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Volumn 6, Issue 3, 2007, Pages 374-382

Role of active site tyrosines in dynamic aspects of DNA binding by AP endonuclease

Author keywords

AP endonuclease; APE1; Apex; Base excision repair; DNA binding; EMSA; Kinetics; Tyrosine

Indexed keywords

DNA (APURINIC OR APYRIMIDINIC SITE) LYASE; HYDROXYL GROUP; TYROSINE;

EID: 33847258902     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.dnarep.2006.11.004     Document Type: Article
Times cited : (5)

References (52)
  • 1
    • 0029010778 scopus 로고
    • Site-directed mutagenesis of the human DNA repair enzyme HAP1: identification of residues important for AP endonuclease and RNase H activity
    • Barzilay G., Walker L.J., Robson C.N., and Hickson I.D. Site-directed mutagenesis of the human DNA repair enzyme HAP1: identification of residues important for AP endonuclease and RNase H activity. Nucleic Acids Res. 23 (1995) 1544
    • (1995) Nucleic Acids Res. , vol.23 , pp. 1544
    • Barzilay, G.1    Walker, L.J.2    Robson, C.N.3    Hickson, I.D.4
  • 2
    • 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., et al. 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 (2004) 5134
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5134
    • Beloglazova, N.G.1    Kirpota, O.O.2    Starostin, K.V.3    Ishchenko, A.A.4    Yamkovoy, V.I.5
  • 3
    • 0029079249 scopus 로고
    • Processivity of Escherichia coli and rat liver mitochondrial uracil-DNA glycosylase is affected by NaCl concentration
    • Bennett S.E., Sanderson R.J., and Mosbaugh D.W. Processivity of Escherichia coli and rat liver mitochondrial uracil-DNA glycosylase is affected by NaCl concentration. Biochemistry 34 (1995) 6109
    • (1995) Biochemistry , vol.34 , pp. 6109
    • Bennett, S.E.1    Sanderson, R.J.2    Mosbaugh, D.W.3
  • 4
    • 0017174203 scopus 로고
    • Purification and characterization of human endonucleases specific for damaged DNA. Analysis of lesions induced by ultraviolet or X-radiation
    • Brent T.P. Purification and characterization of human endonucleases specific for damaged DNA. Analysis of lesions induced by ultraviolet or X-radiation. Biochim. Biophys. Acta 454 (1976) 172
    • (1976) Biochim. Biophys. Acta , vol.454 , pp. 172
    • Brent, T.P.1
  • 5
    • 0033554862 scopus 로고    scopus 로고
    • Human apurinic/apyrimidinic endonuclease is processive
    • Carey D.C., and Strauss P.R. Human apurinic/apyrimidinic endonuclease is processive. Biochemistry 38 (1999) 16553
    • (1999) Biochemistry , vol.38 , pp. 16553
    • Carey, D.C.1    Strauss, P.R.2
  • 6
    • 0030917436 scopus 로고    scopus 로고
    • Reactivity of human apurinic/apyrimidinic endonuclease and Escherichia coli exonuclease III with bistranded abasic sites in DNA
    • Chaudhry M.A., and Weinfeld M. Reactivity of human apurinic/apyrimidinic endonuclease and Escherichia coli exonuclease III with bistranded abasic sites in DNA. J. Biol. Chem. 272 (1997) 15650
    • (1997) J. Biol. Chem. , vol.272 , pp. 15650
    • Chaudhry, M.A.1    Weinfeld, M.2
  • 7
    • 0001473891 scopus 로고    scopus 로고
    • Chemistry of glycosylases and endonucleases involved in base-excision repair
    • David S.S., and Williams S.D. Chemistry of glycosylases and endonucleases involved in base-excision repair. Chem. Rev. 98 (1998) 1221
    • (1998) Chem. Rev. , vol.98 , pp. 1221
    • David, S.S.1    Williams, S.D.2
  • 8
    • 0028342951 scopus 로고
    • Repair of oxidative damage to DNA: enzymology and biology
    • Demple B., and Harrison L. Repair of oxidative damage to DNA: enzymology and biology. Annu. Rev. Biochem. 63 (1994) 915
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 915
    • Demple, B.1    Harrison, L.2
  • 9
    • 0026323008 scopus 로고
    • Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes
    • Demple B., Herman T., and Chen D.S. Cloning and expression of APE, the cDNA encoding the major human apurinic endonuclease: definition of a family of DNA repair enzymes. Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 11450
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 11450
    • Demple, B.1    Herman, T.2    Chen, D.S.3
  • 10
    • 0025120572 scopus 로고
    • The enzymology of apurinic/apyrimidinic endonucleases
    • Doetsch P.W., and Cunningham R.P. The enzymology of apurinic/apyrimidinic endonucleases. Mutat. Res. 236 (1990) 173
    • (1990) Mutat. Res. , vol.236 , pp. 173
    • Doetsch, P.W.1    Cunningham, R.P.2
  • 11
    • 84961981834 scopus 로고    scopus 로고
    • Elements in abasic site recognition by the major human and Escherichia coli apurinic/apyrimidinic endonucleases
    • Erzberger J.P., Barsky D., Scharer O.D., Colvin M.E., and Wilson III D.M. Elements in abasic site recognition by the major human and Escherichia coli apurinic/apyrimidinic endonucleases. Nucleic Acids Res. 26 (1998) 2771
    • (1998) Nucleic Acids Res. , vol.26 , pp. 2771
    • Erzberger, J.P.1    Barsky, D.2    Scharer, O.D.3    Colvin, M.E.4    Wilson III, D.M.5
  • 14
    • 0034733652 scopus 로고    scopus 로고
    • A carboxylate triad is essential for the polymerase activity of Escherichia coli DNA polymerase I (Klenow fragment). Presence of two functional triads at the catalytic center
    • Gangurde R., Kaushik N., Singh K., and Modak M.J. A carboxylate triad is essential for the polymerase activity of Escherichia coli DNA polymerase I (Klenow fragment). Presence of two functional triads at the catalytic center. J. Biol. Chem. 275 (2000) 19685
    • (2000) J. Biol. Chem. , vol.275 , pp. 19685
    • Gangurde, R.1    Kaushik, N.2    Singh, K.3    Modak, M.J.4
  • 15
    • 0019877067 scopus 로고
    • A gel electrophoresis method for quantifying the binding of proteins to specific DNA regions: application to components of the Escherichia coli lactose operon regulatory system
    • Garner M.M., and Revzin A. A gel electrophoresis method for quantifying the binding of proteins to specific DNA regions: application to components of the Escherichia coli lactose operon regulatory system. Nucleic Acids Res. 9 (1981) 3047
    • (1981) Nucleic Acids Res. , vol.9 , pp. 3047
    • Garner, M.M.1    Revzin, A.2
  • 16
    • 0017047039 scopus 로고
    • An analysis on the slope of Scatchard plots
    • Henis Y.I., and Levitzki A. An analysis on the slope of Scatchard plots. Eur. J. Biochem. 71 (1976) 529
    • (1976) Eur. J. Biochem. , vol.71 , pp. 529
    • Henis, Y.I.1    Levitzki, A.2
  • 17
    • 0030478864 scopus 로고    scopus 로고
    • Negative regulation of the major human AP-endonuclease, a multifunctional protein
    • Izumi T., Henner W.D., and Mitra S. Negative regulation of the major human AP-endonuclease, a multifunctional protein. Biochemistry 35 (1996) 14679
    • (1996) Biochemistry , vol.35 , pp. 14679
    • Izumi, T.1    Henner, W.D.2    Mitra, S.3
  • 18
    • 0033557226 scopus 로고    scopus 로고
    • DNA binding specificity and transactivation properties of SREBP-2 bound to multiple sites on the human apoA-II promoter
    • Kan H.Y., Pissios P., Chambaz J., and Zannis V.I. DNA binding specificity and transactivation properties of SREBP-2 bound to multiple sites on the human apoA-II promoter. Nucleic Acids Res. 27 (1999) 1104
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1104
    • Kan, H.Y.1    Pissios, P.2    Chambaz, J.3    Zannis, V.I.4
  • 19
    • 0019876798 scopus 로고
    • Purification and characterization of an apurinic/apyrimidinic endonuclease from HeLa cells
    • Kane C.M., and Linn S. Purification and characterization of an apurinic/apyrimidinic endonuclease from HeLa cells. J. Biol. Chem. 256 (1981) 3405
    • (1981) J. Biol. Chem. , vol.256 , pp. 3405
    • Kane, C.M.1    Linn, S.2
  • 20
    • 0018462339 scopus 로고
    • Protein affinities for small molecules: conceptions and misconceptions
    • Klotz I.M., and Hunston D.L. Protein affinities for small molecules: conceptions and misconceptions. Arch. Biochem. Biophys. 193 (1979) 314
    • (1979) Arch. Biochem. Biophys. , vol.193 , pp. 314
    • Klotz, I.M.1    Hunston, D.L.2
  • 22
    • 0043000837 scopus 로고
    • An altered apurinic DNA endonuclease activity in group A and group D xeroderma pigmentosum fibroblasts
    • Kuhnlein U., Penhoet E.E., and Linn S. An altered apurinic DNA endonuclease activity in group A and group D xeroderma pigmentosum fibroblasts. Proc. Natl. Acad. Sci. U.S.A. 73 (1976) 1169
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 1169
    • Kuhnlein, U.1    Penhoet, E.E.2    Linn, S.3
  • 23
    • 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
    • (1993) Nature , vol.362 , pp. 709
    • Lindahl, T.1
  • 26
    • 0017342847 scopus 로고
    • Human endonuclease specific for apurinic/apyrimidinic sites in DNA. Partial purification and characterization of multiple forms from placenta
    • Linsley W.S., Penhoet E.E., and Linn S. Human endonuclease specific for apurinic/apyrimidinic sites in DNA. Partial purification and characterization of multiple forms from placenta. J. Biol. Chem. 252 (1977) 1235
    • (1977) J. Biol. Chem. , vol.252 , pp. 1235
    • Linsley, W.S.1    Penhoet, E.E.2    Linn, S.3
  • 27
    • 0033586728 scopus 로고    scopus 로고
    • Single-turnover analysis of mutant human apurinic/apyrimidinic endonuclease
    • Lucas J.A., Masuda Y., Bennett R.A., Strauss N.S., and Strauss P.R. Single-turnover analysis of mutant human apurinic/apyrimidinic endonuclease. Biochemistry 38 (1999) 4958
    • (1999) Biochemistry , vol.38 , pp. 4958
    • Lucas, J.A.1    Masuda, Y.2    Bennett, R.A.3    Strauss, N.S.4    Strauss, P.R.5
  • 28
    • 0032515143 scopus 로고    scopus 로고
    • Dynamics of the interaction of human apurinic endonuclease (Ape1) with its substrate and product
    • Masuda Y., Bennett R.A., and Demple B. Dynamics of the interaction of human apurinic endonuclease (Ape1) with its substrate and product. J. Biol. Chem. 273 (1998) 30352
    • (1998) J. Biol. Chem. , vol.273 , pp. 30352
    • Masuda, Y.1    Bennett, R.A.2    Demple, B.3
  • 29
    • 0032515067 scopus 로고    scopus 로고
    • Rapid dissociation of human apurinic endonuclease (Ape1) from incised DNA induced by magnesium
    • Masuda Y., Bennett R.A., and Demple B. Rapid dissociation of human apurinic endonuclease (Ape1) from incised DNA induced by magnesium. J. Biol. Chem. 273 (1998) 30360
    • (1998) J. Biol. Chem. , vol.273 , pp. 30360
    • Masuda, Y.1    Bennett, R.A.2    Demple, B.3
  • 30
    • 0032836651 scopus 로고    scopus 로고
    • Initiation of base excision repair: glycosylase mechanisms and structures
    • McCullough A.K., Dodson M.L., and Lloyd R.S. Initiation of base excision repair: glycosylase mechanisms and structures. Annu. Rev. Biochem. 68 (1999) 255
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 255
    • McCullough, A.K.1    Dodson, M.L.2    Lloyd, R.S.3
  • 32
    • 0035818408 scopus 로고    scopus 로고
    • Oligonucleotides with bistranded abasic sites interfere with substrate binding and catalysis by human apurinic/apyrimidinic endonuclease
    • McKenzie J.A., and Strauss P.R. Oligonucleotides with bistranded abasic sites interfere with substrate binding and catalysis by human apurinic/apyrimidinic endonuclease. Biochemistry 40 (2001) 13254
    • (2001) Biochemistry , vol.40 , pp. 13254
    • McKenzie, J.A.1    Strauss, P.R.2
  • 33
    • 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. DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination [corrected]. Nature 403 (2000) 451
    • (2000) Nature , vol.403 , pp. 451
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 34
    • 0019289003 scopus 로고
    • Further characterization of human fibroblast apurinic/apyrimidinic DNA endonucleases. The definition of two mechanistic classes of enzyme
    • Mosbaugh D.W., and Linn S. Further characterization of human fibroblast apurinic/apyrimidinic DNA endonucleases. The definition of two mechanistic classes of enzyme. J. Biol. Chem. 255 (1980) 11743
    • (1980) J. Biol. Chem. , vol.255 , pp. 11743
    • Mosbaugh, D.W.1    Linn, S.2
  • 36
    • 0033152195 scopus 로고    scopus 로고
    • Endogenous apurinic/apyrimidinic sites in genomic DNA of mammalian tissues
    • Nakamura J., and Swenberg J.A. Endogenous apurinic/apyrimidinic sites in genomic DNA of mammalian tissues. Cancer Res 59 (1999) 2522
    • (1999) Cancer Res , vol.59 , pp. 2522
    • Nakamura, J.1    Swenberg, J.A.2
  • 37
    • 0023034951 scopus 로고
    • Differences in the kinetic properties of BamHI endonuclease and methylase with linear DNA substrates
    • Nardone G., George J., and Chirikjian J.G. Differences in the kinetic properties of BamHI endonuclease and methylase with linear DNA substrates. J. Biol. Chem. 261 (1986) 12128
    • (1986) J. Biol. Chem. , vol.261 , pp. 12128
    • Nardone, G.1    George, J.2    Chirikjian, J.G.3
  • 38
    • 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 III D.M. Mapping the protein-DNA interface and the metal-binding site of the major human apurinic/apyrimidinic endonuclease. J. Mol. Biol. 298 (2000) 447
    • (2000) J. Mol. Biol. , vol.298 , pp. 447
    • Nguyen, L.H.1    Barsky, D.2    Erzberger, J.P.3    Wilson III, D.M.4
  • 39
    • 0025187297 scopus 로고
    • A sensitive method for the determination of protein-DNA binding specificities
    • Pollock R., and Treisman R. A sensitive method for the determination of protein-DNA binding specificities. Nucleic Acids Res. 18 (1990) 6197
    • (1990) Nucleic Acids Res. , vol.18 , pp. 6197
    • Pollock, R.1    Treisman, R.2
  • 40
    • 0025936119 scopus 로고
    • Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants
    • Robson C.N., and Hickson I.D. Isolation of cDNA clones encoding a human apurinic/apyrimidinic endonuclease that corrects DNA repair and mutagenesis defects in E. coli xth (exonuclease III) mutants. Nucleic Acids Res. 19 (1991) 5519
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5519
    • Robson, C.N.1    Hickson, I.D.2
  • 41
    • 0004136246 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New Yok
    • Sambrook Ja.R., and David W. Molecular Cloning (2001), Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New Yok
    • (2001) Molecular Cloning
    • Sambrook, Ja.R.1    David, W.2
  • 42
    • 0026683715 scopus 로고
    • cDNA cloning, sequencing, expression and possible domain structure of human APEX nuclease homologous to Escherichia coli exonuclease III
    • Seki S., Hatsushika M., Watanabe S., Akiyama K., Nagao K., and Tsutsui K. cDNA cloning, sequencing, expression and possible domain structure of human APEX nuclease homologous to Escherichia coli exonuclease III. Biochim. Biophys. Acta 1131 (1992) 287
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 287
    • Seki, S.1    Hatsushika, M.2    Watanabe, S.3    Akiyama, K.4    Nagao, K.5    Tsutsui, K.6
  • 43
    • 0031021533 scopus 로고    scopus 로고
    • Substrate binding by human apurinic/apyrimidinic endonuclease indicates a Briggs-Haldane mechanism
    • Strauss P.R., Beard W.A., Patterson T.A., and Wilson S.H. Substrate binding by human apurinic/apyrimidinic endonuclease indicates a Briggs-Haldane mechanism. J. Biol. Chem. 272 (1997) 1302
    • (1997) J. Biol. Chem. , vol.272 , pp. 1302
    • Strauss, P.R.1    Beard, W.A.2    Patterson, T.A.3    Wilson, S.H.4
  • 45
    • 0022381905 scopus 로고
    • Facilitated diffusion during catalysis by EcoRI endonuclease. Nonspecific interactions in EcoRI catalysis
    • Terry B.J., Jack W.E., and Modrich P. Facilitated diffusion during catalysis by EcoRI endonuclease. Nonspecific interactions in EcoRI catalysis. J. Biol. Chem. 260 (1985) 13130
    • (1985) J. Biol. Chem. , vol.260 , pp. 13130
    • Terry, B.J.1    Jack, W.E.2    Modrich, P.3
  • 46
    • 0026703932 scopus 로고
    • Extension of the DNA binding consensus of the chicken c-Myb and v-Myb proteins
    • Weston K. Extension of the DNA binding consensus of the chicken c-Myb and v-Myb proteins. Nucleic Acids Res. 20 (1992) 3043
    • (1992) Nucleic Acids Res. , vol.20 , pp. 3043
    • Weston, K.1
  • 47
    • 0030839750 scopus 로고    scopus 로고
    • Abasic site binding by the human apurinic endonuclease, Ape, and determination of the DNA contact sites
    • Wilson III D.M., Takeshita M., and Demple B. Abasic site binding by the human apurinic endonuclease, Ape, and determination of the DNA contact sites. Nucleic Acids Res. 25 (1997) 933
    • (1997) Nucleic Acids Res. , vol.25 , pp. 933
    • Wilson III, D.M.1    Takeshita, M.2    Demple, B.3
  • 48
    • 0037870269 scopus 로고    scopus 로고
    • Stabilization of eukaryotic topoisomerase II-DNA cleavage complexes
    • Wilstermann A.M., and Osheroff N. Stabilization of eukaryotic topoisomerase II-DNA cleavage complexes. Curr. Top. Med. Chem. 3 (2003) 321
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 321
    • Wilstermann, A.M.1    Osheroff, N.2
  • 49
    • 0026583944 scopus 로고
    • Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity
    • Xanthoudakis S., and Curran T. Identification and characterization of Ref-1, a nuclear protein that facilitates AP-1 DNA-binding activity. Embo J. 11 (1992) 653
    • (1992) Embo J. , vol.11 , pp. 653
    • Xanthoudakis, S.1    Curran, T.2
  • 50
    • 0026714672 scopus 로고
    • Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme
    • Xanthoudakis S., Miao G., Wang F., Pan Y.C., and Curran T. Redox activation of Fos-Jun DNA binding activity is mediated by a DNA repair enzyme. Embo J. 11 (1992) 3323
    • (1992) Embo J. , vol.11 , pp. 3323
    • Xanthoudakis, S.1    Miao, G.2    Wang, F.3    Pan, Y.C.4    Curran, T.5
  • 51
    • 0016651743 scopus 로고
    • Mutations simultaneously affecting endonuclease II and exonuclease III in Escherichia coli
    • Yajko D.M., and Weiss B. Mutations simultaneously affecting endonuclease II and exonuclease III in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 72 (1975) 688
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 688
    • Yajko, D.M.1    Weiss, B.2


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