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Volumn 38, Issue 3, 1997, Pages 165-171

Mutational Specificity of the Ferrous Ion in a supF Gene of Endonuclease III/VIII Deficient Escherichia coli

Author keywords

5 hydroxycytosine; Endonuclease III; Endonuclease VIII; Ferrous ion; Oxygen radicals; supF gene

Indexed keywords

ESCHERICHIA COLI; GENES; OXYGEN;

EID: 0031217940     PISSN: 04493060     EISSN: None     Source Type: Journal    
DOI: 10.1269/jrr.38.165     Document Type: Article
Times cited : (9)

References (30)
  • 1
    • 0031091260 scopus 로고    scopus 로고
    • Enzymatic repair mechanisms for base modifications induced by oxygen radicals
    • Yamamoto, K., Uraki, F., Yonei, S. and Yukawa, O. (1997) Enzymatic repair mechanisms for base modifications induced by oxygen radicals. J. Radiat. Res. 38: 1-4.
    • (1997) J. Radiat. Res. , vol.38 , pp. 1-4
    • Yamamoto, K.1    Uraki, F.2    Yonei, S.3    Yukawa, O.4
  • 2
    • 0030228822 scopus 로고    scopus 로고
    • Damage induced by hydroxy radicals generated in the hydration layer of γ-irradiated frozen aqueous solution of DNA
    • Ohshima, H., Iida, Y., Matsuda, A. and Kuwabara, M. (1996) Damage induced by hydroxy radicals generated in the hydration layer of γ-irradiated frozen aqueous solution of DNA. J. Radiat. Res. 37: 199-207.
    • (1996) J. Radiat. Res. , vol.37 , pp. 199-207
    • Ohshima, H.1    Iida, Y.2    Matsuda, A.3    Kuwabara, M.4
  • 3
    • 0027171266 scopus 로고
    • Oxidants, antioxidants, and the degenerative diseases of aging
    • Ames, B. N., Shigenaga, M. K. and Hagen, T. M. (1993) Oxidants, antioxidants, and the degenerative diseases of aging. Proc. Natl. Acad. Sci. USA 90: 7915-7922.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7915-7922
    • Ames, B.N.1    Shigenaga, M.K.2    Hagen, T.M.3
  • 5
    • 0026591033 scopus 로고
    • Endogenous oxidative damage of deoxycytidine in DNA
    • Wagner, J. R., Hu, C. C. and Ames, B. N. (1992) Endogenous oxidative damage of deoxycytidine in DNA. Proc. Natl. Acad. Sci. USA 89: 3380-3384.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3380-3384
    • Wagner, J.R.1    Hu, C.C.2    Ames, B.N.3
  • 6
    • 0028341311 scopus 로고
    • Major oxidative products of cytosine, 5-hydroxycytosine and 5-hydroxyuracil, exhibit sequence context-dependent mispairing in vitro
    • Purmal, A. A., Kow, Y. W. and Wallace, S. S. (1994) Major oxidative products of cytosine, 5-hydroxycytosine and 5-hydroxyuracil, exhibit sequence context-dependent mispairing in vitro. Nucleic Acids Res. 22: 72-78.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 72-78
    • Purmal, A.A.1    Kow, Y.W.2    Wallace, S.S.3
  • 7
    • 0024110769 scopus 로고
    • mutM, a second mutator locus in Escherichia coli that generates G.C→T.a transversions
    • Cabrera, M., Nghiem, Y. and Miller, J.H. (1988) mutM, a second mutator locus in Escherichia coli that generates G.C→T.A transversions. J. Bacteriol. 170: 5405-5407.
    • (1988) J. Bacteriol. , vol.170 , pp. 5405-5407
    • Cabrera, M.1    Nghiem, Y.2    Miller, J.H.3
  • 8
    • 0024570448 scopus 로고
    • Isolation of a formamidopyrimidine-DNA glycosylase (fpg) mutant of Escherichia coli K12
    • Boiteux, S. and Huisman, O. (1989) Isolation of a formamidopyrimidine-DNA glycosylase (fpg) mutant of Escherichia coli K12. Mol. Gen. Genet. 215: 300-305.
    • (1989) Mol. Gen. Genet. , vol.215 , pp. 300-305
    • Boiteux, S.1    Huisman, O.2
  • 9
    • 0343879974 scopus 로고
    • Endonuclease III (nth) mutants of Escherichia coli
    • Cunningham, R. P. and Weiss, B. (1985) Endonuclease III (nth) mutants of Escherichia coli. Proc. Natl. Acad. Sci. USA 82: 474-478.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 474-478
    • Cunningham, R.P.1    Weiss, B.2
  • 10
    • 0030958623 scopus 로고    scopus 로고
    • Characterization of Endonuclease III (nth) and Endonuclease VIII (nei) mutants of Escherichia coli K12
    • Saito, Y., Uraki, F., Nakajima, S., Asaeda, A., Ono, K., Kubo, K. and Yamamoto, K. (1997) Characterization of Endonuclease III (nth) and Endonuclease VIII (nei) mutants of Escherichia coli K12. J. Bacteriol. 179: 3783-3785.
    • (1997) J. Bacteriol. , vol.179 , pp. 3783-3785
    • Saito, Y.1    Uraki, F.2    Nakajima, S.3    Asaeda, A.4    Ono, K.5    Kubo, K.6    Yamamoto, K.7
  • 11
    • 0026533905 scopus 로고
    • Substrate specificity of the Escherichia coli Fpg protein (formamidopyrimidine-DNA glycosylase): Excision of purine lesions in DNA produced by ionizing radiation or photosensitization
    • Boiteux, S., Gajewski, E., Laval, J. and Dizdaroglu, M. (1992) Substrate specificity of the Escherichia coli Fpg protein (formamidopyrimidine-DNA glycosylase): excision of purine lesions in DNA produced by ionizing radiation or photosensitization. Biochemistry 31: 106-110.
    • (1992) Biochemistry , vol.31 , pp. 106-110
    • Boiteux, S.1    Gajewski, E.2    Laval, J.3    Dizdaroglu, M.4
  • 12
    • 0028295382 scopus 로고
    • Isolation and characterization of endonuclease VIII from Escherichia coli
    • Melamede, R. J., Hatahet, Z., Kow, Y.W., Ide, H. and Wallace, S.S. (1994) Isolation and characterization of endonuclease VIII from Escherichia coli. Biochemistry 33: 1255-1264.
    • (1994) Biochemistry , vol.33 , pp. 1255-1264
    • Melamede, R.J.1    Hatahet, Z.2    Kow, Y.W.3    Ide, H.4    Wallace, S.S.5
  • 13
    • 0024393445 scopus 로고
    • Purification and characterization of Escherichia coli endonuclease III from the cloned nth gene
    • Asahara, H., Wistort, P. M., Bank, J. F., Bakerian, R. H. and Cunningham, R. P. (1989) Purification and characterization of Escherichia coli endonuclease III from the cloned nth gene. Biochemistry 28: 4444-4449.
    • (1989) Biochemistry , vol.28 , pp. 4444-4449
    • Asahara, H.1    Wistort, P.M.2    Bank, J.F.3    Bakerian, R.H.4    Cunningham, R.P.5
  • 14
    • 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 N-glycosylase, while 5-hydroxy-2′-deoxyuridine is a substrate for uracil DNA N-glycosylase
    • Hatahet, Z., Kow, Y. W., Purmal, A. A., Cunningham, R. P. and Wallace, S. S. (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 N-glycosylase, while 5-hydroxy-2′-deoxyuridine is a substrate for uracil DNA N-glycosylase. J. Biol. Chem. 269: 18814-18820.
    • (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
  • 15
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • Shibutani, S., Takeshita, M. and Grollman, A.P. (1991) Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature 349: 431-434.
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 16
    • 0026440035 scopus 로고
    • Deficiency of 8-hydroxyguanine DNA endonuclease activity and accumulation of the 8-hydroxyguanine in mutator mutant (mutM) of Escherichia coli
    • Bessho, T., Tano, K., Kasai, H. and Nishimura, S. (1992) Deficiency of 8-hydroxyguanine DNA endonuclease activity and accumulation of the 8-hydroxyguanine in mutator mutant (mutM) of Escherichia coli. Biochem. Biophys. Res. Commun. 188: 372-378.
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 372-378
    • Bessho, T.1    Tano, K.2    Kasai, H.3    Nishimura, S.4
  • 17
    • 0028361161 scopus 로고
    • Hydrogen peroxide induces G:C to T:A and G:C to C:G transversions in the supF gene of Escherichia coli
    • Akasaka, S. and Yamamoto, K. (1994) Hydrogen peroxide induces G:C to T:A and G:C to C:G transversions in the supF gene of Escherichia coli. Mol. Gen. Genet. 243: 500-505.
    • (1994) Mol. Gen. Genet. , vol.243 , pp. 500-505
    • Akasaka, S.1    Yamamoto, K.2
  • 18
    • 0028074914 scopus 로고
    • Mutagenesis resulting from DNA damage by lipid peroxidation in the supF gene of Escherichia coli
    • Akasaka, S. and Yamamoto, K. (1994) Mutagenesis resulting from DNA damage by lipid peroxidation in the supF gene of Escherichia coli. Mutat. Res. 315: 105-112.
    • (1994) Mutat. Res. , vol.315 , pp. 105-112
    • Akasaka, S.1    Yamamoto, K.2
  • 19
    • 0029046461 scopus 로고
    • Mutational specificity of the ferrous ion in a supF gene of Escherichia coli
    • Akasaka, S. and Yamamoto, K. (1995) Mutational specificity of the ferrous ion in a supF gene of Escherichia coli. Biochem. Biophys. Res. Commun. 213: 74-80.
    • (1995) Biochem. Biophys. Res. Commun. , vol.213 , pp. 74-80
    • Akasaka, S.1    Yamamoto, K.2
  • 20
    • 0026011652 scopus 로고
    • Mutagenic spectrum resulting from DNA damage by oxygen radicals
    • McBride, T. J., Preston B. D. and Loeb, L., A. (1991) Mutagenic spectrum resulting from DNA damage by oxygen radicals. Biochemistry 30: 207-213.
    • (1991) Biochemistry , vol.30 , pp. 207-213
    • McBride, T.J.1    Preston, B.D.2    Loeb, L.A.3
  • 21
    • 0026753852 scopus 로고
    • Mutations induced by methylene blue plus light in single-stranded M13mp2
    • McBride, T. J., Schneider, J. E., Floyd, R. A. and Loeb, L. A. (1992) Mutations induced by methylene blue plus light in single-stranded M13mp2. Proc. Natl. Acad. Sci. USA 89: 6866-6870.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6866-6870
    • McBride, T.J.1    Schneider, J.E.2    Floyd, R.A.3    Loeb, L.A.4
  • 23
    • 0030995625 scopus 로고    scopus 로고
    • An Escherichia coli topB mutant increases deletion and frameshift mutations in the supF target gene
    • Uematsu, N., Eda, S. and Yamamoto, K (1997) An Escherichia coli topB mutant increases deletion and frameshift mutations in the supF target gene. Mutat. Res., 383: 223-230.
    • (1997) Mutat. Res. , vol.383 , pp. 223-230
    • Uematsu, N.1    Eda, S.2    Yamamoto, K.3
  • 24
    • 0026615884 scopus 로고
    • G:C→T.A and G:C→C:G transversions are the predominant spontaneous mutations in the Escherichia coli supF gene: An improved lacZ(am) E. coli host designed for assaying pZ189 supF mutational specificity
    • Akasaka, S., Takimoto, K. and Yamamoto, K. (1992) G:C→T.A and G:C→C:G transversions are the predominant spontaneous mutations in the Escherichia coli supF gene: an improved lacZ(am) E. coli host designed for assaying pZ189 supF mutational specificity. Mol. Gen. Genet. 235: 173-178.
    • (1992) Mol. Gen. Genet. , vol.235 , pp. 173-178
    • Akasaka, S.1    Takimoto, K.2    Yamamoto, K.3
  • 25
    • 0026574764 scopus 로고
    • An Escherichia coli plasmid-based, mutational system in which supF mutants are selectable: Insertion elements dominate the spontaneous spectra
    • Rodriguez, H., Snow, E.T., Bhat, U. and Loechler, E.L. (1992) An Escherichia coli plasmid-based, mutational system in which supF mutants are selectable: insertion elements dominate the spontaneous spectra. Mutat. Res. 270:219-231.
    • (1992) Mutat. Res. , vol.270 , pp. 219-231
    • Rodriguez, H.1    Snow, E.T.2    Bhat, U.3    Loechler, E.L.4
  • 26
    • 0026024037 scopus 로고
    • Construction of Escherichia coli K12 phr deletion and insertion mutants by gene replacement
    • Akasaka, S., and Yamamoto, K. (1991) Construction of Escherichia coli K12 phr deletion and insertion mutants by gene replacement. Mutat. Res. 254: 27-35.
    • (1991) Mutat. Res. , vol.254 , pp. 27-35
    • Akasaka, S.1    Yamamoto, K.2
  • 28
    • 0018448030 scopus 로고
    • A procedure for the quantitation of relaxed closed circular DNA in the presence of superhelical DNA: An improved fluorometric assay for nicking-closing enzyme
    • Kowalski, D. (1979) A procedure for the quantitation of relaxed closed circular DNA in the presence of superhelical DNA: an improved fluorometric assay for nicking-closing enzyme. Anal. Biochem. 93: 346-354.
    • (1979) Anal. Biochem. , vol.93 , pp. 346-354
    • Kowalski, D.1
  • 29
    • 0031090454 scopus 로고    scopus 로고
    • Spectrum of spontaneous mutations in the cyclic AMP receptor protein gene on chromosomal DNA of Escherichia coli
    • Takimoto, K., Tachibana, A., Ayaki, H. and Yamamoto, K. (1997) Spectrum of spontaneous mutations in the cyclic AMP receptor protein gene on chromosomal DNA of Escherichia coli. J. Radiat. Res. 38: 27-36.
    • (1997) J. Radiat. Res. , vol.38 , pp. 27-36
    • Takimoto, K.1    Tachibana, A.2    Ayaki, H.3    Yamamoto, K.4
  • 30
    • 0031158849 scopus 로고    scopus 로고
    • Comparison of oxidation products from DNA components by γ-irradiation and Fenton-type reactions
    • Murata-Kamiya, N., Kamiya, H., Muraoka, M., Kaji, H. and Kasai, H. (1997) Comparison of oxidation products from DNA components by γ-irradiation and Fenton-type reactions. J. Radiat. Res. 38: 121-131.
    • (1997) J. Radiat. Res. , vol.38 , pp. 121-131
    • Murata-Kamiya, N.1    Kamiya, H.2    Muraoka, M.3    Kaji, H.4    Kasai, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.