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Volumn 7, Issue 1, 2008, Pages 31-39

Discrimination of lesion removal of N-methylpurine-DNA glycosylase revealed by a potent neutralizing monoclonal antibody

Author keywords

Base excision repair; Epitope mapping; Inhibition; MPG; Substrate specificity

Indexed keywords

HYPOXANTHINE; IMMUNOGLOBULIN G1; IMMUNOGLOBULIN G2A; IMMUNOGLOBULIN G2B; MONOCLONAL ANTIBODY; N METHYLPURINE DNA GLYCOSYLASE; NEUTRALIZING ANTIBODY; POLYDEOXYRIBONUCLEOTIDE SYNTHASE; UNCLASSIFIED DRUG;

EID: 36549048414     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2007.07.012     Document Type: Article
Times cited : (8)

References (36)
  • 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 362 (1993) 709-715
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 3
    • 0022363977 scopus 로고
    • Methylation-induced blocks to in vitro DNA replication
    • Larson K., Sahm J., Shenkar R., and Strauss B. Methylation-induced blocks to in vitro DNA replication. Mutat. Res. 150 (1985) 77-84
    • (1985) Mutat. Res. , vol.150 , pp. 77-84
    • Larson, K.1    Sahm, J.2    Shenkar, R.3    Strauss, B.4
  • 4
    • 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 L., and 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. 259 (1984) 5543-5548
    • (1984) J. Biol. Chem. , vol.259 , pp. 5543-5548
    • Breimer, L.1    Lindahl, T.2
  • 5
    • 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. 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 (1994) 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
  • 6
    • 0030787013 scopus 로고    scopus 로고
    • What structural features determine repair enzyme specificity and mechanism in chemically modified DNA?
    • Singer B., and Hang B. What structural features determine repair enzyme specificity and mechanism in chemically modified DNA?. Chem. Res. Toxicol. 10 (1997) 713-732
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 713-732
    • Singer, B.1    Hang, B.2
  • 7
    • 0032512439 scopus 로고    scopus 로고
    • Specific interaction of wild-type and truncated mouse N-methylpurine-DNA glycosylase with ethenoadenine-containing DNA
    • Roy R., Biswas T., Hazra T.K., Roy G., Grabowski D.T., Izumi T., Srinivasan G., and Mitra S. Specific interaction of wild-type and truncated mouse N-methylpurine-DNA glycosylase with ethenoadenine-containing DNA. Biochemistry 37 (1998) 580-589
    • (1998) Biochemistry , vol.37 , pp. 580-589
    • Roy, R.1    Biswas, T.2    Hazra, T.K.3    Roy, G.4    Grabowski, D.T.5    Izumi, T.6    Srinivasan, G.7    Mitra, S.8
  • 8
    • 0028657625 scopus 로고
    • Purification and biochemical characterization of recombinant N-methylpurine-DNA glycosylase of the mouse
    • Roy R., Brooks C., and Mitra S. Purification and biochemical characterization of recombinant N-methylpurine-DNA glycosylase of the mouse. Biochemistry 33 (1994) 15131-15140
    • (1994) Biochemistry , vol.33 , pp. 15131-15140
    • Roy, R.1    Brooks, C.2    Mitra, S.3
  • 9
    • 0029829188 scopus 로고    scopus 로고
    • Distinct substrate preference of human and mouse N-methylpurine-DNA glycosylases
    • Roy R., Kennel S.J., and Mitra S. Distinct substrate preference of human and mouse N-methylpurine-DNA glycosylases. Carcinogenesis 17 (1996) 2177-2182
    • (1996) Carcinogenesis , vol.17 , pp. 2177-2182
    • Roy, R.1    Kennel, S.J.2    Mitra, S.3
  • 10
    • 0027759522 scopus 로고
    • Purification and characterization of human 3-methyladenine-DNA glycosylase
    • O' Connor T.R. Purification and characterization of human 3-methyladenine-DNA glycosylase. Nucl. Acids Res. 21 (1993) 5561-5569
    • (1993) Nucl. Acids Res. , vol.21 , pp. 5561-5569
    • O' Connor, T.R.1
  • 11
    • 0028239225 scopus 로고
    • Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases
    • Saparbaev M., and Laval J. Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 5873-5877
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 5873-5877
    • Saparbaev, M.1    Laval, J.2
  • 12
    • 0028174274 scopus 로고
    • 1,N6-ethenoadenine is preferred over 3-methyladenine as substrate by a cloned human N-methylpurine-DNA glycosylase (3-methyladenine-DNA glycosylase)
    • Dosanjh M.K., Roy R., Mitra S., and Singer B. 1,N6-ethenoadenine is preferred over 3-methyladenine as substrate by a cloned human N-methylpurine-DNA glycosylase (3-methyladenine-DNA glycosylase). Biochemistry 33 (1994) 1624-1628
    • (1994) Biochemistry , vol.33 , pp. 1624-1628
    • Dosanjh, M.K.1    Roy, R.2    Mitra, S.3    Singer, B.4
  • 14
    • 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 A.Y., Scharer O.D., Samson L., Verdine G.L., and Ellenberger T. Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision. Cell 95 (1998) 249-258
    • (1998) Cell , vol.95 , pp. 249-258
    • Lau, A.Y.1    Scharer, O.D.2    Samson, L.3    Verdine, G.L.4    Ellenberger, T.5
  • 15
    • 0023919219 scopus 로고
    • Regulation and expression of the adaptive response to alkylating agents
    • Lindahl T., Sedgwick B., Sekiguchi M., and Nakabeppu Y. Regulation and expression of the adaptive response to alkylating agents. Annu. Rev. Biochem. 57 (1988) 133-157
    • (1988) Annu. Rev. Biochem. , vol.57 , pp. 133-157
    • Lindahl, T.1    Sedgwick, B.2    Sekiguchi, M.3    Nakabeppu, Y.4
  • 16
    • 0021402416 scopus 로고
    • Inducible repair of O-alkylated DNA pyrimidines in Escherichia coli
    • McCarthy T.V., Karran P., and Lindahl T. Inducible repair of O-alkylated DNA pyrimidines in Escherichia coli. EMBO J. 3 (1984) 545-550
    • (1984) EMBO J. , vol.3 , pp. 545-550
    • McCarthy, T.V.1    Karran, P.2    Lindahl, T.3
  • 17
    • 0028045942 scopus 로고
    • DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the AlkA enzyme in Escherichia coli
    • Bjelland S., Birkeland N.K., Benneche T., Volden G., and Seeberg E. DNA glycosylase activities for thymine residues oxidized in the methyl group are functions of the AlkA enzyme in Escherichia coli. J. Biol. Chem. 269 (1994) 30489-30495
    • (1994) J. Biol. Chem. , vol.269 , pp. 30489-30495
    • Bjelland, S.1    Birkeland, N.K.2    Benneche, T.3    Volden, G.4    Seeberg, E.5
  • 18
    • 0028903751 scopus 로고
    • Purification and properties of the alkylation repair DNA glycosylase encoded the MAG gene from Saccharomyces cerevisiae
    • Bjoras M., Klungland A., Johansen R.F., and Seeberg E. Purification and properties of the alkylation repair DNA glycosylase encoded the MAG gene from Saccharomyces cerevisiae. Biochemistry 34 (1995) 4577-4582
    • (1995) Biochemistry , vol.34 , pp. 4577-4582
    • Bjoras, M.1    Klungland, A.2    Johansen, R.F.3    Seeberg, E.4
  • 19
    • 0029819596 scopus 로고    scopus 로고
    • The domains of mammalian base excision repair enzyme N-methylpurine-DNA glycosylase. Interaction, conformational change, and role in DNA binding and damage recognition
    • Roy R., Kumar A., Lee J.C., and Mitra S. The domains of mammalian base excision repair enzyme N-methylpurine-DNA glycosylase. Interaction, conformational change, and role in DNA binding and damage recognition. J. Biol. Chem. 271 (1996) 23690-23697
    • (1996) J. Biol. Chem. , vol.271 , pp. 23690-23697
    • Roy, R.1    Kumar, A.2    Lee, J.C.3    Mitra, S.4
  • 20
    • 0037178808 scopus 로고    scopus 로고
    • 1,N(2)-ethenoguanine, a mutagenic DNA adduct, is a primary substrate of Escherichia coli mismatch- specific uracil-DNA glycosylase and human alkylpurine-DNA-N-glycosylase
    • Saparbaev M., Langouet S., Privezentzev C.V., Guengerich F.P., Cai H., Elder R.H., and Laval J. 1,N(2)-ethenoguanine, a mutagenic DNA adduct, is a primary substrate of Escherichia coli mismatch- specific uracil-DNA glycosylase and human alkylpurine-DNA-N-glycosylase. J. Biol. Chem. 277 (2002) 26987-26993
    • (2002) J. Biol. Chem. , vol.277 , pp. 26987-26993
    • Saparbaev, M.1    Langouet, S.2    Privezentzev, C.V.3    Guengerich, F.P.4    Cai, H.5    Elder, R.H.6    Laval, J.7
  • 21
    • 0022993948 scopus 로고
    • Site-specific mutagenesis in vivo by single methylated or deaminated purine bases
    • Hill-Perkins M., Jones M.D., and Karran P. Site-specific mutagenesis in vivo by single methylated or deaminated purine bases. Mutat. Res. 162 (1986) 153-163
    • (1986) Mutat. Res. , vol.162 , pp. 153-163
    • Hill-Perkins, M.1    Jones, M.D.2    Karran, P.3
  • 22
    • 0018620965 scopus 로고
    • DNA glycosylases, endonucleases for apurinic/apyrimidinic sites, and base excision-repair
    • Lindahl T. DNA glycosylases, endonucleases for apurinic/apyrimidinic sites, and base excision-repair. Prog. Nucleic Acid Res. Mol. Biol. 22 (1979) 135-163
    • (1979) Prog. Nucleic Acid Res. Mol. Biol. , vol.22 , pp. 135-163
    • Lindahl, T.1
  • 23
    • 0025949662 scopus 로고
    • Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase
    • Chakravarti D., Ibeanu G.C., Tano K., and Mitra S. Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase. J. Biol. Chem. 266 (1991) 15710-15715
    • (1991) J. Biol. Chem. , vol.266 , pp. 15710-15715
    • Chakravarti, D.1    Ibeanu, G.C.2    Tano, K.3    Mitra, S.4
  • 24
    • 0019410292 scopus 로고
    • Analysis of surface proteins of mouse lung carcinomas using monoclonal antibodies
    • Kennel S.J., Foote L.J., and Lankford P.K. Analysis of surface proteins of mouse lung carcinomas using monoclonal antibodies. Cancer Res. 41 (1981) 3465-3470
    • (1981) Cancer Res. , vol.41 , pp. 3465-3470
    • Kennel, S.J.1    Foote, L.J.2    Lankford, P.K.3
  • 25
    • 0018953062 scopus 로고
    • Production of monoclonal antibodies: strategy and tactics
    • de St. Groth S.F., and Scheidegger D.J. Production of monoclonal antibodies: strategy and tactics. J. Immunol. Methods 35 (1980) 1-21
    • (1980) J. Immunol. Methods , vol.35 , pp. 1-21
    • de St. Groth, S.F.1    Scheidegger, D.J.2
  • 26
    • 0020491969 scopus 로고
    • Binding of monoclonal antibody to protein antigen in fluid phase or bound to solid supports
    • Kennel S.J. Binding of monoclonal antibody to protein antigen in fluid phase or bound to solid supports. J. Immunol. Methods 26 (1982) 1-12
    • (1982) J. Immunol. Methods , vol.26 , pp. 1-12
    • Kennel, S.J.1
  • 27
    • 0019457053 scopus 로고
    • Monoclonal antibodies from rats immunized with fragment D of human fibrinogen
    • Kennel S.J., Chen J.P., Lankford P.K., and Foote L.J. Monoclonal antibodies from rats immunized with fragment D of human fibrinogen. Thromb. Res. 22 (1981) 309-320
    • (1981) Thromb. Res. , vol.22 , pp. 309-320
    • Kennel, S.J.1    Chen, J.P.2    Lankford, P.K.3    Foote, L.J.4
  • 28
    • 0036936756 scopus 로고    scopus 로고
    • S.J. Monoclonal antibodies to CD44 epitopes on mouse endothelium
    • Davern S.M., Lankford P.K., and Foote L.J. S.J. Monoclonal antibodies to CD44 epitopes on mouse endothelium. Hybrid. Hybridomics 21 (2002) 339-349
    • (2002) Hybrid. Hybridomics , vol.21 , pp. 339-349
    • Davern, S.M.1    Lankford, P.K.2    Foote, L.J.3
  • 29
    • 0019877035 scopus 로고
    • Shotgun DNA sequencing using cloned DNase I-generated fragments
    • Anderson S. Shotgun DNA sequencing using cloned DNase I-generated fragments. Nucleic Acids Res. 9 (1981) 3015-3027
    • (1981) Nucleic Acids Res. , vol.9 , pp. 3015-3027
    • Anderson, S.1
  • 31
    • 0034635534 scopus 로고    scopus 로고
    • Mutation of a unique aspartate residue abolishes the catalytic activity but not substrate binding of the mouse N-methylpurine-DNA glycosylase (MPG)
    • Roy R., Biswas T., Lee J.C., and Mitra S. Mutation of a unique aspartate residue abolishes the catalytic activity but not substrate binding of the mouse N-methylpurine-DNA glycosylase (MPG). J. Biol. Chem. 275 (2000) 4278-4282
    • (2000) J. Biol. Chem. , vol.275 , pp. 4278-4282
    • Roy, R.1    Biswas, T.2    Lee, J.C.3    Mitra, S.4
  • 32
    • 33749568015 scopus 로고    scopus 로고
    • Magnesium, essential for base excision repair enzymes, inhibits substrate binding of N-methylpurine-DNA glycosylase
    • Adhikari S., Toretsky J.A., Yuan L., and Roy R. Magnesium, essential for base excision repair enzymes, inhibits substrate binding of N-methylpurine-DNA glycosylase. J. Biol. Chem. 281 (2006) 29525-29532
    • (2006) J. Biol. Chem. , vol.281 , pp. 29525-29532
    • Adhikari, S.1    Toretsky, J.A.2    Yuan, L.3    Roy, R.4
  • 33
    • 0026574664 scopus 로고
    • Characterization of the Escherichia coli uracil-DNA glycosylase. Inhibitor protein complex
    • Bennett S.E., and Mosbaugh D.W. Characterization of the Escherichia coli uracil-DNA glycosylase. Inhibitor protein complex. J. Biol. Chem. 267 (1992) 22512-22521
    • (1992) J. Biol. Chem. , vol.267 , pp. 22512-22521
    • Bennett, S.E.1    Mosbaugh, D.W.2
  • 35
    • 0034610336 scopus 로고    scopus 로고
    • Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG
    • Lau A.Y., Wyatt M.D., Glassner B.J., Samson L.D., and Ellenberger T. Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG. Proc. Natl. Acad. Sci. U.S.A. 5 (2000) 13573-13578
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.5 , pp. 13573-13578
    • Lau, A.Y.1    Wyatt, M.D.2    Glassner, B.J.3    Samson, L.D.4    Ellenberger, T.5
  • 36
    • 1642411206 scopus 로고    scopus 로고
    • Dissecting the broad substrate specificity of human 3-methyladenine- DNA glycosylase
    • O'Brien P.J., and Ellenberger T. Dissecting the broad substrate specificity of human 3-methyladenine- DNA glycosylase. J. Biol. Chem. 279 (2004) 9750-9757
    • (2004) J. Biol. Chem. , vol.279 , pp. 9750-9757
    • O'Brien, P.J.1    Ellenberger, T.2


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