5
  • 62
    • 0027215749 scopus 로고
    • Mechanism of HIV-1 reverse transcriptase: Termination of processive synthesis on a natural DNA template is influenced by the sequence of the template · primer stem
    • [62] J. Abbotts, K. Bebenek, T.A. Kunkel, S.H. Wilson, Mechanism of HIV-1 reverse transcriptase: termination of processive synthesis on a natural DNA template is influenced by the sequence of the template · primer stem, J. Biol. Chem. 268 (1993) 10312-10323.
    • (1993) J. Biol. Chem. , vol.268 , pp. 10312-10323
    • Abbotts, J.1    Bebenek, K.2    Kunkel, T.A.3    Wilson, S.H.4
  • 65
    • 0010390038 scopus 로고    scopus 로고
    • Studies of human DNA polymerase β dRpase activity on AP endonuclease-incised abasic site DNA
    • In press
    • [65] R. Prasad, W.A. Beard, P. Strauss, S.H. Wilson, Studies of human DNA polymerase β dRpase activity on AP endonuclease-incised abasic site DNA, J. Biol. Chem., In press.
    • J. Biol. Chem.
    • Prasad, R.1    Beard, W.A.2    Strauss, P.3    Wilson, S.H.4
  • 66
    • 0029836483 scopus 로고    scopus 로고
    • Characterization of the metal ion binding helix-hairpin-helix motifs in human DNA polymerase β by X-ray structural analysis
    • [66] H. Pelletier, M.R. Sawaya, Characterization of the metal ion binding helix-hairpin-helix motifs in human DNA polymerase β by X-ray structural analysis, Biochemistry 35 (1996) 12778-12787.
    • (1996) Biochemistry , vol.35 , pp. 12778-12787
    • Pelletier, H.1    Sawaya, M.R.2
  • 67
    • 0030891201 scopus 로고    scopus 로고
    • Repair activity in DNA polymerases: A structurally conserved helix-hairpin-helix motif in base excision repair enzymes and in DNA polymerase β
    • [67] G.P. Mullen, S.H. Wilson, Repair activity in DNA polymerases: a structurally conserved helix-hairpin-helix motif in base excision repair enzymes and in DNA polymerase β, Biochemistry 36 (1997) 4713-4717.
    • (1997) Biochemistry , vol.36 , pp. 4713-4717
    • Mullen, G.P.1    Wilson, S.H.2
  • 68
    • 0029886039 scopus 로고    scopus 로고
    • Three-dimensional solution structure of the N-terminal domain of DNA polymerase Interaction with a single-stranded DNA polymerase β: Interaction with a single-stranded DNA oligomer
    • [68] D. Liu, R. Prasad, S.H. Wilson, E.F. DeRose, G.P. Mullen, Three-dimensional solution structure of the N-terminal domain of DNA polymerase Interaction with a single-stranded DNA polymerase β: interaction with a single-stranded DNA oligomer, Biochemistry 35 (1996) 6188-6200.
    • (1996) Biochemistry , vol.35 , pp. 6188-6200
    • Liu, D.1    Prasad, R.2    Wilson, S.H.3    Derose, E.F.4    Mullen, G.P.5
  • 69
    • 0029929070 scopus 로고    scopus 로고
    • The helix-hairpin-helix DNA-binding motif: A structural basis for non-sequence-specific recognition of DNA
    • [69] A.J. Doherty, L.C. Serpell, C.P. Ponting, The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA, Nucleic Acids Res. 24 (1996) 2488-2497.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2488-2497
    • Doherty, A.J.1    Serpell, L.C.2    Ponting, C.P.3
  • 70
    • 5544239019 scopus 로고    scopus 로고
    • Purification of a mammalian homolog of Escherichia coli endonuclease III: Identification of a bovine pyrimidine hydrate-thymine glycol DNA-glycosylase/AP lyase by irreversible cross linking to a thymine glycol-containing oligodeoxynucleotide
    • [70] T.P. Hubert, R.J. Boorstein, H.C. Kung, P.H. Bolton, D. Xing, R.P. Cunningham, G.W. Teebor, Purification of a mammalian homolog of Escherichia coli endonuclease III: identification of a bovine pyrimidine hydrate-thymine glycol DNA-glycosylase/AP lyase by irreversible cross linking to a thymine glycol-containing oligodeoxynucleotide, Biochemistry 35 (1996) 2505-2511.
    • (1996) Biochemistry , vol.35 , pp. 2505-2511
    • Hubert, T.P.1    Boorstein, R.J.2    Kung, H.C.3    Bolton, P.H.4    Xing, D.5    Cunningham, R.P.6    Teebor, G.W.7
  • 71
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • [71] M.M. Thayer, H. Ahern, D. Xing, R.P. Cunningham, J.A. Tainer, Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure, EMBO J. 14 (1995) 4108-4120.
    • (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
  • 72
    • 0029084487 scopus 로고
    • Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: Protein mimicry of DNA
    • [72] C.D. Mol, A.S. Arvai, R.J. Sanderson, G. Slupphaug, B. Kavli, H.E. Krokan, D.W. Mosbaug, J.A. Tainer, Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA, Cell 82 (1995) 701-708.
    • (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    Krokan, H.E.6    Mosbaug, D.W.7    Tainer, J.A.8
  • 73
    • 0029904839 scopus 로고    scopus 로고
    • A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA
    • [73] G. Slupphaug, C.D. Mol, B. Kavli, A.S. Arvai, H.E. Krokan, J.A. Tainer, A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA, Nature 384 (1996) 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
  • 74
    • 0028863468 scopus 로고
    • Atomic model of a pyrimidine dimer excision repair enzyme complexed with a DNA substrate: Structural basis for damaged DNA recognition
    • [74] D.G. Vassylyev, T. Kashiwagi, Y. Mikami, M. Ariyoshi, S. Iwai, E. Ohtsuka, 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
  • 75
    • 0030574226 scopus 로고    scopus 로고
    • Push and pull of base-flipping
    • [75] T.A. Kunkel, S.H. Wilson, Push and pull of base-flipping, Nature 384 (1996) 25-26.
    • (1996) Nature , vol.384 , pp. 25-26
    • Kunkel, T.A.1    Wilson, S.H.2
  • 77
    • 0024473938 scopus 로고
    • O6-ethylguanine carcinogenic lesions in DNA: An NMR study of O6etG · C pairing in dodecanucleotide duplexes
    • [77] M.W. Kalnick, B.F.L. Li, P.E. Swann, D.J. Patel, O6-ethylguanine carcinogenic lesions in DNA: an NMR study of O6etG · C pairing in dodecanucleotide duplexes, Biochemistry 28 (1989) 6170-6192.
    • (1989) Biochemistry , vol.28 , pp. 6170-6192
    • Kalnick, M.W.1    Li, B.F.L.2    Swann, P.E.3    Patel, D.J.4
  • 78
    • 0029886521 scopus 로고    scopus 로고
    • NMR study of the conformation of the 2-aminopurine:Cytosine mismatch in DNA
    • [78] P.A. Fagan, C. Fàbrega, R. Eritja, M.F. Goodman, D.E. Wemmer, NMR study of the conformation of the 2-aminopurine:cytosine mismatch in DNA, Biochemistry 35 (1996) 4026-4033.
    • (1996) Biochemistry , vol.35 , pp. 4026-4033
    • Fagan, P.A.1    Fàbrega, C.2    Eritja, R.3    Goodman, M.F.4    Wemmer, D.E.5
  • 79
    • 0025891866 scopus 로고
    • NMR structural studies of the ionizing radiation adduct 7-hydro-8-oxodeoxyguanosine (8-oxo-7H-dG) opposite deoxyadenosine in a DNA duplex: 8-oxo-7-dg(syn) · dA(anti) alignment at lesion site
    • [79] M. Kouchakdjian, V. Bodepudi, S. Shibutani, M. Eisenberg, F. Johnson, A.P. Grollman, D.J. Patel, NMR structural studies of the ionizing radiation adduct 7-hydro-8-oxodeoxyguanosine (8-oxo-7H-dG) opposite deoxyadenosine in a DNA duplex: 8-oxo-7-dg(syn) · dA(anti) alignment at lesion site, Biochemistry 30 (1991) 1403-1412.
    • (1991) Biochemistry , vol.30 , pp. 1403-1412
    • Kouchakdjian, M.1    Bodepudi, V.2    Shibutani, S.3    Eisenberg, M.4    Johnson, F.5    Grollman, A.P.6    Patel, D.J.7
  • 80
    • 0030585418 scopus 로고    scopus 로고
    • Finding a basis for flipping bases
    • [80] X. Cheng, R.M. Blumenthal, Finding a basis for flipping bases, Structure 4 (1996) 639-645.
    • (1996) Structure , vol.4 , pp. 639-645
    • Cheng, X.1    Blumenthal, R.M.2
  • 81
  • 82
    • 0022505062 scopus 로고
    • Structure of an adenine-cytosine base pair in DNA and its implications for mismatch repair
    • [82] W.N. Hunter, T. Brown, N.N. Anand, O. Kennard, Structure of an adenine-cytosine base pair in DNA and its implications for mismatch repair, Nature 320 (1986) 552-555.
    • (1986) Nature , vol.320 , pp. 552-555
    • Hunter, W.N.1    Brown, T.2    Anand, N.N.3    Kennard, O.4
  • 84
  • 87
    • 0029810085 scopus 로고    scopus 로고
    • Characterization of the DNA polymerase requirement of human base excision repair
    • [87] K. Nealon, I.D. Nicholl, M.K. Kenny, Characterization of the DNA polymerase requirement of human base excision repair, Nucleic Acids Res. 24 (1996) 3763-3770.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3763-3770
    • Nealon, K.1    Nicholl, I.D.2    Kenny, M.K.3
  • 88
    • 0032539979 scopus 로고    scopus 로고
    • Different DNA polymerases are involved in the short-and long-patch base excision repair in mammalian cells
    • [88] P. Fortini, B. Pascucci, R.W. Sobol, S.H. Wilson, E. Dogliotti, Different DNA polymerases are involved in the short-and long-patch base excision repair in mammalian cells, Biochemistry 37 (1998) 3575-3580.
    • (1998) Biochemistry , vol.37 , pp. 3575-3580
    • Fortini, P.1    Pascucci, B.2    Sobol, R.W.3    Wilson, S.H.4    Dogliotti, E.5
  • 89
    • 0030939690 scopus 로고    scopus 로고
    • Reconstitution of human base excision repair with purified proteins
    • [89] I.D. Nicholl, K. Nealon, M.K. Kenny, Reconstitution of human base excision repair with purified proteins, Biochemistry 36 (1997) 7557-7566.
    • (1997) Biochemistry , vol.36 , pp. 7557-7566
    • Nicholl, I.D.1    Nealon, K.2    Kenny, M.K.3
  • 90
    • 0027937618 scopus 로고
    • Assembly of DNA polymerase delta and epsilon holoenzymes depends on the geometry of the DNA template
    • [90] L.M. Podust, V.N. Podust, C. Floth, U. Hubscher, Assembly of DNA polymerase delta and epsilon holoenzymes depends on the geometry of the DNA template, Nucleic Acids Res. 22 (1994) 2970-2975.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 2970-2975
    • Podust, L.M.1    Podust, V.N.2    Floth, C.3    Hubscher, U.4
  • 91
    • 0029678248 scopus 로고    scopus 로고
    • Clamp loading, unloading and intrinsic stability of the PCNA, beta and gp45 sliding clamps of human, E. coli and T4 replicases
    • [91] N. Yao, J. Turner, Z. Kelman, P.T. Stukenberg, F. Dean, D. Shechter, Z.Q. Pan, J. Hurwitz, M. O'Donnell, Clamp loading, unloading and intrinsic stability of the PCNA, beta and gp45 sliding clamps of human, E. coli and T4 replicases, Genes Cells 1 (1996) 101-113.
    • (1996) Genes Cells , vol.1 , pp. 101-113
    • Yao, N.1    Turner, J.2    Kelman, Z.3    Stukenberg, P.T.4    Dean, F.5    Shechter, D.6    Pan, Z.Q.7    Hurwitz, J.8    O'Donnell, M.9
  • 92
    • 0028281443 scopus 로고
    • The characterization of a mammalian DNA structure-specific endonuclease
    • [92] J.J. Harrington, M.R. Lieber, The characterization of a mammalian DNA structure-specific endonuclease, EMBO J. 13 (1994) 1235-1246.
    • (1994) EMBO J. , vol.13 , pp. 1235-1246
    • Harrington, J.J.1    Lieber, M.R.2
  • 93
    • 0031054051 scopus 로고    scopus 로고
    • Enzymes and reactions at the eukaryotic DNA replication fork
    • [93] R.A. Bambara, R.S. Murante, L.A. Henricksen, Enzymes and reactions at the eukaryotic DNA replication fork, J. Biol. Chem. 272 (1997) 4647-4650.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4647-4650
    • Bambara, R.A.1    Murante, R.S.2    Henricksen, L.A.3
  • 94
    • 0029885134 scopus 로고    scopus 로고
    • Processing of branched DNA intermediates by a complex of human FEN-1 and PCNA
    • [94] X. Wu, J. Li, X. Li, C.L. Hsieh, P.M. Burgers, M.R. Lieber, Processing of branched DNA intermediates by a complex of human FEN-1 and PCNA, Nucleic Acids Res. 24 (1996) 2036-2043.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2036-2043
    • Wu, X.1    Li, J.2    Li, X.3    Hsieh, C.L.4    Burgers, P.M.5    Lieber, M.R.6
  • 95
    • 0029964484 scopus 로고    scopus 로고
    • dNTP binding site in rat DNA polymerase beta revealed by controlled proteolysis and azido photoprobe crosslinking
    • [95] D.K. Srivastava, R.K. Evans, A. Kumar, W.A. Beard, S.H. Wilson, dNTP binding site in rat DNA polymerase beta revealed by controlled proteolysis and azido photoprobe crosslinking, Biochemistry 35 (1996) 3728-3734.
    • (1996) Biochemistry , vol.35 , pp. 3728-3734
    • Srivastava, D.K.1    Evans, R.K.2    Kumar, A.3    Beard, W.A.4    Wilson, S.H.5
  • 96
    • 0032080334 scopus 로고    scopus 로고
    • Functional analysis of the amino-terminal 8-kDa domain of DNA polymerase beta as revealed by site-directed mutagenesis. DNA binding and 5′-deoxyribose phosphate lyase activities
    • [96] R. Prasad, Y.J. Chyan, W.A. Beard, M.W. Maciejewski, G.P. Mullen, S.H. Wilson, Functional analysis of the amino-terminal 8-kDa domain of DNA polymerase beta as revealed by site-directed mutagenesis. DNA binding and 5′-deoxyribose phosphate lyase activities, J. Biol. Chem. 273 (1998) 11121-11126.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11121-11126
    • Prasad, R.1    Chyan, Y.J.2    Beard, W.A.3    Maciejewski, M.W.4    Mullen, G.P.5    Wilson, S.H.6
  • 97
    • 0031883128 scopus 로고    scopus 로고
    • Structural insights into DNA polymerase β fidelity: Hold tight if you want it right
    • [97] W.A. Beard, S.H. Wilson, Structural insights into DNA polymerase β fidelity: hold tight if you want it right, Chemistry & Biology 5 (1998) R7-R13.
    • (1998) Chemistry & Biology , vol.5
    • Beard, W.A.1    Wilson, S.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.