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Volumn 82, Issue 4, 2006, Pages 241-250

Cloning and characterization of an ascidian homolog of the human 8-oxoguanine DNA glycosylase (Ogg1) that is involved in the repair of 8-oxo-7,8-dihydroguanine in DNA in Ciona intestinalis

Author keywords

8 oxo 7,8 dihydroguanine; Base excision repair; Ciona intestinalis; Ogg1; Oxidatively damaged DNA

Indexed keywords

8 OXO 7,8 DIHYDROGUANINE DNA GLYCOSYLASE; COMPLEMENTARY DNA; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA GLYCOSYLTRANSFERASE; PROTEIN OGG1; UNCLASSIFIED DRUG;

EID: 33646759895     PISSN: 09553002     EISSN: 13623095     Source Type: Journal    
DOI: 10.1080/09553000600649216     Document Type: Article
Times cited : (6)

References (54)
  • 2
    • 0033105094 scopus 로고    scopus 로고
    • Conserved domains in DNA repair proteins and evolution of repair systems
    • Aravind L, Walker DR, Koonin EV. 1999. Conserved domains in DNA repair proteins and evolution of repair systems. Nucleic Acids Research 27:1223-1242.
    • (1999) Nucleic Acids Research , vol.27 , pp. 1223-1242
    • Aravind, L.1    Walker, D.R.2    Koonin, E.V.3
  • 3
    • 10944251591 scopus 로고    scopus 로고
    • Repair and genetic consequences of endogenous DNA base damage in mammalian cells
    • Barnes DE, Lindahl T. 2004. Repair and genetic consequences of endogenous DNA base damage in mammalian cells. Annual Review of Genetics 38:445-476.
    • (2004) Annual Review of Genetics , vol.38 , pp. 445-476
    • Barnes, D.E.1    Lindahl, T.2
  • 4
    • 0344586043 scopus 로고    scopus 로고
    • Mutagenicity, toxicity, and repair of DNA base damage induced by oxidation
    • Bjelland S, Seeberg E. 2003. Mutagenicity, toxicity, and repair of DNA base damage induced by oxidation. Mutation Research 531:37-80.
    • (2003) Mutation Research , vol.531 , pp. 37-80
    • Bjelland, S.1    Seeberg, E.2
  • 5
    • 0036290411 scopus 로고    scopus 로고
    • Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase
    • Bjørås M, Seeberg E, Luna L, Pearl LH, Barrett TE. 2002. Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase. Journal of Molecular Biology 317:171-177.
    • (2002) Journal of Molecular Biology , vol.317 , pp. 171-177
    • Bjørås, M.1    Seeberg, E.2    Luna, L.3    Pearl, L.H.4    Barrett, T.E.5
  • 6
    • 0037096191 scopus 로고    scopus 로고
    • Repair of 8-oxoguanine in Saccharomyces cerevisiae: Interplay of DNA repair and replication mechanisms
    • Boiteux S, Gellon L, Guibourt N. 2002. Repair of 8-oxoguanine in Saccharomyces cerevisiae: Interplay of DNA repair and replication mechanisms. Free Radical Biology and Medicine 32:1244-1253.
    • (2002) Free Radical Biology and Medicine , vol.32 , pp. 1244-1253
    • Boiteux, S.1    Gellon, L.2    Guibourt, N.3
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72:248-254.
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 0032568337 scopus 로고    scopus 로고
    • Repair of oxidatively damaged guanine in Saccharomyces cerevisiae by an alternative pathway
    • Bruner SD, Nash HM, Lane WS, Verdine GL. 1998. Repair of oxidatively damaged guanine in Saccharomyces cerevisiae by an alternative pathway. Current Biology 8:393-403.
    • (1998) Current Biology , vol.8 , pp. 393-403
    • Bruner, S.D.1    Nash, H.M.2    Lane, W.S.3    Verdine, G.L.4
  • 9
    • 0034708226 scopus 로고    scopus 로고
    • Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA
    • Bruner SD, Norman DPG, Verdine GL. 2000. Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Nature 403:859-866.
    • (2000) Nature , vol.403 , pp. 859-866
    • Bruner, S.D.1    Norman, D.P.G.2    Verdine, G.L.3
  • 11
    • 0035850219 scopus 로고    scopus 로고
    • Repair activities of 8-oxoguanine DNA glycosylase from Arckaeoblobus fulgidus, a hyperthermophilic archaeon
    • Chung JH, Suh MJ, Park YI, Tainer JA, Han YS. 2001. Repair activities of 8-oxoguanine DNA glycosylase from Arckaeoblobus fulgidus, a hyperthermophilic archaeon. Mutation Research 486:99-111.
    • (2001) Mutation Research , vol.486 , pp. 99-111
    • Chung, J.H.1    Suh, M.J.2    Park, Y.I.3    Tainer, J.A.4    Han, Y.S.5
  • 14
    • 3343022751 scopus 로고    scopus 로고
    • An evolutionary analysis of the helix-hairpin-helix superfamily of DNA repair glycosylases
    • Denver DR, Swenson SL, Lynch M. 2003. An evolutionary analysis of the helix-hairpin-helix superfamily of DNA repair glycosylases. Molecular Biology and Evolution 20:1603-1611.
    • (2003) Molecular Biology and Evolution , vol.20 , pp. 1603-1611
    • Denver, D.R.1    Swenson, S.L.2    Lynch, M.3
  • 15
    • 0033569954 scopus 로고    scopus 로고
    • Excision of oxidatively damaged DNA bases by the human α-hOgg1 protein and the polymorphic α-hOgg1 (Ser 326 Cys) protein which is frequently found in human populations
    • Dherin C, Radicella JP, Dizdaroglu M, Boiteux S. 1999. Excision of oxidatively damaged DNA bases by the human α-hOgg1 protein and the polymorphic α-hOgg1 (Ser 326 Cys) protein which is frequently found in human populations. Nucleic Acids Research 27:4001-4007.
    • (1999) Nucleic Acids Research , vol.27 , pp. 4001-4007
    • Dherin, C.1    Radicella, J.P.2    Dizdaroglu, M.3    Boiteux, S.4
  • 16
    • 0034556627 scopus 로고    scopus 로고
    • Repair of oxidative DNA damage in Drosophila melanogaster. Identification and characterization of dOgg1, a second DNA glycosylase activity for 8-hydroxyguanine and formamidopyrimidines
    • Dherin C, Dizdaroglu M, Doerflinger H, Boiteux S, Radicella JP. 2000. Repair of oxidative DNA damage in Drosophila melanogaster. Identification and characterization of dOgg1, a second DNA glycosylase activity for 8-hydroxyguanine and formamidopyrimidines. Nucleic Acids Research 28:4583-4592.
    • (2000) Nucleic Acids Research , vol.28 , pp. 4583-4592
    • Dherin, C.1    Dizdaroglu, M.2    Doerflinger, H.3    Boiteux, S.4    Radicella, J.P.5
  • 17
    • 0032786233 scopus 로고    scopus 로고
    • A phylogenomic study of DNA repair genes, proteins, and processes
    • Eisen JA, Hanawalt PC. 1999. A phylogenomic study of DNA repair genes, proteins, and processes. Mutation Research 435:171-213.
    • (1999) Mutation Research , vol.435 , pp. 171-213
    • Eisen, J.A.1    Hanawalt, P.C.2
  • 18
    • 0035543852 scopus 로고    scopus 로고
    • An OGG1 orthologue encoding a functional 8-oxoguanine DNA glycosylase/AP lyase in Arabidopsis thaliana
    • Garcia-Ortiz MV, Ariza RR, Roldan-Arjona T. 2001. An OGG1 orthologue encoding a functional 8-oxoguanine DNA glycosylase/AP lyase in Arabidopsis thaliana. Plant Molecular Biology 47:795-804.
    • (2001) Plant Molecular Biology , vol.47 , pp. 795-804
    • Garcia-Ortiz, M.V.1    Ariza, R.R.2    Roldan-Arjona, T.3
  • 19
    • 0027324378 scopus 로고
    • Mutagenesis by 8-oxoguanine: An enemy within
    • Grollman AP, Moriya M. 1993. Mutagenesis by 8-oxoguanine: an enemy within. Trends of Genetics 9:246-249.
    • (1993) Trends of Genetics , vol.9 , pp. 246-249
    • Grollman, A.P.1    Moriya, M.2
  • 20
    • 4544273926 scopus 로고    scopus 로고
    • Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase
    • Hsu GW, Ober M, Carell T, Beese LS. 2004. Error-prone replication of oxidatively damaged DNA by a high-fidelity DNA polymerase. Nature 431:217-221.
    • (2004) Nature , vol.431 , pp. 217-221
    • Hsu, G.W.1    Ober, M.2    Carell, T.3    Beese, L.S.4
  • 22
    • 0031045858 scopus 로고    scopus 로고
    • An alternative splicing event which occurs in mouse pachtene spermatocytes generates a form of DNA ligase III with distinct biochemical properties that may function in meiotic recombination
    • Mackey ZB, Ramos W, Levin DS, Walter CA, McCarry JR, Tomkinson AE. 1997. An alternative splicing event which occurs in mouse pachtene spermatocytes generates a form of DNA ligase III with distinct biochemical properties that may function in meiotic recombination. Molecular and Cellular Biology 17:989-998.
    • (1997) Molecular and Cellular Biology , vol.17 , pp. 989-998
    • Mackey, Z.B.1    Ramos, W.2    Levin, D.S.3    Walter, C.A.4    McCarry, J.R.5    Tomkinson, A.E.6
  • 23
    • 0026513966 scopus 로고
    • MutT protein specifically hydrolyzes a potent mutagenic substrate for DNA synthesis
    • Maki H, Sekiguchi M. 1992. MutT protein specifically hydrolyzes a potent mutagenic substrate for DNA synthesis. Nature 355:273-275.
    • (1992) Nature , vol.355 , pp. 273-275
    • Maki, H.1    Sekiguchi, M.2
  • 24
    • 0034011261 scopus 로고    scopus 로고
    • Oxyradicals and DNA damage
    • Marnett LJ. 2000. Oxyradicals and DNA damage. Carcinogenesis 21:361-370.
    • (2000) Carcinogenesis , vol.21 , pp. 361-370
    • Marnett, L.J.1
  • 25
  • 26
    • 0025301064 scopus 로고
    • MutY, and adenine glycosylase active on G:A mispairs has homology to endonuclease III
    • Michaels ML, Pham L, Nghiem Y, Cruz C, Miller JH. 1990. MutY, and adenine glycosylase active on G:A mispairs has homology to endonuclease III. Nucleic Acids Research 18:3841-3845.
    • (1990) Nucleic Acids Research , vol.18 , pp. 3841-3845
    • Michaels, M.L.1    Pham, L.2    Nghiem, Y.3    Cruz, C.4    Miller, J.H.5
  • 27
    • 0025871264 scopus 로고
    • MutM, a protein that prevents G:C→T:A transversions, is formamidopyrimidine-DNA glycosylase
    • Michaels ML, Pham L, Cruz C, Miller JH. 1991. MutM, a protein that prevents G:C→T:A transversions, is formamidopyrimidine-DNA glycosylase. Nucleic Acids Research 19:3629-3632.
    • (1991) Nucleic Acids Research , vol.19 , pp. 3629-3632
    • Michaels, M.L.1    Pham, L.2    Cruz, C.3    Miller, J.H.4
  • 33
    • 0030991774 scopus 로고    scopus 로고
    • Mechanism of action of base release by Escherichia coli Fpg protein: Role of lysine 155 in catalysis
    • Rabow LE, Kow YW. 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
  • 37
    • 0035724599 scopus 로고    scopus 로고
    • Ascidian embryos as a model system to analyze expression and function of development genes
    • Satoh N. 2003. Ascidian embryos as a model system to analyze expression and function of development genes. Differentiation 68:1-12.
    • (2003) Differentiation , vol.68 , pp. 1-12
    • Satoh, N.1
  • 39
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxoG
    • Shibutani S, Takeshita M, Grollman AP. 1991. Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxoG. Nature 349:431-434.
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 42
    • 0029896229 scopus 로고    scopus 로고
    • Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae which codes for a DNA glycosylase that excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine
    • van der Kemp PA, Thomas D, Barbey R, de Oliveila R, Boiteux S. 1996. Cloning and expression in Escherichia coli of the OGG1 gene of Saccharomyces cerevisiae which codes for a DNA glycosylase that excises 7,8-dihydro-8- oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine. Proceedings of the National Academy of Sciences of the United States of America 93:5197-5202.
    • (1996) Proceedings of the National Academy of Sciences of the United States of America , vol.93 , pp. 5197-5202
    • Van Der Kemp, P.A.1    Thomas, D.2    Barbey, R.3    De Oliveila, R.4    Boiteux, S.5
  • 43
  • 44
    • 0036628726 scopus 로고    scopus 로고
    • Biological consequences of free radical-damaged DNA bases
    • Wallace SS. 2002. Biological consequences of free radical-damaged DNA bases. Free Radical Biology and Medicine 33:1-14.
    • (2002) Free Radical Biology and Medicine , vol.33 , pp. 1-14
    • Wallace, S.S.1
  • 46
    • 0027455602 scopus 로고
    • Developmental regulation of the base excision repair enzyme uracil DNA glycosylase in the rat
    • Weng Y, Sirover MA. 1993. Developmental regulation of the base excision repair enzyme uracil DNA glycosylase in the rat. Mutation Research 293:133-141.
    • (1993) Mutation Research , vol.293 , pp. 133-141
    • Weng, Y.1    Sirover, M.A.2
  • 47
    • 0026452281 scopus 로고    scopus 로고
    • Genetic effects of oxidative DNA damage: Comparative mutagenesis of 7,8-dihydro-8-oxoguanine and 7,8-dihydro-8-oxoadenine in Escherichia coli
    • Wood ML, Esteve M, Morningstar ML, Kuziemko GM, Essigmann JM. 1996. Genetic effects of oxidative DNA damage: Comparative mutagenesis of 7,8-dihydro-8-oxoguanine and 7,8-dihydro-8-oxoadenine in Escherichia coli. Nucleic Acids Research 20:6023-6032.
    • (1996) Nucleic Acids Research , vol.20 , pp. 6023-6032
    • Wood, M.L.1    Esteve, M.2    Morningstar, M.L.3    Kuziemko, G.M.4    Essigmann, J.M.5
  • 48
    • 4644366937 scopus 로고    scopus 로고
    • Identification of downstream genes of the ascidian muscle determinant gene Ci-machol
    • Yagi K, Satoh N, Satou Y. 2004. Identification of downstream genes of the ascidian muscle determinant gene Ci-machol. Developmental Biology 15:478-489.
    • (2004) Developmental Biology , vol.15 , pp. 478-489
    • Yagi, K.1    Satoh, N.2    Satou, Y.3
  • 49
    • 0030770356 scopus 로고    scopus 로고
    • Biochemical and physicochemical characterization of normal and variant forms of human MTH1 protein with antimutagenic activity
    • Yakushiji H, Maraboeuf F, Takahashi M, Deng ZS, Kawabata S, Nakabeppu Y, Sekiguchi M. 1997. Biochemical and physicochemical characterization of normal and variant forms of human MTH1 protein with antimutagenic activity. Mutation Research 384:181-194.
    • (1997) Mutation Research , vol.384 , pp. 181-194
    • Yakushiji, H.1    Maraboeuf, F.2    Takahashi, M.3    Deng, Z.S.4    Kawabata, S.5    Nakabeppu, Y.6    Sekiguchi, M.7
  • 50
    • 0347135657 scopus 로고    scopus 로고
    • Morpholino-based gene knockdown screen of novel genes with developmental function in Ciona intestinalis
    • Yamada L, Shoguchi E, Wada S, Kobayashi K, Mochizuki Y, Satou Y, Satoh N. 2003. Morpholino-based gene knockdown screen of novel genes with developmental function in Ciona intestinalis. Development 130:6485-6495.
    • (2003) Development , vol.130 , pp. 6485-6495
    • Yamada, L.1    Shoguchi, E.2    Wada, S.3    Kobayashi, K.4    Mochizuki, Y.5    Satou, Y.6    Satoh, N.7
  • 51
    • 0032531869 scopus 로고    scopus 로고
    • Escherichia coli MutY protein has a guanine-DNA glycosylase that acts on 7,8-dihydro-8-oxoguanine:guanine mispair to prevent spontaneous G:C-C:G transversions
    • Zhang Q-M, Ishikawa N, Nakahara T, Yonei S. 1998. Escherichia coli MutY protein has a guanine-DNA glycosylase that acts on 7,8-dihydro-8-oxoguanine: guanine mispair to prevent spontaneous G:C-C:G transversions. Nucleic Acids Research 26:4669-4675.
    • (1998) Nucleic Acids Research , vol.26 , pp. 4669-4675
    • Zhang, Q.-M.1    Ishikawa, N.2    Nakahara, T.3    Yonei, S.4
  • 52
    • 0034634691 scopus 로고    scopus 로고
    • Identification of repair enzymes for 5-formyluracil in DNA: Nth, Nei and MutM proteins of Escherichia coli
    • Zhang Q-M, Miyabe I, Matsumoto Y, Kino K, Sugiyama H, Yonei S. 2000. Identification of repair enzymes for 5-formyluracil in DNA: Nth, Nei and MutM proteins of Escherichia coli. Journal of Biological Chemistry 275:35471-35477.
    • (2000) Journal of Biological Chemistry , vol.275 , pp. 35471-35477
    • Zhang, Q.-M.1    Miyabe, I.2    Matsumoto, Y.3    Kino, K.4    Sugiyama, H.5    Yonei, S.6
  • 53
    • 7944227532 scopus 로고    scopus 로고
    • DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTH1 enzymes in human cells
    • Zhang Q-M, Yonekura S, Takao M, Yasui A, Sugiyama H, Yonei S. 2005. DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the hNEIL1 and hNTH1 enzymes in human cells. DNA Repair 4:71-79.
    • (2005) DNA Repair , vol.4 , pp. 71-79
    • Zhang, Q.-M.1    Yonekura, S.2    Takao, M.3    Yasui, A.4    Sugiyama, H.5    Yonei, S.6


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