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Volumn 460, Issue 3-4, 2000, Pages 201-210

Structural studies of human alkyladenine glycosylase and E. coli 3-methyladenine glycosylase

Author keywords

AAG; AlkA; Base flipping; Glycosidase mechanism; Protein DNA complex

Indexed keywords

GLYCOSYLTRANSFERASE;

EID: 0034734322     PISSN: 09218777     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0921-8777(00)00027-6     Document Type: Article
Times cited : (65)

References (33)
  • 1
    • 0030787013 scopus 로고    scopus 로고
    • What structural features determine repair enzyme specificity and mechanism in chemically modified DNA?
    • Singer B., 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
  • 2
    • 0029133553 scopus 로고
    • Escherichia coli, Saccharomyces cerevisiae, rat and human 3-methyladenine DNA glycosylases repair 1,N6-ethenoadenine when present in DNA
    • Saparbaev M., Kleibl K., Laval J. Escherichia coli, Saccharomyces cerevisiae, rat and human 3-methyladenine DNA glycosylases repair 1,N6-ethenoadenine when present in DNA. Nucleic Acids Res. 23:1995;3750-3755.
    • (1995) Nucleic Acids Res. , vol.23 , pp. 3750-3755
    • Saparbaev, M.1    Kleibl, K.2    Laval, J.3
  • 3
    • 0028239225 scopus 로고
    • Excision of hypoxanthine from DNA containing dIMP residues by the Escherichia coli, yeast, rat, and human alkylpurine DNA glycosylases
    • Saparbaev M., 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
  • 6
    • 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., 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
  • 7
    • 0028010888 scopus 로고
    • HhaI methyltransferase flips its target base out of the DNA helix
    • Klimasauskas S., Kumar S., Roberts R.J., Cheng X. HhaI methyltransferase flips its target base out of the DNA helix. Cell. 76:1994;357-369.
    • (1994) Cell , vol.76 , pp. 357-369
    • Klimasauskas, S.1    Kumar, S.2    Roberts, R.J.3    Cheng, X.4
  • 8
    • 0029068629 scopus 로고
    • The crystal structure of HaeIII methyltransferase convalently complexed to DNA: An extrahelical cytosine and rearranged base pairing
    • Reinisch K.M., Chen L., Verdine G.L., Lipscomb W.N. The crystal structure of HaeIII methyltransferase convalently complexed to DNA: an extrahelical cytosine and rearranged base pairing. Cell. 82:1995;143-153.
    • (1995) Cell , vol.82 , pp. 143-153
    • Reinisch, K.M.1    Chen, L.2    Verdine, G.L.3    Lipscomb, W.N.4
  • 10
    • 0038342180 scopus 로고    scopus 로고
    • Specific binding of a designed pyrrolidine abasic site analog to multiple DNA glycosylases
    • Scharer O.D., Nash H.M., Jiricny J., Laval J., Verdine G.L. Specific binding of a designed pyrrolidine abasic site analog to multiple DNA glycosylases. J. Biol. Chem. 273:1998;8592-8597.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8592-8597
    • Scharer, O.D.1    Nash, H.M.2    Jiricny, J.3    Laval, J.4    Verdine, G.L.5
  • 11
    • 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., 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
  • 12
    • 0029904839 scopus 로고    scopus 로고
    • A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA
    • Slupphaug G., Mol C.D., Kavli B., Arvai A.S., Krokan H.E., Tainer J.A. A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA. Nature. 384:1996;87-92.
    • (1996) Nature , vol.384 , pp. 87-92
    • Slupphaug, G.1    Mol, C.D.2    Kavli, B.3    Arvai, A.S.4    Krokan, H.E.5    Tainer, J.A.6
  • 13
    • 0031149139 scopus 로고    scopus 로고
    • How do DNA repair proteins locate damaged bases in the genome?
    • Verdine G.L., Bruner S.D. How do DNA repair proteins locate damaged bases in the genome? Chem. Biol. 4:1997;329-334.
    • (1997) Chem. Biol. , vol.4 , pp. 329-334
    • Verdine, G.L.1    Bruner, S.D.2
  • 14
    • 0026611472 scopus 로고
    • Release of N2,3-ethenoguanine from chloroacetaldehyde-treated DNA by Escherichia coli 3-methyladenine DNA glycosylase II
    • Matijasevic Z., Sekiguchi M., Ludlum D.B. Release of N2,3-ethenoguanine from chloroacetaldehyde-treated DNA by Escherichia coli 3-methyladenine DNA glycosylase II. Proc. Natl. Acad. Sci. U.S.A. 89:1992;9331-9334.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 9331-9334
    • Matijasevic, Z.1    Sekiguchi, M.2    Ludlum, D.B.3
  • 15
    • 0025720012 scopus 로고
    • Conformation of an enzyme-bound substrate of staphylococcal nuclease as determined by NMR
    • Weber D.J., Mullen G.P., Mildvan A.S. Conformation of an enzyme-bound substrate of staphylococcal nuclease as determined by NMR. Biochemistry. 30:1991;7425-7437.
    • (1991) Biochemistry , vol.30 , pp. 7425-7437
    • Weber, D.J.1    Mullen, G.P.2    Mildvan, A.S.3
  • 17
    • 0034651873 scopus 로고    scopus 로고
    • DNA bending and a flip-out mechanism for base excision by the helix-hairpin-helix DNA glycosylase, Escherichia coli AlkA
    • Hollis T., Ichikawa Y., Ellenberger T. DNA bending and a flip-out mechanism for base excision by the helix-hairpin-helix DNA glycosylase, Escherichia coli AlkA. EMBO J. 19:2000;101-109.
    • (2000) EMBO J. , vol.19 , pp. 101-109
    • Hollis, T.1    Ichikawa, Y.2    Ellenberger, T.3
  • 19
    • 0029836483 scopus 로고    scopus 로고
    • Characterization of the metal ion binding helix-hairpin-helix motifs in human DNA polymerase beta by X-ray structural analysis
    • Pelletier H., Sawaya M.R. Characterization of the metal ion binding helix-hairpin-helix motifs in human DNA polymerase beta by X-ray structural analysis. Biochemistry. 35:1996;12778-12787.
    • (1996) Biochemistry , vol.35 , pp. 12778-12787
    • Pelletier, H.1    Sawaya, M.R.2
  • 20
    • 0033568642 scopus 로고    scopus 로고
    • Crystal structure of an IRF-DNA complex reveals novel DNA recognition and cooperative binding to a tandem repeat of core sequences
    • Fujii Y., Shimizu T., Kusumoto M., Kyogoku Y., Taniguchi T., Hakoshima T. Crystal structure of an IRF-DNA complex reveals novel DNA recognition and cooperative binding to a tandem repeat of core sequences. EMBO J. 18:1999;5028-5041.
    • (1999) EMBO J. , vol.18 , pp. 5028-5041
    • Fujii, Y.1    Shimizu, T.2    Kusumoto, M.3    Kyogoku, Y.4    Taniguchi, T.5    Hakoshima, T.6
  • 21
    • 0032167424 scopus 로고    scopus 로고
    • Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA
    • Parikh S.S., Mol C.D., Slupphaug G., Bharati S., Krokan H.E., Tainer J.A. Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. EMBO J. 17:1998;5214-5226.
    • (1998) EMBO J. , vol.17 , pp. 5214-5226
    • Parikh, S.S.1    Mol, C.D.2    Slupphaug, G.3    Bharati, S.4    Krokan, H.E.5    Tainer, J.A.6
  • 22
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • Thayer M.M., Ahern H., Xing D., Cunningham R.P., Tainer J.A. Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J. 14:1995;4108-4120.
    • (1995) EMBO J. , vol.14 , pp. 4108-4120
    • Thayer, M.M.1    Ahern, H.2    Xing, D.3    Cunningham, R.P.4    Tainer, J.A.5
  • 24
    • 0033594890 scopus 로고    scopus 로고
    • MRNA cap recognition: Dominant role of enhanced stacking interactions between methylated bases and protein aromatic side chains
    • Hu G., Gershon P.D., Hodel A.E., Quiocho F.A. mRNA cap recognition: dominant role of enhanced stacking interactions between methylated bases and protein aromatic side chains. Proc. Natl. Acad. Sci. U.S.A. 96:1999;7149-7154.
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 7149-7154
    • Hu, G.1    Gershon, P.D.2    Hodel, A.E.3    Quiocho, F.A.4
  • 25
    • 0028287938 scopus 로고
    • Transition state analysis and inhibitor design for enzymatic reactions
    • Schramm V.L., Horenstein B.A., Kline P.C. Transition state analysis and inhibitor design for enzymatic reactions. J. Biol. Chem. 269:1994;18259-18262.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18259-18262
    • Schramm, V.L.1    Horenstein, B.A.2    Kline, P.C.3
  • 26
    • 0032487974 scopus 로고    scopus 로고
    • Synthesis of a 2-deoxy-ribose type 1-N-iminosugar
    • Makino K., Ichikawa Y. Synthesis of a 2-deoxy-ribose type 1-N-iminosugar. Tetrahedron Lett. 39:1998;8245-8248.
    • (1998) Tetrahedron Lett. , vol.39 , pp. 8245-8248
    • Makino, K.1    Ichikawa, Y.2
  • 27
    • 0029132769 scopus 로고
    • Studies on the catalytic mechanism of five DNA glycosylases. Probing for enzyme-DNA imino intermediates
    • Sun B., Latham K.A., Dodson M.L., Lloyd R.S. Studies on the catalytic mechanism of five DNA glycosylases. Probing for enzyme-DNA imino intermediates. J. Biol. Chem. 270:1995;19501-19508.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19501-19508
    • Sun, B.1    Latham, K.A.2    Dodson, M.L.3    Lloyd, R.S.4
  • 28
    • 0026658707 scopus 로고
    • Crystal structure of a B-DNA dodecamer containing inosine, d(CGCIAATTCGCG), at 2.4 A resolution and its comparison with other B-DNA dodecamers
    • Xuan J.C., Weber I.T. Crystal structure of a B-DNA dodecamer containing inosine, d(CGCIAATTCGCG), at 2.4 A resolution and its comparison with other B-DNA dodecamers. Nucleic Acids Res. 20:1992;5457-5464.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 5457-5464
    • Xuan, J.C.1    Weber, I.T.2
  • 30
    • 0028675029 scopus 로고
    • The effects of N7-methylguanine on duplex DNA structure
    • Ezaz-Nikpay K., Verdine G.L. The effects of N7-methylguanine on duplex DNA structure. Chem. Biol. 1:1994;235-240.
    • (1994) Chem. Biol. , vol.1 , pp. 235-240
    • Ezaz-Nikpay, K.1    Verdine, G.L.2
  • 31
    • 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., Mosbaugh D.W. Processivity of Escherichia coli and rat liver mitochondrial uracil-DNA glycosylase is affected by NaCl concentration. Biochemistry. 34:1995;6109-6119.
    • (1995) Biochemistry , vol.34 , pp. 6109-6119
    • Bennett, S.E.1    Sanderson, R.J.2    Mosbaugh, D.W.3
  • 32
    • 0027300148 scopus 로고
    • Processivity of uracil DNA glycosylase
    • Higley M., Lloyd R.S. Processivity of uracil DNA glycosylase. Mutat. Res. 294:1993;109-116.
    • (1993) Mutat. Res. , vol.294 , pp. 109-116
    • Higley, M.1    Lloyd, R.S.2
  • 33
    • 0024971541 scopus 로고
    • Modulation of the DNA scanning activity of the Micrococcus luteus UV endonuclease
    • Hamilton R.W., Lloyd R.S. Modulation of the DNA scanning activity of the Micrococcus luteus UV endonuclease. J. Biol. Chem. 264:1989;17422-17427.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17422-17427
    • Hamilton, R.W.1    Lloyd, R.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.