메뉴 건너뛰기




Volumn 9, Issue 12, 1999, Pages 653-656

A new member of the endonuclease III family of DNA repair enzymes that removes methylated purines from DNA

Author keywords

[No Author keywords available]

Indexed keywords

3 METHYLADENINE; 7 METHYLGUANINE; AQUIFEX AEOLICUS; CLONED GENE; DNA GLYCOSYLTRANSFERASE; DNA REPAIR; ENDONUCLEASE III; ENZYME ACTIVITY; ENZYME MECHANISM; ESCHERICHIA COLI; MESYLIC ACID METHYL ESTER; THERMOTOGA MARITIMA;

EID: 0033577974     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(99)80288-7     Document Type: Article
Times cited : (40)

References (28)
  • 1
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl T: Instability and decay of the primary structure of DNA. Nature 1993, 362:709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 3
    • 0028675314 scopus 로고
    • Reconstitution of the DNA base excision-repair pathway
    • Dianov G, Lindahl T: Reconstitution of the DNA base excision-repair pathway. Curr Biol 1994, 4:1069-1076.
    • (1994) Curr Biol , vol.4 , pp. 1069-1076
    • Dianov, G.1    Lindahl, T.2
  • 4
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylases in the base excision repair of DNA
    • Krokan HE, Standal R, Slupphaug G: DNA glycosylases in the base excision repair of DNA. Biochem J 1997, 325:1-16.
    • (1997) Biochem J , vol.325 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 6
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • Thayer MM, Ahern H, Xing D, Cunningham RP, Tainer JA: Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J 1995, 14:4108-4120.
    • (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
  • 7
    • 0023952376 scopus 로고
    • A selective recognition mode of a nucleic acid base by an aromatic amino acid: L-phenylalanine-7-methylguanosine 5′-monophosphate stacking interaction
    • Ishida T, Doi M, Inoue M: A selective recognition mode of a nucleic acid base by an aromatic amino acid: L-phenylalanine-7-methylguanosine 5′-monophosphate stacking interaction. Nucl Acids Res 1988, 16:6175-6190.
    • (1988) Nucl Acids Res , vol.16 , pp. 6175-6190
    • Ishida, T.1    Doi, M.2    Inoue, M.3
  • 8
    • 0023929705 scopus 로고
    • Specific ring interaction on the tryptophan-7-methylguanine system: Comparative crystallographic studies of indole derivatives-7-methylguanine base, nucleoside and nucleotide complexes
    • Ishida T, Doi M, Ueda H, Inoue M, Scheldrick GM: Specific ring interaction on the tryptophan-7-methylguanine system: comparative crystallographic studies of indole derivatives-7-methylguanine base, nucleoside and nucleotide complexes. J Am Chem Soc 1988, 110:2286-2294.
    • (1988) J Am Chem Soc , vol.110 , pp. 2286-2294
    • Ishida, T.1    Doi, M.2    Ueda, H.3    Inoue, M.4    Scheldrick, G.M.5
  • 9
    • 4243468938 scopus 로고    scopus 로고
    • The cation-π interaction
    • Ma JC, Dougherty DA: The cation-π interaction. Chem Rev 1997, 97:1303-1324.
    • (1997) Chem Rev , vol.97 , pp. 1303-1324
    • Ma, J.C.1    Dougherty, D.A.2
  • 11
    • 16044372779 scopus 로고    scopus 로고
    • Three-dimensional structure of a DNA repair enzyme, 3-methyladenine DNA glycosylase II, from Escherichia coli
    • Yamagata Y, Kato M, Odawara K, Tokuno Y, Nakashima Y, Matsushima N, et al.: Three-dimensional structure of a DNA repair enzyme, 3-methyladenine DNA glycosylase II, from Escherichia coli. Cell 1996, 86:311-319.
    • (1996) Cell , vol.86 , pp. 311-319
    • Yamagata, Y.1    Kato, M.2    Odawara, K.3    Tokuno, Y.4    Nakashima, Y.5    Matsushima, N.6
  • 12
    • 0032538337 scopus 로고    scopus 로고
    • Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: Mechanisms for nucleotide flipping and base excision
    • Lau AY, Schärer OD, Samson L, Verdine GL, Ellenberger T: Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision. Cell 1998, 95:249-258.
    • (1998) Cell , vol.95 , pp. 249-258
    • Lau, A.Y.1    Schärer, O.D.2    Samson, L.3    Verdine, G.L.4    Ellenberger, T.5
  • 13
    • 0002692765 scopus 로고    scopus 로고
    • Repair of alkylation damage to DNA
    • Edited by Hickson ID. Landes Bioscience
    • Seeberg E, Berdal KG: Repair of alkylation damage to DNA. In Base Excision Repair of DNA Damage. Edited by Hickson ID. Landes Bioscience; 1997:151-168.
    • (1997) Base Excision Repair of DNA Damage , pp. 151-168
    • Seeberg, E.1    Berdal, K.G.2
  • 14
    • 0026505044 scopus 로고
    • The suicidal DNA repair methyltransferases of microbes
    • Samson L: The suicidal DNA repair methyltransferases of microbes. Mol Microbiol 1992, 6:825-831.
    • (1992) Mol Microbiol , vol.6 , pp. 825-831
    • Samson, L.1
  • 15
    • 0031763884 scopus 로고    scopus 로고
    • MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily
    • Guan Y, Manuel RC, Arvai AS, Parikh SS, Mol CD, Miller JH, et al.: MutY catalytic core, mutant and bound adenine structures define specificity for DNA repair enzyme superfamily. Nat Struct Biol 1998, 5:1058-1064.
    • (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    Miller, J.H.6
  • 16
    • 0032555571 scopus 로고    scopus 로고
    • Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease III. Direct identification of Lys-212 as the active nucleophilic residue
    • Ikeda S, Biswas T, Roy R, Izumi T, Boldogh I, Kurosky A, et al.: Purification and characterization of human NTH1, a homolog of Escherichia coli endonuclease III. Direct identification of Lys-212 as the active nucleophilic residue. J Biol Chem 1998, 273:21585-21593.
    • (1998) J Biol Chem , vol.273 , pp. 21585-21593
    • Ikeda, S.1    Biswas, T.2    Roy, R.3    Izumi, T.4    Boldogh, I.5    Kurosky, A.6
  • 17
    • 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
    • Breimer LH, Lindahl T: 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 1984, 259:5543-5548.
    • (1984) J Biol Chem , vol.259 , pp. 5543-5548
    • Breimer, L.H.1    Lindahl, T.2
  • 18
    • 0025301064 scopus 로고
    • MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III
    • Michaels ML, Pham L, Nghiem Y, Cruz C, Miller JH: MutY, an adenine glycosylase active on G-A mispairs, has homology to endonuclease III. Nucl Acids Res 1990, 18:3841-3845.
    • (1990) Nucl Acids Res , vol.18 , pp. 3841-3845
    • Michaels, M.L.1    Pham, L.2    Nghiem, Y.3    Cruz, C.4    Miller, J.H.5
  • 19
    • 0026701365 scopus 로고
    • The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine)
    • Michaels ML, Miller JH: The GO system protects organisms from the mutagenic effect of the spontaneous lesion 8-hydroxyguanine (7,8-dihydro-8-oxoguanine). J Bacteriol 1992, 174:6321-6325.
    • (1992) J Bacteriol , vol.174 , pp. 6321-6325
    • Michaels, M.L.1    Miller, J.H.2
  • 20
    • 0029834498 scopus 로고    scopus 로고
    • Counteracting the mutagenic effect of hydrolytic deamination of DNA 5-methylcytosine residues at high temperature: DNA mismatch N-glycosylase Mig.Mth of the thermophilic archaeon Methanobacterium thermoautotrophicum THF
    • Horst JP, Fritz HJ: Counteracting the mutagenic effect of hydrolytic deamination of DNA 5-methylcytosine residues at high temperature: DNA mismatch N-glycosylase Mig.Mth) of the thermophilic archaeon Methanobacterium thermoautotrophicum THF. EMBO J 1996, 15:5459-5469.
    • (1996) EMBO J , vol.15 , pp. 5459-5469
    • Horst, J.P.1    Fritz, H.J.2
  • 21
    • 0032953961 scopus 로고    scopus 로고
    • Methanobacterium thermoformicicum thymine DNA mismatch glycosylase: Conversion of an N-glycosylase to an AP lyase
    • Begley TJ, Cunningham RP: Methanobacterium thermoformicicum thymine DNA mismatch glycosylase: conversion of an N-glycosylase to an AP lyase. Protein Eng 1999, 12:333-340.
    • (1999) Protein Eng , vol.12 , pp. 333-340
    • Begley, T.J.1    Cunningham, R.P.2
  • 22
    • 0028800939 scopus 로고
    • Purification and cloning of Micrococcus luteus ultraviolet endonuclease, an N-glycosylase/ abasic lyase that proceeds via an imino enzyme-DNA intermediate
    • Piersen CE, Prince MA, Augustine ML, Dodson ML, Lloyd RS: Purification and cloning of Micrococcus luteus ultraviolet endonuclease, an N-glycosylase/ abasic lyase that proceeds via an imino enzyme-DNA intermediate. J Biol Chem 1995, 270:23475-23484.
    • (1995) J Biol Chem , vol.270 , pp. 23475-23484
    • Piersen, C.E.1    Prince, M.A.2    Augustine, M.L.3    Dodson, M.L.4    Lloyd, R.S.5
  • 23
    • 0029682322 scopus 로고    scopus 로고
    • Site-directed mutagenesis in vitro by megaprimer PCR
    • Barik S: Site-directed mutagenesis in vitro by megaprimer PCR. Methods Mol Biol 1996, 57:203-215.
    • (1996) Methods Mol Biol , vol.57 , pp. 203-215
    • Barik, S.1
  • 24
    • 0024110510 scopus 로고
    • Nucleotide sequence of the nfo gene of Escherichia coli K-12
    • Saporito SM, Cunningham RP: Nucleotide sequence of the nfo gene of Escherichia coli K-12. J Bacteriol 1988, 170:5141-5145.
    • (1988) J Bacteriol , vol.170 , pp. 5141-5145
    • Saporito, S.M.1    Cunningham, R.P.2
  • 26
    • 0017828018 scopus 로고
    • Properties of 3-methyladenine-DNA glycosylase from Escherichia coli
    • Riazuddin S, Lindahl T: Properties of 3-methyladenine-DNA glycosylase from Escherichia coli. Biochemistry 1978, 17:2110-2118.
    • (1978) Biochemistry , vol.17 , pp. 2110-2118
    • Riazuddin, S.1    Lindahl, T.2
  • 28
    • 0031744963 scopus 로고    scopus 로고
    • Repair in Escherichia coli alkB mutants of abasic sites and 3-methyladenine residues in DNA
    • Dinglay S, Gold B, Sedgwick B: Repair in Escherichia coli alkB mutants of abasic sites and 3-methyladenine residues in DNA. Mutat Res 1998, 407:109-116.
    • (1998) Mutat Res , vol.407 , pp. 109-116
    • Dinglay, S.1    Gold, B.2    Sedgwick, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.