메뉴 건너뛰기




Volumn 40, Issue 22, 2012, Pages 11638-11647

Defining the functional footprint for recognition and repair of deaminated DNA

Author keywords

[No Author keywords available]

Indexed keywords

ALKYLADENINE DNA GLYCOSYLTRANSFERASE; DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; DNA GLYCOSYLTRANSFERASE; OLIGONUCLEOTIDE; UNCLASSIFIED DRUG;

EID: 84871251700     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks952     Document Type: Article
Times cited : (11)

References (42)
  • 1
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • Lindahl, T. (1993) Instability and decay of the primary structure of DNA. Nature, 362, 709-715.
    • (1993) Nature , vol.362 , pp. 709-715
    • Lindahl, T.1
  • 2
    • 0020490817 scopus 로고
    • Metabolism of dITP in HeLa cell extracts, incorporation into DNA by isolated nuclei and release of hypoxanthine from DNA by a hypoxanthine-DNA glycosylase activity
    • Myrnes, B., Guddal, P. H. and Krokan, H. (1982) Metabolism of dITP in HeLa cell extracts, incorporation into DNA by isolated nuclei and release of hypoxanthine from DNA by a hypoxanthine-DNA glycosylase activity. Nucleic Acids Res., 10, 3693-3701.
    • (1982) Nucleic Acids Res , vol.10 , pp. 3693-3701
    • Myrnes, B.1    Guddal, P.H.2    Krokan, H.3
  • 3
    • 0025800612 scopus 로고
    • Preferential recognition of I. T base-pairs in the initiation of excision-repair by hypoxanthine-DNA glycosylase
    • Dianov, G. and Lindahl, T. (1991) Preferential recognition of I. T base-pairs in the initiation of excision-repair by hypoxanthine-DNA glycosylase. Nucleic Acids Res., 19, 3829-3833.
    • (1991) Nucleic Acids Res , vol.19 , pp. 3829-3833
    • Dianov, G.1    Lindahl, T.2
  • 4
    • 0016257644 scopus 로고
    • Heat-induced deamination of cytosine residues in deoxyribonucleic acid
    • Lindahl, T. and Nyberg, B. (1974) Heat-induced deamination of cytosine residues in deoxyribonucleic acid. Biochemistry, 13, 3405-3410.
    • (1974) Biochemistry , vol.13 , pp. 3405-3410
    • Lindahl, T.1    Nyberg, B.2
  • 5
    • 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. (1994) Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases. Proc. Natl Acad. Sci. USA, 91, 5873-5877.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 5873-5877
    • Saparbaev, M.1    Laval, J.2
  • 7
    • 0344061031 scopus 로고    scopus 로고
    • Stability, miscoding potential, and repair of 20-deoxyxanthosine in DNA: Implications for nitric oxide-induced mutagenesis
    • Wuenschell, G. E., O'Connor, T. R. and Termini, J. (2003) Stability, miscoding potential, and repair of 20-deoxyxanthosine in DNA: implications for nitric oxide-induced mutagenesis. Biochemistry, 42, 3608-3616.
    • (2003) Biochemistry , vol.42 , pp. 3608-3616
    • Wuenschell, G.E.1    O'Connor, T.R.2    Termini, J.3
  • 8
    • 36549042510 scopus 로고    scopus 로고
    • Oxanine DNA glycosylase activities in mammalian systems
    • Dong, L., Meira, L. B., Hazra, T. K., Samson, L. D. and Cao, W. (2008) Oxanine DNA glycosylase activities in mammalian systems. DNA Repair, 7, 128-134.
    • (2008) DNA Repair , vol.7 , pp. 128-134
    • Dong, L.1    Meira, L.B.2    Hazra, T.K.3    Samson, L.D.4    Cao, W.5
  • 9
    • 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. (1998) Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision. Cell, 95, 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
  • 10
    • 0034610336 scopus 로고    scopus 로고
    • Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase
    • Lau, A. Y., Wyatt, M. D., Glassner, B. J., Samson, L. D. and Ellenberger, T. (2000) Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG. Proc. Natl Acad. Sci. USA, 97, 13573-13578.
    • (2000) AAG. Proc. Natl Acad. Sci. USA , vol.97 , pp. 13573-13578
    • Lau, A.Y.1    Wyatt, M.D.2    Glassner, B.J.3    Samson, L.D.4    Ellenberger, T.5
  • 11
    • 79953861195 scopus 로고    scopus 로고
    • Structural basis for the inhibition of human alkyladenine DNA glycosylase (AAG) by 3, N4-ethenocytosine-containing DNA
    • Lingaraju, G. M., Davis, C. A., Setser, J. W., Samson, L. D. and Drennan, C. L. (2011) Structural basis for the inhibition of human alkyladenine DNA glycosylase (AAG) by 3, N4-ethenocytosine-containing DNA. J. Biol. Chem., 286, 13205-13213.
    • (2011) J. Biol. Chem , vol.286 , pp. 13205-13213
    • Lingaraju, G.M.1    Davis, C.A.2    Setser, J.W.3    Samson, L.D.4    Drennan, C.L.5
  • 12
    • 1642411206 scopus 로고    scopus 로고
    • Dissecting the broad substrate specificity of human 3-methyladenine-DNA glycosylase
    • O'Brien, P. J. and Ellenberger, T. (2004) Dissecting the broad substrate specificity of human 3-methyladenine-DNA glycosylase. J. Biol. Chem., 279, 9750-9757.
    • (2004) J. Biol. Chem , vol.279 , pp. 9750-9757
    • O'Brien, P.J.1    Ellenberger, T.2
  • 13
    • 84856812291 scopus 로고    scopus 로고
    • Searching for DNA lesions: Structural evidence for lower-and higher-affinity DNA binding conformations of human alkyladenine DNA glycosylase
    • Setser, J. W., Lingaraju, G. M., Davis, C. A., Samson, L. D. and Drennan, C. L. (2012) Searching for DNA lesions: structural evidence for lower-and higher-affinity DNA binding conformations of human alkyladenine DNA glycosylase. Biochemistry, 51, 382-390.
    • (2012) Biochemistry , vol.51 , pp. 382-390
    • Setser, J.W.1    Lingaraju, G.M.2    Davis, C.A.3    Samson, L.D.4    Drennan, C.L.5
  • 14
    • 77956412697 scopus 로고    scopus 로고
    • Nonspecific DNA binding and coordination of the first two steps of base excision repair
    • Baldwin, M. R. and O'Brien, P. J. (2010) Nonspecific DNA binding and coordination of the first two steps of base excision repair. Biochemistry, 49, 7879-7891.
    • (2010) Biochemistry , vol.49 , pp. 7879-7891
    • Baldwin, M.R.1    O'Brien, P.J.2
  • 15
    • 0034719372 scopus 로고    scopus 로고
    • DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination [corrected]
    • Mol, C. D., Izumi, T., Mitra, S. and Tainer, J. A. (2000) DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination [corrected]. Nature, 403, 451-456.
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 16
    • 57749097697 scopus 로고    scopus 로고
    • Coordinating the initial steps of base excision repair. Apurinic/apyrimidinic endonuclease 1 actively stimulates thymine DNA glycosylase by disrupting the product complex
    • Fitzgerald, M. E. and Drohat, A. C. (2008) Coordinating the initial steps of base excision repair. Apurinic/apyrimidinic endonuclease 1 actively stimulates thymine DNA glycosylase by disrupting the product complex. J. Biol. Chem., 283, 32680-32690.
    • (2008) J. Biol. Chem , vol.283 , pp. 32680-32690
    • Fitzgerald, M.E.1    Drohat, A.C.2
  • 17
    • 0032951710 scopus 로고    scopus 로고
    • Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease 1
    • Waters, T. R., Gallinari, P., Jiricny, J. and Swann, P. F. (1999) Human thymine DNA glycosylase binds to apurinic sites in DNA but is displaced by human apurinic endonuclease 1. J. Biol. Chem., 274, 67-74.
    • (1999) J. Biol. Chem , vol.274 , pp. 67-74
    • Waters, T.R.1    Gallinari, P.2    Jiricny, J.3    Swann, P.F.4
  • 18
    • 0035863739 scopus 로고    scopus 로고
    • Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: Potential coordination of the initial steps in base excision repair
    • Hill, J. W., Hazra, T. K., Izumi, T. and Mitra, S. (2001) Stimulation of human 8-oxoguanine-DNA glycosylase by AP-endonuclease: potential coordination of the initial steps in base excision repair. Nucleic Acids Res., 29, 430-438.
    • (2001) Nucleic Acids Res , vol.29 , pp. 430-438
    • Hill, J.W.1    Hazra, T.K.2    Izumi, T.3    Mitra, S.4
  • 20
    • 78149469033 scopus 로고    scopus 로고
    • Functions of disordered regions in mammalian early base excision repair proteins
    • Hegde, M. L., Hazra, T. K. and Mitra, S. (2010) Functions of disordered regions in mammalian early base excision repair proteins. Cell. Mol. Life Sci., 67, 3573-3587.
    • (2010) Cell. Mol. Life Sci , vol.67 , pp. 3573-3587
    • Hegde, M.L.1    Hazra, T.K.2    Mitra, S.3
  • 21
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward, J. J., Sodhi, J. S., McGuffin, L. J., Buxton, B. F. and Jones, D. T. (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol., 337, 635-645.
    • (2004) J. Mol. Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 22
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H. J. and Wright, P. E. (2005) Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol., 6, 197-208.
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 23
    • 0142126715 scopus 로고    scopus 로고
    • Human alkyladenine DNA glycosylase uses acid-base catalysis for selective excision of damaged purines
    • O'Brien, P. J. and Ellenberger, T. (2003) Human alkyladenine DNA glycosylase uses acid-base catalysis for selective excision of damaged purines. Biochemistry, 42, 12418-12429.
    • (2003) Biochemistry , vol.42 , pp. 12418-12429
    • O'Brien, P.J.1    Ellenberger, T.2
  • 24
    • 0035815108 scopus 로고    scopus 로고
    • Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease Ape1: Implications for the catalytic mechanism
    • Beernink, P. T., Segelke, B. W., Hadi, M. Z., Erzberger, J. P., Wilson, D. M. 3rd and Rupp, B. (2001) Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism. J. Mol. Biol., 307, 1023-1034.
    • (2001) J. Mol. Biol , vol.307 , pp. 1023-1034
    • Beernink, P.T.1    Segelke, B.W.2    Hadi, M.Z.3    Erzberger, J.P.4    Wilson III, D.M.5    Rupp, B.6
  • 25
    • 0032486475 scopus 로고    scopus 로고
    • Domain mapping of human apurinic/apyrimidinic endonuclease. Structural and functional evidence for a disordered amino terminus and a tight globular carboxyl domain
    • Strauss, P. R. and Holt, C. M. (1998) Domain mapping of human apurinic/apyrimidinic endonuclease. Structural and functional evidence for a disordered amino terminus and a tight globular carboxyl domain. J. Biol. Chem., 273, 14435-14441.
    • (1998) J. Biol. Chem , vol.273 , pp. 14435-14441
    • Strauss, P.R.1    Holt, C.M.2
  • 26
    • 0031901923 scopus 로고    scopus 로고
    • Deletion analysis of human AP-endonuclease: Minimum sequence required for the endonuclease activity
    • Izumi, T. and Mitra, S. (1998) Deletion analysis of human AP-endonuclease: minimum sequence required for the endonuclease activity. Carcinogenesis, 19, 525-527.
    • (1998) Carcinogenesis , vol.19 , pp. 525-527
    • Izumi, T.1    Mitra, S.2
  • 27
    • 67649592232 scopus 로고    scopus 로고
    • Human AP endonuclease 1 stimulates multiple-turnover base excision by alkyladenine DNA glycosylase
    • Baldwin, M. R. and O'Brien, P. J. (2009) Human AP endonuclease 1 stimulates multiple-turnover base excision by alkyladenine DNA glycosylase. Biochemistry, 48, 6022-6033.
    • (2009) Biochemistry , vol.48 , pp. 6022-6033
    • Baldwin, M.R.1    O'Brien, P.J.2
  • 29
    • 55249097156 scopus 로고    scopus 로고
    • Human alkyladenine DNA glycosylase employs a processive search for DNA damage
    • Hedglin, M. and O'Brien, P. J. (2008) Human alkyladenine DNA glycosylase employs a processive search for DNA damage. Biochemistry, 47, 11434-11445.
    • (2008) Biochemistry , vol.47 , pp. 11434-11445
    • Hedglin, M.1    O'Brien, P.J.2
  • 30
    • 35648950472 scopus 로고    scopus 로고
    • Pre-steady-state kinetic characterization of the AP endonuclease activity of human AP endonuclease 1
    • Maher, R. L. and Bloom, L. B. (2007) Pre-steady-state kinetic characterization of the AP endonuclease activity of human AP endonuclease 1. J. Biol. Chem., 282, 30577-30585.
    • (2007) J. Biol. Chem , vol.282 , pp. 30577-30585
    • Maher, R.L.1    Bloom, L.B.2
  • 31
    • 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. (1998) Specific interaction of wild-type and truncated mouse N-methylpurine-DNA glycosylase with ethenoadenine-containing DNA. Biochemistry, 37, 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
  • 32
    • 0032169406 scopus 로고    scopus 로고
    • Interaction of the recombinant human methylpurine-DNA glycosylase (MPG protein) with oligodeoxyribonucleotides containing either hypoxanthine or abasic sites
    • Miao, F., Bouziane, M. and O'Connor, T. R. (1998) Interaction of the recombinant human methylpurine-DNA glycosylase (MPG protein) with oligodeoxyribonucleotides containing either hypoxanthine or abasic sites. Nucleic Acids Res., 26, 4034-4041.
    • (1998) Nucleic Acids Res , vol.26 , pp. 4034-4041
    • Miao, F.1    Bouziane, M.2    O'Connor, T.R.3
  • 33
    • 0034607548 scopus 로고    scopus 로고
    • Mapping the protein-DNA interface and the metal-binding site of the major human apurinic/apyrimidinic endonuclease
    • Nguyen, L. H., Barsky, D., Erzberger, J. P. and Wilson, D. M. 3rd. (2000) Mapping the protein-DNA interface and the metal-binding site of the major human apurinic/apyrimidinic endonuclease. J. Mol. Biol., 298, 447-459.
    • (2000) J. Mol. Biol , vol.298 , pp. 447-459
    • Nguyen, L.H.1    Barsky, D.2    Erzberger, J.P.3    Wilson III, D.M.4
  • 34
    • 80052329330 scopus 로고    scopus 로고
    • Structural, thermodynamic, and kinetic basis for the activities of some nucleic acid repair enzymes
    • Nevinsky, G. A. (2011) Structural, thermodynamic, and kinetic basis for the activities of some nucleic acid repair enzymes. J. Mol. Recognit., 24, 656-677.
    • (2011) J. Mol. Recognit , vol.24 , pp. 656-677
    • Nevinsky, G.A.1
  • 35
    • 4944240061 scopus 로고    scopus 로고
    • Thermodynamic, kinetic and structural basis for recognition and repair of abasic sites in DNA by apurinic/apyrimidinic endonuclease from human placenta
    • Beloglazova, N. G., Kirpota, O. O., Starostin, K. V., Ishchenko, A. A., Yamkovoy, V. I., Zharkov, D. O., Douglas, K. T. and Nevinsky, G. A. (2004) Thermodynamic, kinetic and structural basis for recognition and repair of abasic sites in DNA by apurinic/apyrimidinic endonuclease from human placenta. Nucleic Acids Res., 32, 4134-5146.
    • (2004) Nucleic Acids Res , vol.32 , pp. 4134-5146
    • Beloglazova, N.G.1    Kirpota, O.O.2    Starostin, K.V.3    Ishchenko, A.A.4    Yamkovoy, V.I.5    Zharkov, D.O.6    Douglas, K.T.7    Nevinsky, G.A.8
  • 36
    • 77951895418 scopus 로고    scopus 로고
    • Probing conformational changes in Ape1 during the progression of base excision repair
    • Yu, E., Gaucher, S. P. and Hadi, M. Z. (2010) Probing conformational changes in Ape1 during the progression of base excision repair. Biochemistry, 49, 3786-3796.
    • (2010) Biochemistry , vol.49 , pp. 3786-3796
    • Yu, E.1    Gaucher, S.P.2    Hadi, M.Z.3
  • 37
    • 0026743201 scopus 로고
    • Extraordinarily stable mini-hairpins: Electrophoretical and thermal properties of the various sequence variants of d(GCGAA AGC) and their effect on DNA sequencing
    • Hirao, I., Nishimura, Y., Tagawa, Y., Watanabe, K. and Miura, K. (1992) Extraordinarily stable mini-hairpins: electrophoretical and thermal properties of the various sequence variants of d(GCGAA AGC) and their effect on DNA sequencing. Nucleic Acids Res., 20, 3891-3896.
    • (1992) Nucleic Acids Res , vol.20 , pp. 3891-3896
    • Hirao, I.1    Nishimura, Y.2    Tagawa, Y.3    Watanabe, K.4    Miura, K.5
  • 38
    • 67650021397 scopus 로고    scopus 로고
    • Nucleic acid folding determined by mesoscale modeling and NMR spectroscopy: Solution structure of d(GCGA AAGC)
    • Santini, G. P., Cognet, J. A., Xu, D., Singarapu, K. K. and Herve du Penhoat, C. (2009) Nucleic acid folding determined by mesoscale modeling and NMR spectroscopy: solution structure of d(GCGA AAGC). J. Phys. Chem. B, 113, 6881-6893.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 6881-6893
    • Santini, G.P.1    Cognet, J.A.2    Xu, D.3    Singarapu, K.K.4    Herve Du Penhoat, C.5
  • 39
    • 0025942059 scopus 로고
    • A thermodynamic study of unusually stable RNA and DNA hairpins
    • Antao, V. P., Lai, S. Y. and Tinoco, I. Jr. (1991) A thermodynamic study of unusually stable RNA and DNA hairpins. Nucleic Acids Res., 19, 5901-5905.
    • (1991) Nucleic Acids Res , vol.19 , pp. 5901-5905
    • Antao, V.P.1    Lai, S.Y.2    Tinoco Jr., I.3
  • 40
    • 3142676291 scopus 로고    scopus 로고
    • Protein-DNA footprinting by endcapped duplex oligodeoxyribonucleotides
    • Ng, P. S. and Bergstrom, D. E. (2004) Protein-DNA footprinting by endcapped duplex oligodeoxyribonucleotides. Nucleic Acids Res., 32, e107.
    • (2004) Nucleic Acids Res , vol.32
    • Ng, P.S.1    Bergstrom, D.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.