메뉴 건너뛰기




Volumn 407, Issue 2, 1998, Pages 169-176

Activity of Escherichia coli DNA-glycosylases on DNA damaged by methylating and ethylating agents and influence of 3-substituted adenine derivatives

Author keywords

3 methyladenine DNA glycosylase (E. coli) inhibitor; AlkA protein; ANPG protein; DNA repair; Ethylated DNA; Fpg protein; Methylated DNA; TagA protein

Indexed keywords

ALKYLATING AGENT; DNA GLYCOSYLTRANSFERASE; RECOMBINANT ENZYME;

EID: 0031777550     PISSN: 09218777     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0921-8777(98)00005-6     Document Type: Article
Times cited : (69)

References (40)
  • 2
    • 0000785768 scopus 로고
    • Carcinogenesis by alkylating agents
    • C.E. Searle (Ed), ASC Monograph 182, American Chemical Society, Washington, DC
    • P.D. Lawley, Carcinogenesis by alkylating agents, in: C.E. Searle (Ed), Chemical Carcinogens, Vol. 1, ASC Monograph 182, American Chemical Society, Washington, DC, 1984, pp. 325-484.
    • (1984) Chemical Carcinogens , vol.1 , pp. 325-484
    • Lawley, P.D.1
  • 3
    • 0028808359 scopus 로고
    • Urinary excretion of 3-methyladenine and 3-ethyladenine after controlled exposure to tobacco smoke
    • A. Kopplin, G. Eberle-Adamkiewicz, K.H. Glusenkamp, P. Nehls, U. Kirstein, Urinary excretion of 3-methyladenine and 3-ethyladenine after controlled exposure to tobacco smoke, Carcinogenesis 16 (1995) 2637-2641.
    • (1995) Carcinogenesis , vol.16 , pp. 2637-2641
    • Kopplin, A.1    Eberle-Adamkiewicz, G.2    Glusenkamp, K.H.3    Nehls, P.4    Kirstein, U.5
  • 4
    • 0020341190 scopus 로고
    • Non-enzymatic methylation of DNA by the intracellular methyl group donor S-adenosyl-methionine is a potentially mutagenic reaction
    • B. Rydberg, T. Lindahl, Non-enzymatic methylation of DNA by the intracellular methyl group donor S-adenosyl-methionine is a potentially mutagenic reaction, EMBO J. 1 (1982) 211-216.
    • (1982) EMBO J. , vol.1 , pp. 211-216
    • Rydberg, B.1    Lindahl, T.2
  • 5
    • 37049065759 scopus 로고
    • The methylation of guanosine and related compounds with diazomethane
    • J.A. Haines, C.B. Reese, J.L. Todd, The methylation of guanosine and related compounds with diazomethane, J. Chem. Soc. (1962) 5281-5288.
    • (1962) J. Chem. Soc. , pp. 5281-5288
    • Haines, J.A.1    Reese, C.B.2    Todd, J.L.3
  • 6
    • 0021760535 scopus 로고
    • Two rotameric forms of open ring 7-methylguanine are present in alkylated polynucleotides
    • S. Boiteux, J. Belleney, B.P. Roques, J. Laval, Two rotameric forms of open ring 7-methylguanine are present in alkylated polynucleotides, Nucleic Acids Res. 12 (1984) 5429-5439.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 5429-5439
    • Boiteux, S.1    Belleney, J.2    Roques, B.P.3    Laval, J.4
  • 8
    • 0023898319 scopus 로고
    • Ring-opened 7-methylguanine residues in DNA are a block to in vitro DNA synthesis
    • T.R. O'Connor, S. Boiteux, J. Laval, Ring-opened 7-methylguanine residues in DNA are a block to in vitro DNA synthesis, Nucleic Acids Res. 16 (1988) 879-5894.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 879-5894
    • O'Connor, T.R.1    Boiteux, S.2    Laval, J.3
  • 9
    • 0017760103 scopus 로고
    • Two enzymes are required for strand incision in repair of alkylated DNA
    • J. Laval, Two enzymes are required for strand incision in repair of alkylated DNA, Nature 269 (1977) 829-831.
    • (1977) Nature , vol.269 , pp. 829-831
    • Laval, J.1
  • 10
    • 0028045942 scopus 로고
    • DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the AlkA enzyme in Escherichia coli
    • S. Bjelland, N.K. Birkeland, T. Benneche, G. Volden, E. Seeberg, DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the AlkA enzyme in Escherichia coli, J. Biol. Chem. 269 (1994) 30489-30495.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30489-30495
    • Bjelland, S.1    Birkeland, N.K.2    Benneche, T.3    Volden, G.4    Seeberg, E.5
  • 11
    • 0029936462 scopus 로고    scopus 로고
    • Excision of DNA adducts of nitrogen mustards by bacterial and mammalian 3-methyladenine-DNA glycosylases
    • W.B. Mattes, C.S. Lee, J. Laval, T. O'Connor, Excision of DNA adducts of nitrogen mustards by bacterial and mammalian 3-methyladenine-DNA glycosylases, Carcinogenesis 17 (1996) 643-648.
    • (1996) Carcinogenesis , vol.17 , pp. 643-648
    • Mattes, W.B.1    Lee, C.S.2    Laval, J.3    O'Connor, T.4
  • 12
    • 0030005132 scopus 로고    scopus 로고
    • Role of DNA repair enzymes in the cellular resistance to oxidative stress
    • J. Laval, Role of DNA repair enzymes in the cellular resistance to oxidative stress, Pathol. Biol. 44 (1996) 14-24.
    • (1996) Pathol. Biol. , vol.44 , pp. 14-24
    • Laval, J.1
  • 13
    • 0027759522 scopus 로고
    • Purification and characterization of human 3-methyladenine-DNA glycosylase
    • T.R. O'Connor, Purification and characterization of human 3-methyladenine-DNA glycosylase, Nucleic Acids Res. 21 (1993) 5561-5569.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 5561-5569
    • O'Connor, T.R.1
  • 14
    • 0025013468 scopus 로고
    • Physiological properties and repair of apurinic/apyrimidinic sites and imidazole ring-opened guanines in DNA
    • J. Laval, S. Boiteux, T.R. O'Connor, Physiological properties and repair of apurinic/apyrimidinic sites and imidazole ring-opened guanines in DNA, Mutat. Res. 233 (1990) 73-79.
    • (1990) Mutat. Res. , vol.233 , pp. 73-79
    • Laval, J.1    Boiteux, S.2    O'Connor, T.R.3
  • 15
    • 0025924488 scopus 로고
    • 6-benzylguanine analogues on sensitivity of human tumor cells to the cytotoxic effects of alkylating agents
    • 6-benzylguanine analogues on sensitivity of human tumor cells to the cytotoxic effects of alkylating agents, Cancer Res. 51 (1991) 3367-3372.
    • (1991) Cancer Res. , vol.51 , pp. 3367-3372
    • Dolan, M.E.1    Mitchell, R.B.2    Mummert, C.3    Moschel, R.C.4    Pegg, A.E.5
  • 16
    • 0023433565 scopus 로고
    • Formamidopyrimidine-DNA glycosylase of Escherichia coli: Cloning and sequencing of the fpg structural gene and overproduction of the protein
    • S. Boiteux, T.R. O'Connor, J. Laval, Formamidopyrimidine-DNA glycosylase of Escherichia coli: cloning and sequencing of the fpg structural gene and overproduction of the protein, EMBO J. 6 (1987) 3177-3183.
    • (1987) EMBO J. , vol.6 , pp. 3177-3183
    • Boiteux, S.1    O'Connor, T.R.2    Laval, J.3
  • 17
    • 0021685040 scopus 로고
    • Structure and expression of alkA gene of Escherichia coli involved in adaptive response to alkylating agents
    • Y. Nakabeppu, T. Miyala, H. Kondo, S. Iwanaga, M. Sekiguchi, Structure and expression of alkA gene of Escherichia coli involved in adaptive response to alkylating agents, J. Biol. Chem. 259 (1984) 13730-13736.
    • (1984) J. Biol. Chem. , vol.259 , pp. 13730-13736
    • Nakabeppu, Y.1    Miyala, T.2    Kondo, H.3    Iwanaga, S.4    Sekiguchi, M.5
  • 18
    • 0025108951 scopus 로고
    • Isolation and structure of a cDNA expressing a mammalian 3-methyladenine-DNA glycosylase
    • T.R. O'Connor, F. Laval, Isolation and structure of a cDNA expressing a mammalian 3-methyladenine-DNA glycosylase, EMBO J. 9 (1990) 3337-3342.
    • (1990) EMBO J. , vol.9 , pp. 3337-3342
    • O'Connor, T.R.1    Laval, F.2
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantisation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford, A rapid and sensitive method for the quantisation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 0017828018 scopus 로고
    • Properties of 3-methyladenine-DNA glycosylase from Escherichia coli
    • S. Riazuddin, T. Lindhal, Properties of 3-methyladenine-DNA glycosylase from Escherichia coli, Biochemistry 17 (1978) 2110-2118.
    • (1978) Biochemistry , vol.17 , pp. 2110-2118
    • Riazuddin, S.1    Lindhal, T.2
  • 21
    • 0020060168 scopus 로고
    • Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine
    • L. Thomas, C.H. Yang, A. Goldthwait, Two DNA glycosylases in Escherichia coli which release primarily 3-methyladenine, Biochemistry 21 (1982) 1162-1169.
    • (1982) Biochemistry , vol.21 , pp. 1162-1169
    • Thomas, L.1    Yang, C.H.2    Goldthwait, A.3
  • 22
    • 0017392934 scopus 로고
    • DNA N-glycosidases: Properties of uracil-DNA glycosidase from Escherichia coli
    • T. Lindahl, S. Ljungquist, W. Siegert, B. Nyberg, B. Sperens, DNA N-glycosidases: properties of uracil-DNA glycosidase from Escherichia coli, J. Biol. Chem. 252 (1977) 286-3294.
    • (1977) J. Biol. Chem. , vol.252 , pp. 286-3294
    • Lindahl, T.1    Ljungquist, S.2    Siegert, W.3    Nyberg, B.4    Sperens, B.5
  • 23
    • 0022545166 scopus 로고
    • Cloning of Micrococcus luteus 3-methyladenine-DNA glycosylase genes in Escherichia coli
    • J. Pierre, J. Laval, Cloning of Micrococcus luteus 3-methyladenine-DNA glycosylase genes in Escherichia coli, Gene 43 (1986) 139-146.
    • (1986) Gene , vol.43 , pp. 139-146
    • Pierre, J.1    Laval, J.2
  • 24
    • 0021331957 scopus 로고
    • DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation or ring contraction are functions of endonuclease III in Escherichia coli
    • L.H. Breimer, T. Lindahl, DNA glycosylase activities for thymine residues damaged by ring saturation, fragmentation or ring contraction are functions of endonuclease III in Escherichia coli, J. Biol. Chem. 259 (1984) 5543-5548.
    • (1984) J. Biol. Chem. , vol.259 , pp. 5543-5548
    • Breimer, L.H.1    Lindahl, T.2
  • 25
    • 0024347210 scopus 로고
    • Excision of the imidazole ring-opened form of N-2-aminofluorene-C(8)-guanine adduct in poly(dG-dC) by Escherichia coli formamidopyrimidine-DNA glycosylase
    • S. Boiteux, M. Bichara, R.P.P. Fuchs, J. Laval, Excision of the imidazole ring-opened form of N-2-aminofluorene-C(8)-guanine adduct in poly(dG-dC) by Escherichia coli formamidopyrimidine-DNA glycosylase, Carcinogenesis 10 (1989) 1905-1909.
    • (1989) Carcinogenesis , vol.10 , pp. 1905-1909
    • Boiteux, S.1    Bichara, M.2    Fuchs, R.P.P.3    Laval, J.4
  • 26
    • 0030005059 scopus 로고    scopus 로고
    • Reduction of the toxicity and mutagenicity of aziridine in mammalian cells harboring the Escherichia coli fpg gene
    • C. Cussac, F. Laval, Reduction of the toxicity and mutagenicity of aziridine in mammalian cells harboring the Escherichia coli fpg gene, Nucleic Acids Res. 24 (1996) 1742-1746.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 1742-1746
    • Cussac, C.1    Laval, F.2
  • 28
    • 0023047501 scopus 로고
    • Nucleotide sequence of the tag gene from Escherichia coli
    • A.M. Steinum, E. Seeberg, Nucleotide sequence of the tag gene from Escherichia coli, Nucleic Acids Res. 14 (1986) 3763-3772.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 3763-3772
    • Steinum, A.M.1    Seeberg, E.2
  • 29
    • 0025784273 scopus 로고
    • Human cDNA expressing a functional DNA glycosylase excising 3-methyladenine and 7-methylguanine
    • T.R. O'Connor, J. Laval, Human cDNA expressing a functional DNA glycosylase excising 3-methyladenine and 7-methylguanine, Biochem. Biophys. Res. Commun. 176 (1991) 1170-1177.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 1170-1177
    • O'Connor, T.R.1    Laval, J.2
  • 32
    • 0028934537 scopus 로고
    • Crystal structure and mutational analysis of human uracil-DNA glycosylase: Structural basis for specificity and catalysis
    • C.D. Mol, A.S. Arvai, G. Slupphang, B. Kavil, 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    Slupphang, G.3    Kavil, B.4    Alseth, I.5    Krokan, H.E.6    Tainer, J.A.7
  • 33
    • 0028959237 scopus 로고
    • The structural basis of specific base-excision repair by uracil-DNA glycosylase
    • R. Savva, K. McAuley-Hecht, T. Brown, L. Pearl, The structural basis of specific base-excision repair by uracil-DNA glycosylase, Nature 373 (1995) 487-493.
    • (1995) Nature , vol.373 , pp. 487-493
    • Savva, R.1    McAuley-Hecht, K.2    Brown, T.3    Pearl, L.4
  • 34
    • 0021528507 scopus 로고
    • 3-Methyladenine residues in DNA induce the SOS function sfiA in Escherichia coli
    • S. Boiteux, O. Huisman, J. Laval, 3-Methyladenine residues in DNA induce the SOS function sfiA in Escherichia coli, EMBO J. 3 (1984) 2569-2573.
    • (1984) EMBO J. , vol.3 , pp. 2569-2573
    • Boiteux, S.1    Huisman, O.2    Laval, J.3
  • 35
    • 0023145705 scopus 로고
    • Induction of SOS and adaptive responses by alkylating agents in Escherichia coli mutants deficient in 3-methyladenine-DNA glycosylase activities
    • R. Costa de Oliveira, J. Laval, S. Boiteux, Induction of SOS and adaptive responses by alkylating agents in Escherichia coli mutants deficient in 3-methyladenine-DNA glycosylase activities, Mutat. Res. 183 (1986) 11-20.
    • (1986) Mutat. Res. , vol.183 , pp. 11-20
    • De Costa Oliveira, R.1    Laval, J.2    Boiteux, S.3
  • 36
    • 0028116270 scopus 로고
    • The frequency of MMS-induced, umuDC-dependent, mutations declines during starvation in Escherichia coli
    • E. Grzesiuk, C. Janion, The frequency of MMS-induced, umuDC-dependent, mutations declines during starvation in Escherichia coli, Mol. Gen. Genet. 245 (1994) 486-492.
    • (1994) Mol. Gen. Genet. , vol.245 , pp. 486-492
    • Grzesiuk, E.1    Janion, C.2
  • 37
    • 0024538236 scopus 로고
    • Expression of DNA damage-inducible genes of Escherichia coli upon treatment with methylating, ethylating and propylating agents
    • M.R. Volkert, F.H. Gately, L.I. Hajec, Expression of DNA damage-inducible genes of Escherichia coli upon treatment with methylating, ethylating and propylating agents, Mutat. Res. 217 (1989) 109-115.
    • (1989) Mutat. Res. , vol.217 , pp. 109-115
    • Volkert, M.R.1    Gately, F.H.2    Hajec, L.I.3
  • 39
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair
    • H.E. Krokan, R. Standl, G. Slupphaug, DNA glycosylases in the base excision repair, Biochem. J. 325 (1997) 1-16.
    • (1997) Biochem. J. , vol.325 , pp. 1-16
    • Krokan, H.E.1    Standl, R.2    Slupphaug, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.