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Volumn 11, Issue 8, 2004, Pages 714-720

DNA binding and nucleotide flipping by the human DNA repair protein AGT

Author keywords

[No Author keywords available]

Indexed keywords

6 O ALKYLGUANINE DNA ALKYLTRANSFERASE; 6 O ALKYLGUANINE DNA ALKYLTRANSFERASE INHIBITOR; 6 O METHYLGUANINE; ALKYLATING AGENT; BRCA2 PROTEIN; CELL PROTEIN; CYSTEINE; DNA BINDING PROTEIN; DNA REPAIR PROTEIN; GUANINE DERIVATIVE; HELIX LOOP HELIX PROTEIN; METHYLATED DNA PROTEIN CYSTEINE METHYLTRANSFERASE; N1,O6 ETHANOXANTHOSINE; NUCLEOTIDE; PHOSPHATE; RECQ HELICASE; TYROSINE; UNCLASSIFIED DRUG; XANTHOSINE;

EID: 3543029188     PISSN: 15459993     EISSN: None     Source Type: Journal    
DOI: 10.1038/nsmb791     Document Type: Article
Times cited : (270)

References (48)
  • 1
    • 0033520969 scopus 로고    scopus 로고
    • Quality control by DNA repair
    • Lindahl, T. & Wood, R.D. Quality control by DNA repair. Science 286, 1897-1905 (1999).
    • (1999) Science , vol.286 , pp. 1897-1905
    • Lindahl, T.1    Wood, R.D.2
  • 2
    • 0037068446 scopus 로고    scopus 로고
    • Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage
    • Trewick, S.C., Henshaw, T.F., Hausinger, R.P., Lindahl, T. & Sedgwick, B. Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage. Nature 419, 174-178 (2002).
    • (2002) Nature , vol.419 , pp. 174-178
    • Trewick, S.C.1    Henshaw, T.F.2    Hausinger, R.P.3    Lindahl, T.4    Sedgwick, B.5
  • 3
    • 0037068433 scopus 로고    scopus 로고
    • AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli
    • Falnes, P.O., Johansen, R.F. & Seeberg, E. AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli. Nature 419, 178-182 (2002).
    • (2002) Nature , vol.419 , pp. 178-182
    • Falnes, P.O.1    Johansen, R.F.2    Seeberg, E.3
  • 4
    • 0037456369 scopus 로고    scopus 로고
    • Human and bacterial oxidative demethylases repair alkylation damage in both RNA and DNA
    • Aas, P.A. et al. Human and bacterial oxidative demethylases repair alkylation damage in both RNA and DNA, Nature 421, 859-863 (2003).
    • (2003) Nature , vol.421 , pp. 859-863
    • Aas, P.A.1
  • 7
    • 0027351670 scopus 로고
    • Regulation of repair of alkylation damage in mammalian genomes
    • Mitra, S. & Kaina, B. Regulation of repair of alkylation damage in mammalian genomes. Prog. Nucleic Acid Res. Mol. Biol. 44, 109-142 (1993).
    • (1993) Prog. Nucleic Acid Res. Mol. Biol. , vol.44 , pp. 109-142
    • Mitra, S.1    Kaina, B.2
  • 8
    • 0036570062 scopus 로고    scopus 로고
    • Clinical relevance of MGMT in the treatment of cancer
    • Gerson, S.L. Clinical relevance of MGMT in the treatment of cancer. J. Clin. Oncol. 20, 2388-2399 (2002).
    • (2002) J. Clin. Oncol. , vol.20 , pp. 2388-2399
    • Gerson, S.L.1
  • 9
    • 0035477234 scopus 로고    scopus 로고
    • 6-ethanoxanthosine, a mechanism-based crosslinker
    • 6-ethanoxanthosine, a mechanism-based crosslinker. Nucleic Acids Res. 29, 4025-4034 (2001).
    • (2001) Nucleic Acids Res. , vol.29 , pp. 4025-4034
    • Noll, D.M.1    Clarke, N.D.2
  • 11
    • 0034734387 scopus 로고    scopus 로고
    • 6-alkylguanine-DNA alkyltransferase
    • 6-alkylguanine-DNA alkyltransferase. Mutat. Res. 460, 151-163 (2000).
    • (2000) Mutat. Res. , vol.460 , pp. 151-163
    • Daniels, D.S.1    Tainer, J.A.2
  • 12
    • 0034599723 scopus 로고    scopus 로고
    • Active and alkylated human AGT structures: A novel zinc site, inhibitor and extrahelical base binding
    • Daniels, D.S. et al. Active and alkylated human AGT structures: a novel zinc site, inhibitor and extrahelical base binding. EMBO J. 19, 1719-1730 (2000).
    • (2000) EMBO J. , vol.19 , pp. 1719-1730
    • Daniels, D.S.1
  • 13
    • 0032118965 scopus 로고    scopus 로고
    • 6]-methylguanine-DNA methyltransferase binds DNA
    • 6]-methylguanine-DNA methyltransferase binds DNA. Proteins 32, 3-6 (1998).
    • (1998) Proteins , vol.32 , pp. 3-6
    • Vora, R.A.1    Pegg, A.E.2    Ealick, S.E.3
  • 16
    • 0037424237 scopus 로고    scopus 로고
    • 6-alkylguanine-DNA alkyltransferase. Effects of protein and DNA alkylation on complex stability
    • 6-alkylguanine-DNA alkyltransferase. Effects of protein and DNA alkylation on complex stability. J. Biol. Chem. 278, 7973-7980 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 7973-7980
    • Rasimas, J.J.1    Pegg, A.E.2    Fried, M.G.3
  • 18
    • 0034007886 scopus 로고    scopus 로고
    • Overexpression of enzymes that repair endogenous damage to DNA
    • Frosina, G. Overexpression of enzymes that repair endogenous damage to DNA. Eur. J. Biochem. 267, 2135-2149 (2000).
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2135-2149
    • Frosina, G.1
  • 19
    • 0032168569 scopus 로고    scopus 로고
    • Catalytic triads and their relatives
    • Dodson, G. & Wlodawer, A. Catalytic triads and their relatives. Trends Biochem. Sci. 23, 347-352 (1998).
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 347-352
    • Dodson, G.1    Wlodawer, A.2
  • 22
    • 0024292506 scopus 로고
    • 6-methylguanine-DNA methyltransferase from Escherichia coli
    • 6- methylguanine-DNA methyltransferase from Escherichia coli. J. Mol. Biol. 200, 751-752 (1988).
    • (1988) J. Mol. Biol. , vol.200 , pp. 751-752
    • Moody, P.C.1    Demple, B.2
  • 23
    • 0024531901 scopus 로고
    • Facilitated target location in biological systems
    • von Hippel, P.H. & Berg, O.G. Facilitated target location in biological systems. J. Biol. Chem. 264, 675-678 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 675-678
    • Von Hippel, P.H.1    Berg, O.G.2
  • 24
    • 0034387984 scopus 로고    scopus 로고
    • One- and three-dimensional pathways for proteins to reach specific DNA sites
    • Stanford, N.P., Szczelkun, M.D., Marko, J.F. & Halford, S.E. One- and three-dimensional pathways for proteins to reach specific DNA sites. EMBO J. 19, 6546-6557 (2000).
    • (2000) EMBO J. , vol.19 , pp. 6546-6557
    • Stanford, N.P.1    Szczelkun, M.D.2    Marko, J.F.3    Halford, S.E.4
  • 25
    • 0031911656 scopus 로고    scopus 로고
    • 6-methylguanine lesion
    • 6-methylguanine lesion. Mol. Cell. Biol. 18, 1660-1669 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1660-1669
    • Ali, R.B.1
  • 26
    • 0036306053 scopus 로고    scopus 로고
    • Free energy and structural pathways of base flipping in a DNA GCGC containing sequence
    • Banavali, N.K. & MacKerell, A.D. Jr. Free energy and structural pathways of base flipping in a DNA GCGC containing sequence. J. Mol. Biol. 319, 141-160 (2002).
    • (2002) J. Mol. Biol. , vol.319 , pp. 141-160
    • Banavali, N.K.1    MacKerell Jr., A.D.2
  • 27
    • 0037422594 scopus 로고    scopus 로고
    • Protein-facilitated base flipping in DNA by cytosine-5-methyltransferase
    • Huang, N., Banavali, N.K. & MacKerell, A.D. Jr. Protein-facilitated base flipping in DNA by cytosine-5-methyltransferase. Proc. Natl. Acad. Sci. USA 100, 68-73 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 68-73
    • Huang, N.1    Banavali, N.K.2    MacKerell Jr., A.D.3
  • 28
    • 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, 758-766 (2000).
    • (2000) EMBO J. , vol.19 , pp. 758-766
    • Hollis, T.1    Ichikawa, Y.2    Ellenberger, T.3
  • 29
    • 0034708226 scopus 로고    scopus 로고
    • Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA
    • Bruner, S.D., Norman, D.P. & Verdine, G.L. Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Nature 403, 859-866 (2000).
    • (2000) Nature , vol.403 , pp. 859-866
    • Bruner, S.D.1    Norman, D.P.2    Verdine, G.L.3
  • 30
    • 0032498302 scopus 로고    scopus 로고
    • Crystal structure of a G:T/U mismatch-specific DNA glycosylase: Mismatch recognition by complementary-strand interactions
    • Barrett, T.E. et al. Crystal structure of a G:T/U mismatch-specific DNA glycosylase: mismatch recognition by complementary-strand interactions. Cell 92, 117-129 (1998).
    • (1998) Cell , vol.92 , pp. 117-129
    • Barrett, T.E.1
  • 31
    • 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. et al. Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. EMBO J. 17, 5214-5226(1998).
    • (1998) EMBO J. , vol.17 , pp. 5214-5226
    • Parikh, S.S.1
  • 32
    • 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. & Tainer, J.A. DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination [corrected]. Nature 403,451-456(2000).
    • (2000) Nature , vol.403 , pp. 451-456
    • Mol, C.D.1    Izumi, T.2    Mitra, S.3    Tainer, J.A.4
  • 33
    • 0033529716 scopus 로고    scopus 로고
    • Structure of the DNA repair enzyme endonuclease IV and its DNA complex: Double-nucleotide flipping at abasic sites and three-metal-ion catalysis
    • Hosfield, D.J., Guan, Y., Haas, B.J., Cunningham, R.P. & Tainer, J.A. Structure of the DNA repair enzyme endonuclease IV and its DNA complex: double-nucleotide flipping at abasic sites and three-metal-ion catalysis. Cell 98, 397-408 (1999).
    • (1999) Cell , vol.98 , pp. 397-408
    • Hosfield, D.J.1    Guan, Y.2    Haas, B.J.3    Cunningham, R.P.4    Tainer, J.A.5
  • 34
    • 0028010888 scopus 로고
    • Hhal methyltransferase flips its target base out of the DNA helix
    • Klimasauskas, S., Kumar, S., Roberts, R.J. & Cheng, X. Hhal methyltransferase flips its target base out of the DNA helix. Cell 76, 357-369 (1994).
    • (1994) Cell , vol.76 , pp. 357-369
    • Klimasauskas, S.1    Kumar, S.2    Roberts, R.J.3    Cheng, X.4
  • 37
    • 0034708205 scopus 로고    scopus 로고
    • Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding
    • Gajiwala, K.S. et al. Structure of the winged-helix protein hRFX1 reveals a new mode of DNA binding. Nature 403, 916-921 (2000).
    • (2000) Nature , vol.403 , pp. 916-921
    • Gajiwala, K.S.1
  • 38
    • 0033647653 scopus 로고    scopus 로고
    • An overview of the structures of protein-DNA complexes
    • reviews001.1-001.37
    • Luscombe, N.M., Austin, S.E., Berman, H.M. & Thornton, J.M. An overview of the structures of protein-DNA complexes. Genome Biol. 1, reviews001.1-001.37 (2000).
    • (2000) Genome Biol. , vol.1
    • Luscombe, N.M.1    Austin, S.E.2    Berman, H.M.3    Thornton, J.M.4
  • 39
    • 18544372595 scopus 로고    scopus 로고
    • BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure
    • Yang, H. et al. BRCA2 function in DNA binding and recombination from a BRCA2-DSS1-ssDNA structure. Science 297, 1837-1848 (2002).
    • (2002) Science , vol.297 , pp. 1837-1848
    • Yang, H.1
  • 40
    • 0035191378 scopus 로고    scopus 로고
    • Crystal structure of an Xrcc4-DNA ligase IV complex
    • Sibanda, B.L. et al. Crystal structure of an Xrcc4-DNA ligase IV complex. Nat. Struct. Biol. 8, 1015-1019 (2001).
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 1015-1019
    • Sibanda, B.L.1
  • 41
    • 0141865522 scopus 로고    scopus 로고
    • High-resolution structure of the E. coli RecQ helicase catalytic core
    • Bernstein, D.A., Zittel, M.C. & Keck, J.L. High-resolution structure of the E. coli RecQ helicase catalytic core. EMBO J. 22, 4910-4921 (2003).
    • (2003) EMBO J. , vol.22 , pp. 4910-4921
    • Bernstein, D.A.1    Zittel, M.C.2    Keck, J.L.3
  • 43
    • 0028103275 scopus 로고
    • The CCP4 suite, programs for protein crystallography
    • Collaborative Computational Project Number 4. The CCP4 suite, programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 44
    • 1242274650 scopus 로고    scopus 로고
    • Automated protein crystal structure determination using ELVES
    • Holton, J. & Alber, T. Automated protein crystal structure determination using ELVES. Proc. Natl. Acad. Sci. USA 101, 1537-1542 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 1537-1542
    • Holton, J.1    Alber, T.2
  • 45
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza, J. AMoRe: an automated package for molecular replacement. Acta Crystallogr. A. 50, 157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 46
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit - A versatile program for manipulating atomic coordinates and electron density
    • McRee, D.E. XtalView/Xfit-a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125, 156-165 (1999).
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1
  • 47
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A.T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1
  • 48
    • 0024058085 scopus 로고
    • The definition of generalized helicoidal parameters and of axis curvature for irregular nucleic acids
    • Lavery, R. & Sklenar, H. The definition of generalized helicoidal parameters and of axis curvature for irregular nucleic acids. J. Biomol. Struct. Dyn. 6, 63-91 (1988).
    • (1988) J. Biomol. Struct. Dyn. , vol.6 , pp. 63-91
    • Lavery, R.1    Sklenar, H.2


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