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Volumn 73, Issue 2, 2001, Pages 128-134

Alternative forms of formamidopyrimidine-DNA glycosylase from Arabidopsis thaliana

Author keywords

[No Author keywords available]

Indexed keywords

8 HYDROXYGUANINE; BACTERIAL ENZYME; COMPLEMENTARY DNA; DNA GLYCOSYLTRANSFERASE; DOUBLE STRANDED DNA; FORMAMIDOPYRIMIDINE DEOXYRIBONUCLEIC ACID GLYCOSYLASE; HISTIDINE DERIVATIVE; LYASE; METHYLENE BLUE; UNCLASSIFIED DRUG; VEGETABLE PROTEIN;

EID: 0035263211     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/0031-8655(2001)073<0128:AFOFDG>2.0.CO;2     Document Type: Article
Times cited : (23)

References (30)
  • 1
    • 0343593145 scopus 로고    scopus 로고
    • Radiation-induced oxidative DNA base damage and its repair in nuclear matrix-associated DNA and in bulk DNA in hepatic chromatin of rat upon whole-body gamma-irradiation
    • Zastawny, T. H., B. Czerwinska, B. Drzewiecka and R. Olinski (1997) Radiation-induced oxidative DNA base damage and its repair in nuclear matrix-associated DNA and in bulk DNA in hepatic chromatin of rat upon whole-body gamma-irradiation. Free Radic. Biol. Med. 22, 101-107.
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 101-107
    • Zastawny, T.H.1    Czerwinska, B.2    Drzewiecka, B.3    Olinski, R.4
  • 2
    • 0030797051 scopus 로고    scopus 로고
    • Formation, prevention, and repair of DNA damage by iron/hydrogen peroxide
    • Henle, E. S. and S. Linn (1997) Formation, prevention, and repair of DNA damage by iron/hydrogen peroxide. J. Biol. Chem. 272, 19 095-19 098.
    • (1997) J. Biol. Chem. , vol.272 , pp. 19095-19098
    • Henle, E.S.1    Linn, S.2
  • 3
    • 0028957735 scopus 로고
    • Monomeric base damage products from adenine, guanine, and thymine induced by exposure of DNA to ultraviolet radiation
    • Doetsch, P. W., T. H. Zastawny, A. M. Martin and M. Dizdaroglu (1995) Monomeric base damage products from adenine, guanine, and thymine induced by exposure of DNA to ultraviolet radiation. Biochemistry 34, 737-742.
    • (1995) Biochemistry , vol.34 , pp. 737-742
    • Doetsch, P.W.1    Zastawny, T.H.2    Martin, A.M.3    Dizdaroglu, M.4
  • 5
    • 0002696602 scopus 로고
    • Oxygen stress and superoxide dismutases
    • Scandalios, J. G. (1993) Oxygen stress and superoxide dismutases. Plant Physiol. 101, 7-12.
    • (1993) Plant Physiol. , vol.101 , pp. 7-12
    • Scandalios, J.G.1
  • 6
    • 84994930460 scopus 로고
    • Protection against oxygen radicals: An important defence mechanism studied in transgenic plants
    • Foyer, C. H., P. Descourvieres and K. J. Kunert (1994) Protection against oxygen radicals: an important defence mechanism studied in transgenic plants. Plant Cell Environ. 17, 507-523.
    • (1994) Plant Cell Environ. , vol.17 , pp. 507-523
    • Foyer, C.H.1    Descourvieres, P.2    Kunert, K.J.3
  • 7
    • 0030484105 scopus 로고    scopus 로고
    • The role of activated oxygen species in plant disease resistance
    • Mehdy, M. C., Y. K. Sharma, K. Sathasivan and N. W. Bays (1996) The role of activated oxygen species in plant disease resistance. Physiol. Plant. 98, 365-374.
    • (1996) Physiol. Plant. , vol.98 , pp. 365-374
    • Mehdy, M.C.1    Sharma, Y.K.2    Sathasivan, K.3    Bays, N.W.4
  • 8
    • 0025871264 scopus 로고
    • MUTM, a protein that prevents G:C→T:A transversions, is formamidopyrimidine-DNA glycosylase
    • Michaels, M. L., L. Phan, C. Cruz and J. H. Miller (1991) MUTM, a protein that prevents G:C→T:A transversions, is formamidopyrimidine-DNA glycosylase. Nucleic Acids Res. 19, 3629-3632.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3629-3632
    • Michaels, M.L.1    Phan, L.2    Cruz, C.3    Miller, J.H.4
  • 9
    • 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., E. Gajewski, J. Laval and M. Dizdaroglu (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
  • 10
    • 0030818650 scopus 로고    scopus 로고
    • Kinetics of excision of purine lesions from DNA by Escherichia coli Fpg protein
    • Karakaya, A., P. Jaruga, V. A. Bohr, A. P. Grollman and M. Dizdaroglu (1997) Kinetics of excision of purine lesions from DNA by Escherichia coli Fpg protein. Nucleic Acids Res. 25, 474-479.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 474-479
    • Karakaya, A.1    Jaruga, P.2    Bohr, V.A.3    Grollman, A.P.4    Dizdaroglu, M.5
  • 11
    • 0024462459 scopus 로고
    • Mechanism of DNA strand nicking at apurinic/apyrimidinic sites by Escherichia coli [formamidopyrimidine] DNA glycosylase
    • Bailly, V., W. G. Verly, T. J. O'Connor and J. Laval (1989) Mechanism of DNA strand nicking at apurinic/apyrimidinic sites by Escherichia coli [formamidopyrimidine] DNA glycosylase. Biochem. J. 262, 581-589.
    • (1989) Biochem. J. , vol.262 , pp. 581-589
    • Bailly, V.1    Verly, W.G.2    O'Connor, T.J.3    Laval, J.4
  • 13
    • 0001330572 scopus 로고    scopus 로고
    • Two cDNAs encoding Arabidopsis thaliana homologs of bacterial formamidopyrimidine-DNA glycosylase genes are produced by alternative processing (accession nos. AF099970 and AF099971)
    • Murphy, T. M. and M.-J. Gao (1998) Two cDNAs encoding Arabidopsis thaliana homologs of bacterial formamidopyrimidine-DNA glycosylase genes are produced by alternative processing (accession nos. AF099970 and AF099971), Plant Physiol. 118, 1535.
    • (1998) Plant Physiol. , vol.118 , pp. 1535
    • Murphy, T.M.1    Gao, M.-J.2
  • 14
    • 0032945268 scopus 로고    scopus 로고
    • Expression and differential intracellular localization of two major forms of human 8-oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs
    • Nishioka, K., T. Ohtsubo, H. Oda, T. Fujiwara, D. Kang, K. Sugimachi and Y. Nakabeppu (1999) Expression and differential intracellular localization of two major forms of human 8-oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs. Mol. Biol. Cell 10, 1637-1652.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 1637-1652
    • Nishioka, K.1    Ohtsubo, T.2    Oda, H.3    Fujiwara, T.4    Kang, D.5    Sugimachi, K.6    Nakabeppu, Y.7
  • 15
    • 0030841051 scopus 로고    scopus 로고
    • Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene
    • Nilsen, H., M. Otterlei, T. Haug, K. Solum, T. Nagelhus, F. Skorpen and H. E. Krokan (1997) Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene. Nucleic Acids Res. 25, 750-755.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 750-755
    • Nilsen, H.1    Otterlei, M.2    Haug, T.3    Solum, K.4    Nagelhus, T.5    Skorpen, F.6    Krokan, H.E.7
  • 17
    • 0034654256 scopus 로고    scopus 로고
    • Identification of human MutY homolog (hMYH) as a repair enzyme for 2-hydroxyadenine in DNA and detection of multi-forms of hMYH located in nuclei and mitochondria
    • Ohtsubo, T., K. Nishioka, Y. Imaiso, S. Iwai, T. Shimokawa, H. Oda, T. Fujiwara and Y. Nakabeppu (2000) Identification of human MutY homolog (hMYH) as a repair enzyme for 2-hydroxyadenine in DNA and detection of multi-forms of hMYH located in nuclei and mitochondria. Nucleic Acids Res. 28, 1355-1364.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1355-1364
    • Ohtsubo, T.1    Nishioka, K.2    Imaiso, Y.3    Iwai, S.4    Shimokawa, T.5    Oda, H.6    Fujiwara, T.7    Nakabeppu, Y.8
  • 18
    • 0025949412 scopus 로고
    • Nuclear targeting sequences - A consensus
    • Dingwall, C. and R. A. Laskey (1991) Nuclear targeting sequences - a consensus. Trends Biochem. Sci. 16, 478-481.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 478-481
    • Dingwall, C.1    Laskey, R.A.2
  • 19
    • 0031796813 scopus 로고    scopus 로고
    • Molecular cloning of AtMMH, an Arabidopsis thaliana ortholog of the Escherichia coli mutM gene, and analysis of functional domains of its product
    • Ohtsubo, T., O. Matsuda, K. Iba, I. Terashima, M. Sekiguchi and Y. Nakabeppu (1998) Molecular cloning of AtMMH, an Arabidopsis thaliana ortholog of the Escherichia coli mutM gene, and analysis of functional domains of its product. Mol. Gen. Genet. 259, 577-590.
    • (1998) Mol. Gen. Genet. , vol.259 , pp. 577-590
    • Ohtsubo, T.1    Matsuda, O.2    Iba, K.3    Terashima, I.4    Sekiguchi, M.5    Nakabeppu, Y.6
  • 22
    • 0022375581 scopus 로고
    • Expression of a cloned denV gene of bacteriophage T4 in Escherichia coli
    • Valerie, K., E. E. Henderson and J. K. DeRiel (1985) Expression of a cloned denV gene of bacteriophage T4 in Escherichia coli. Proc. Natl. Acad. Sci. USA 82, 4763-4767.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 4763-4767
    • Valerie, K.1    Henderson, E.E.2    DeRiel, J.K.3
  • 23
    • 0013079126 scopus 로고    scopus 로고
    • Ph.D. dissertation, University of California, Davis, CA
    • Martin, C. P. (1997) Ph.D. dissertation, University of California, Davis, CA.
    • (1997)
    • Martin, C.P.1
  • 25
    • 84989701118 scopus 로고
    • Endonuclease activity from tobacco nuclei specific for ultraviolet radiation-damaged DNA
    • Murphy, T. M., C. P. Martin and J. Kami (1993) Endonuclease activity from tobacco nuclei specific for ultraviolet radiation-damaged DNA. Physiol. Plant. 87, 417-425.
    • (1993) Physiol. Plant. , vol.87 , pp. 417-425
    • Murphy, T.M.1    Martin, C.P.2    Kami, J.3
  • 26
    • 0027328401 scopus 로고
    • Cleavage and binding of a DNA fragment containing a single 8-oxoguanine by wild type and mutant FPG proteins
    • Castaing, B., A. Geiger, H. Seliger, P. Nehls, J. Laval, C. Zelwer and S. Boiteux (1993) Cleavage and binding of a DNA fragment containing a single 8-oxoguanine by wild type and mutant FPG proteins. Nucleic Acids Res. 21, 2899-2905.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 2899-2905
    • Castaing, B.1    Geiger, A.2    Seliger, H.3    Nehls, P.4    Laval, J.5    Zelwer, C.6    Boiteux, S.7
  • 27
    • 0027462131 scopus 로고
    • FPG protein of Eschericaia coli is a zinc finger protein whose cysteine residues have a structural and/or function role
    • O'Connor, T. R., R. J. Graves, G. DeMurcia, B. Castaing and J. Laval (1993) FPG protein of Eschericaia coli is a zinc finger protein whose cysteine residues have a structural and/or function role. J. Biol. Chem. 268, 9063-9070.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9063-9070
    • O'Connor, T.R.1    Graves, R.J.2    DeMurcia, G.3    Castaing, B.4    Laval, J.5
  • 28
    • 0032611834 scopus 로고    scopus 로고
    • The initiation of DNA base excision repair of dipyrimidine photoproducts
    • Lloyd, R. S. (1999) The initiation of DNA base excision repair of dipyrimidine photoproducts. Prog. Nuc. Acid Res. Mol. Biol. 62, 155-175.
    • (1999) Prog. Nuc. Acid Res. Mol. Biol. , vol.62 , pp. 155-175
    • Lloyd, R.S.1
  • 29
    • 0030614471 scopus 로고    scopus 로고
    • 2-terminal proline acts as a nucleophile in the glycosylase/AP-lyase reaction catalyzed by Escherichia coli formamidoyrimidine-DNA glycosylase (Fpg) protein
    • 2-terminal proline acts as a nucleophile in the glycosylase/AP-lyase reaction catalyzed by Escherichia coli formamidoyrimidine-DNA glycosylase (Fpg) protein. J. Biol. Chem. 272, 5335-5341.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5335-5341
    • Zharkov, D.O.1    Rieger, R.A.2    Iden, C.R.3    Grollman, A.P.4
  • 30
    • 0030991774 scopus 로고    scopus 로고
    • Mechanism of action of base release by Escherichia coli Fpg protein: Role of lysine 155 in catalysis
    • Rabow, L. E. and Y. W. Kow (1997) Mechanism of action of base release by Escherichia coli Fpg protein: role of lysine 155 in catalysis. Biochemistry 36, 5084-5096.
    • (1997) Biochemistry , vol.36 , pp. 5084-5096
    • Rabow, L.E.1    Kow, Y.W.2


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