메뉴 건너뛰기




Volumn 38, Issue 6, 2005, Pages 676-682

Functional identification of an 8-oxoguanine specific endonuclease from thermotoga maritima

Author keywords

8 Oxoguanine; DNA glycosylase; DNA repair; Hypothetical protein; Thermotoga maritima

Indexed keywords

ARCHAEA; ESCHERICHIA COLI; THERMOTOGA MARITIMA; THERMOTOGALES;

EID: 32644442066     PISSN: 12258687     EISSN: 12258687     Source Type: Journal    
DOI: 10.5483/bmbrep.2005.38.6.676     Document Type: Review
Times cited : (10)

References (30)
  • 2
    • 0034060037 scopus 로고    scopus 로고
    • The human genome project-an overview
    • Bentley, D. R. (2000) The human genome project-an overview. Med. Res. Rev. 20, 189-196.
    • (2000) Med. Res. Rev. , vol.20 , pp. 189-196
    • Bentley, D.R.1
  • 3
    • 0025240665 scopus 로고
    • Homogeneous Escherichia coli FPG protein. A DNA glycosylase which excises imidazole ring-opened purines and nicks DNA at apurinic/apyrimidinic sites
    • Boiteux, S., O'Connor, T. R., Lederer, F., Gouyette, A. and Laval, J. (1990) Homogeneous Escherichia coli FPG protein. A DNA glycosylase which excises imidazole ring-opened purines and nicks DNA at apurinic/apyrimidinic sites. J. Biol. Chem. 265, 3916-3922.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3916-3922
    • Boiteux, S.1    O'Connor, T.R.2    Lederer, F.3    Gouyette, A.4    Laval, J.5
  • 4
    • 0001183058 scopus 로고
    • Mobile modules and motifs
    • Bork, P. (1992) Mobile modules and motifs. Curr. Opin. Struct. Biol. 2, 413-421.
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 413-421
    • Bork, P.1
  • 5
    • 0029997801 scopus 로고    scopus 로고
    • Applying motif and profile searches
    • Bork, P. and Gibson, T. J. (1996) Applying motif and profile searches. Methods Enzymol. 266, 162-184.
    • (1996) Methods Enzymol. , vol.266 , pp. 162-184
    • Bork, P.1    Gibson, T.J.2
  • 6
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 7
    • 0030271920 scopus 로고    scopus 로고
    • Go hunting in sequence databases but watch out for traps
    • Brock, P. and Bairoch, A. (1996) Go hunting in sequence databases but watch out for traps. Trends Genet. 12, 425-427.
    • (1996) Trends Genet. , vol.12 , pp. 425-427
    • Brock, P.1    Bairoch, A.2
  • 8
    • 0345448169 scopus 로고    scopus 로고
    • Substrate specificities and excision kinetics of DNA glycosylases involved in base-excision repair of oxidative DNA damage
    • Dizdaroglu, M. (2003) Substrate specificities and excision kinetics of DNA glycosylases involved in base-excision repair of oxidative DNA damage. Mutat. Res. 531, 109-126.
    • (2003) Mutat. Res. , vol.531 , pp. 109-126
    • Dizdaroglu, M.1
  • 9
    • 0029929070 scopus 로고    scopus 로고
    • The helixhairpin-helix DNA-binding motif: A structural basis for non-sequence-specific recognition of DNA
    • Doherty, A. J., Serpell, L. C. and Ponting, C. P. (1996) The helixhairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA. Nucleic Acids Res. 24, 2488-2497.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2488-2497
    • Doherty, A.J.1    Serpell, L.C.2    Ponting, C.P.3
  • 10
    • 0032493309 scopus 로고    scopus 로고
    • Deoxyribose phosphate excision by the N-terminal domain of the polymerase beta: The mechanism revisited
    • Feng, J. A., Crasto, C. J. and Matsumoto, Y. (1998) Deoxyribose phosphate excision by the N-terminal domain of the polymerase beta: the mechanism revisited. Biochemistry 37, 9605-9611.
    • (1998) Biochemistry , vol.37 , pp. 9605-9611
    • Feng, J.A.1    Crasto, C.J.2    Matsumoto, Y.3
  • 12
    • 0034680168 scopus 로고    scopus 로고
    • Microbial genome sequencing
    • Fraser, C. M., Eisen, J. A. and Salzberg, S. L. (2000) Microbial genome sequencing. Nature 406, 799-803.
    • (2000) Nature , vol.406 , pp. 799-803
    • Fraser, C.M.1    Eisen, J.A.2    Salzberg, S.L.3
  • 14
    • 0032698574 scopus 로고    scopus 로고
    • Characterization of an 8-oxoguanine DNA glycosylase from Methanococcus jannaschii
    • Gogos, A. and Clarke, N. D. (1999) Characterization of an 8-oxoguanine DNA glycosylase from Methanococcus jannaschii, J. Biol. Chem. 274, 30447-30450.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30447-30450
    • Gogos, A.1    Clarke, N.D.2
  • 15
    • 0032533794 scopus 로고    scopus 로고
    • The presence of two distinct 8-oxoguanine repair enzymes in human cells: Their potential complementary roles in preventing mutation
    • Hazra, T. K., Izumi, T., Maidt, L., Floyd, R. A. and Mitra, S. (1998) The presence of two distinct 8-oxoguanine repair enzymes in human cells: their potential complementary roles in preventing mutation. Nucleic Acids Res. 26, 5116-5122.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 5116-5122
    • Hazra, T.K.1    Izumi, T.2    Maidt, L.3    Floyd, R.A.4    Mitra, S.5
  • 16
    • 0033563413 scopus 로고    scopus 로고
    • Two strategies for sequence comparison: Profile-preprocessed and secondary structure-induced multiple alignment
    • Heringa, J. (1999) Two strategies for sequence comparison: profile-preprocessed and secondary structure-induced multiple alignment. Comput. Chem. 23, 341-364.
    • (1999) Comput. Chem. , vol.23 , pp. 341-364
    • Heringa, J.1
  • 17
    • 0030861915 scopus 로고    scopus 로고
    • DNA glycosylase in the base excision repair of DNA
    • Krokan, H. E., Standal, R. and Slupphaug, G. (1997) DNA glycosylase in the base excision repair of DNA. Biochem. J. 325, 1-16.
    • (1997) Biochem. J. , vol.325 , pp. 1-16
    • Krokan, H.E.1    Standal, R.2    Slupphaug, G.3
  • 18
    • 0035623430 scopus 로고    scopus 로고
    • Recognition of DNA damage in mammals
    • Lee, S. H. (2001) Recognition of DNA damage in mammals. J. Biochem. Mol. Biol. 34, 489-495.
    • (2001) J. Biochem. Mol. Biol. , vol.34 , pp. 489-495
    • Lee, S.H.1
  • 19
    • 0025871264 scopus 로고
    • MutM, a protein that prevents G · C →T · A transversions, is formamidopyrimidine-DNA glycosylase
    • Michaels, M. L., Pham, L., Cruz, C. and Miller, J. H. (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    Pham, L.2    Cruz, C.3    Miller, J.H.4
  • 20
    • 0030891201 scopus 로고    scopus 로고
    • DNA polymerase b in abasic site repair: A structurally conserved helix-hairpin-helix motif in lesion detection by base excision repair enzymes
    • Mullen, G. P. and Wilson, S. H. (1997) DNA polymerase b in abasic site repair: A structurally conserved helix-hairpin-helix motif in lesion detection by base excision repair enzymes. Biochemistry 36, 4713-4717.
    • (1997) Biochemistry , vol.36 , pp. 4713-4717
    • Mullen, G.P.1    Wilson, S.H.2
  • 21
    • 0030220956 scopus 로고    scopus 로고
    • Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily
    • Nash, H. M., Bruner, S. D., Scharer, O. D., Kawate, T., Addona, T. A., Spooner, E., Lane, W. S. and Verdine, G. L. (1996) Cloning of a yeast 8-oxoguanine DNA glycosylase reveals the existence of a base-excision DNA-repair protein superfamily. Curr. Biol. 6, 968-980.
    • (1996) Curr. Biol. , vol.6 , pp. 968-980
    • Nash, H.M.1    Bruner, S.D.2    Scharer, O.D.3    Kawate, T.4    Addona, T.A.5    Spooner, E.6    Lane, W.S.7    Verdine, G.L.8
  • 23
    • 0032716382 scopus 로고    scopus 로고
    • Nucleotide excision repair: From E. coll to man
    • Petit, C. and Sancar, A. (1999) Nucleotide excision repair: from E. coll to man. Biochimie 81, 15-25.
    • (1999) Biochimie , vol.81 , pp. 15-25
    • Petit, C.1    Sancar, A.2
  • 24
    • 0030816108 scopus 로고    scopus 로고
    • Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae
    • Radicella, J. P., Dherin, C., Desmaze, C., Fox, M. S. and Boiteux, S. (1997) Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae. Proc. Natl. Acad Sci. USA 94, 8010-8015.
    • (1997) Proc. Natl. Acad Sci. USA , vol.94 , pp. 8010-8015
    • Radicella, J.P.1    Dherin, C.2    Desmaze, C.3    Fox, M.S.4    Boiteux, S.5
  • 25
    • 0030738194 scopus 로고    scopus 로고
    • Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase
    • Rosenquist, T. A., Zharkov, A. P. and Grollman, A. P. (1997) Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase. Proc. Natl. Acad. Sci. USA 94, 7429-7434.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7429-7434
    • Rosenquist, T.A.1    Zharkov, A.P.2    Grollman, A.P.3
  • 26
    • 0037115963 scopus 로고    scopus 로고
    • Oxidative nucleotide damage: Consequences and prevention
    • Sekiguchi, M. and Tsuzuki, T. (2002) Oxidative nucleotide damage: consequences and prevention. Oncogene 21, 8895-8904.
    • (2002) Oncogene , vol.21 , pp. 8895-8904
    • Sekiguchi, M.1    Tsuzuki, T.2
  • 27
    • 0034616341 scopus 로고    scopus 로고
    • Role of the N-terminal proline residue in the catalytic activities of the Escherichia coli Fpg protein
    • Sidorkina, O. M. and Lavai, J. (2000) Role of the N-terminal proline residue in the catalytic activities of the Escherichia coli Fpg protein. J. Biol. Chem. 275, 9924-9929.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9924-9929
    • Sidorkina, O.M.1    Lavai, J.2
  • 28
    • 0033991416 scopus 로고    scopus 로고
    • Sequence analysis of genes and genomes
    • Sterky, F. and Lundeberg, J. (2000) Sequence analysis of genes and genomes. J. Biotechnol. 76, 1-31.
    • (2000) J. Biotechnol. , vol.76 , pp. 1-31
    • Sterky, F.1    Lundeberg, J.2
  • 29
    • 0037867770 scopus 로고    scopus 로고
    • Imidazole ring-opened DNA purines and their biological significance
    • Tudek, B. (2003) Imidazole ring-opened DNA purines and their biological significance. J. Biochem. Mol. Biol. 36, 12-19.
    • (2003) J. Biochem. Mol. Biol. , vol.36 , pp. 12-19
    • Tudek, B.1
  • 30
    • 0030614471 scopus 로고    scopus 로고
    • 2-terminal proline acts as a nucleophile in the glycosylase/AP-lyase reaction catalyzed by Escherichia coli formamidopyrimidine- DNA glycosylase (Fpg) protein
    • 2-terminal proline acts as a nucleophile in the glycosylase/AP-lyase reaction catalyzed by Escherichia coli formamidopyrimidine- 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.