메뉴 건너뛰기




Volumn 51, Issue 1, 2012, Pages 382-390

Searching for DNA lesions: Structural evidence for lower- and higher-affinity DNA binding conformations of human alkyladenine DNA glycosylase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE RESIDUES; DISORDERED STATE; DNA ADDUCTS; DNA BASIS; DNA BINDING; DNA GLYCOSYLASE; DNA LESIONS; ELECTROSTATIC SURFACES; STRUCTURAL EVIDENCE;

EID: 84856812291     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi201484k     Document Type: Article
Times cited : (24)

References (39)
  • 1
    • 0027278557 scopus 로고
    • Instability and decay of the primary structure of DNA
    • DOI 10.1038/362709a0
    • Lindahl, T. (1993) Instability and decay of the primary structure of DNA. Nature 362, 709-715. (Pubitemid 23125973)
    • (1993) Nature , vol.362 , Issue.6422 , pp. 709-715
    • Lindahl, T.1
  • 3
    • 0001473891 scopus 로고    scopus 로고
    • Chemistry of glycosylases and endonucleases involved in base-excision repair
    • David, S. S., and Williams, S. D. (1998) Chemistry of Glycosylases and Endonucleases Involved in Base-Excision Repair. Chem. Rev. 98, 1221-1262.
    • (1998) Chem. Rev. , vol.98 , pp. 1221-1262
    • David, S.S.1    Williams, S.D.2
  • 4
    • 0029842307 scopus 로고    scopus 로고
    • Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase β and the XRCC1 protein
    • Kubota, Y., Nash, R. A., Klungland, A., Schär, P., Barnes, D. E., and Lindahl, T. (1996) Reconstitution of DNA base excision-repair with purified human proteins: Interaction between DNA polymerase ß and the XRCC1 protein. EMBO J. 15, 6662-6670. (Pubitemid 26413798)
    • (1996) EMBO Journal , vol.15 , Issue.23 , pp. 6662-6670
    • Kubota, Y.1    Nash, R.A.2    Klungland, A.3    Schar, P.4    Barnes, D.E.5    Lindahl, T.6
  • 6
    • 1642411206 scopus 로고    scopus 로고
    • Dissecting the Broad Substrate Specificity of Human 3-Methyladenine-DNA Glycosylase
    • DOI 10.1074/jbc.M312232200
    • 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. (Pubitemid 38379541)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.11 , pp. 9750-9757
    • O'Brien, P.J.1    Ellenberger, T.2
  • 7
    • 74049108712 scopus 로고    scopus 로고
    • Chemical biology of mutagenesis and DNA repair: Cellular responses to DNA alkylation
    • Shrivastav, N., Li, D., and Essigmann, J. M. (2010) Chemical biology of mutagenesis and DNA repair: Cellular responses to DNA alkylation. Carcinogenesis 31, 59-70.
    • (2010) Carcinogenesis , vol.31 , pp. 59-70
    • Shrivastav, N.1    Li, D.2    Essigmann, J.M.3
  • 8
    • 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. (2000) Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG. Proc. Natl. Acad. Sci. U.S.A. 97, 13573-13578.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13573-13578
    • Lau, A.Y.1    Wyatt, M.D.2    Glassner, B.J.3    Samson, L.D.4    Ellenberger, T.5
  • 9
    • 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
  • 10
    • 73149092550 scopus 로고    scopus 로고
    • Kinetic mechanism for the flipping and excision of 1,N6-ethenoadenine by human alkyladenine DNA glycosylase
    • Wolfe, A. E., and O'Brien, P. J. (2009) Kinetic mechanism for the flipping and excision of 1,N6-ethenoadenine by human alkyladenine DNA glycosylase. Biochemistry 48, 11357-11369.
    • (2009) Biochemistry , vol.48 , pp. 11357-11369
    • Wolfe, A.E.1    O'Brien, P.J.2
  • 11
    • 0142126715 scopus 로고    scopus 로고
    • Human alkyladenine DNA glycosylase uses acid-base catalysis for selective excision of damaged purines
    • DOI 10.1021/bi035177v
    • 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. (Pubitemid 37296518)
    • (2003) Biochemistry , vol.42 , Issue.42 , pp. 12418-12429
    • O'Brien, P.J.1    Ellenberger, T.2
  • 13
    • 77949543799 scopus 로고    scopus 로고
    • Frameshift mutagenesis and microsatellite instability induced by human alkyladenine DNA glycosylase
    • Klapacz, J., Lingaraju, G. M., Guo, H. H., Shah, D., Moar-Shoshani, A., Loeb, L. A., and Samson, L. D. (2010) Frameshift mutagenesis and microsatellite instability induced by human alkyladenine DNA glycosylase. Mol. Cell 37, 843-853.
    • (2010) Mol. Cell , vol.37 , pp. 843-853
    • Klapacz, J.1    Lingaraju, G.M.2    Guo, H.H.3    Shah, D.4    Moar-Shoshani, A.5    Loeb, L.A.6    Samson, L.D.7
  • 14
    • 0032573432 scopus 로고    scopus 로고
    • Heterogeneous repair of N-methylpurines at the nucleotide level in normal human cells
    • DOI 10.1006/jmbi.1998.2138
    • Ye, N., Holmquist, G. P., and O'Connor, T. R. (1998) Heterogeneous repair of N-methylpurines at the nucleotide level in normal human cells. J. Mol. Biol. 284, 269-285. (Pubitemid 28542453)
    • (1998) Journal of Molecular Biology , vol.284 , Issue.2 , pp. 269-285
    • Ye, N.1    Holmquist, G.P.2    O'Connor, T.R.3
  • 15
    • 0019887628 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids 1. Models and theory
    • Berg, O. G., Winter, R. B., and von Hippel, P. H. (1981) Diffusion-driven mechanisms of protein translocation on nucleic acids. 1. Models and theory. Biochemistry 20, 6929-6948.
    • (1981) Biochemistry , vol.20 , pp. 6929-6948
    • Berg, O.G.1    Winter, R.B.2    Von Hippel, P.H.3
  • 16
    • 0018472170 scopus 로고
    • The one-dimensional diffusion coefficient of proteins absorbed on DNA. Hydrodynamic considerations
    • Schurr, J. M. (1979) The one-dimensional diffusion coefficient of proteins absorbed on DNA. Hydrodynamic considerations. Biophys. Chem. 9, 413-414.
    • (1979) Biophys. Chem. , vol.9 , pp. 413-414
    • Schurr, J.M.1
  • 19
    • 33645807371 scopus 로고    scopus 로고
    • A base-excision DNA-repair protein finds intrahelical lesion bases by fast sliding in contact with DNA
    • Blainey, P. C., van Oijen, A. M., Banerjee, A., Verdine, G. L., and Xie, X. S. (2006) A base-excision DNA-repair protein finds intrahelical lesion bases by fast sliding in contact with DNA. Proc. Natl. Acad. Sci. U.S.A. 103, 5752-5757.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 5752-5757
    • Blainey, P.C.1    Van Oijen, A.M.2    Banerjee, A.3    Verdine, G.L.4    Xie, X.S.5
  • 20
    • 77951113170 scopus 로고    scopus 로고
    • Hopping Enables a DNA Repair Glycosylase to Search Both Strands and Bypass a Bound Protein
    • Hedglin, M., and O'Brien, P. J. (2010) Hopping Enables a DNA Repair Glycosylase To Search Both Strands and Bypass a Bound Protein. ACS Chem. Biol. 5, 427-436.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 427-436
    • Hedglin, M.1    O'Brien, P.J.2
  • 21
    • 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
  • 22
    • 78149245429 scopus 로고    scopus 로고
    • Structure of Escherichia coli AlkA in complex with undamaged DNA
    • Bowman, B. R., Lee, S., Wang, S., and Verdine, G. L. (2010) Structure of Escherichia coli AlkA in complex with undamaged DNA. J. Biol. Chem. 285, 35783-35791.
    • (2010) J. Biol. Chem. , vol.285 , pp. 35783-35791
    • Bowman, B.R.1    Lee, S.2    Wang, S.3    Verdine, G.L.4
  • 23
    • 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., and Ellenberger, T. (2000) DNA bending and a flip-out mechanism for base excision by the helixhairpin-helix DNA glycosylase, Escherichia coli AlkA. EMBO J. 19, 758-766. (Pubitemid 30093749)
    • (2000) EMBO Journal , vol.19 , Issue.4 , pp. 758-766
    • Hollis, T.1    Ichikawa, Y.2    Ellenberger, T.3
  • 24
    • 0034708226 scopus 로고    scopus 로고
    • Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA
    • DOI 10.1038/35002510
    • Bruner, S. D., Norman, D. P., and Verdine, G. L. (2000) Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Nature 403, 859-866. (Pubitemid 30130980)
    • (2000) Nature , vol.403 , Issue.6772 , pp. 859-866
    • Bruner, S.D.1    Norman, D.P.G.2    Verdine, G.L.3
  • 25
    • 77953654163 scopus 로고    scopus 로고
    • Detection of damaged DNA bases by DNA glycosylase enzymes
    • Friedman, J. I., and Stivers, J. T. (2010) Detection of Damaged DNA Bases by DNA Glycosylase Enzymes. Biochemistry 49, 4957-4967.
    • (2010) Biochemistry , vol.49 , pp. 4957-4967
    • Friedman, J.I.1    Stivers, J.T.2
  • 26
    • 0032538337 scopus 로고    scopus 로고
    • Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: Mechanisms for nucleotide flipping and base excision
    • DOI 10.1016/S0092-8674(00)81755-9
    • Lau, A. Y., Scharer, D., Samson, L. D., 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. (Pubitemid 28473785)
    • (1998) Cell , vol.95 , Issue.2 , pp. 249-258
    • Lau, A.Y.1    Scharer, O.D.2    Samson, L.3    Verdine, G.L.4    Ellenberger, T.5
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326. (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 31
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 35
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R., MacArthur, M., and Moss, D. (1993) PROCHECK: A program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.1    MacArthur, M.2    Moss, D.3
  • 38
    • 79952812338 scopus 로고    scopus 로고
    • Substitution of active site tyrosines with tryptophan alters the free energy for nucleotide flipping by human alkyladenine DNA glycosylase
    • Hendershot, J. M., Wolfe, A. E., and O'Brien, P. J. (2011) Substitution of Active Site Tyrosines with Tryptophan Alters the Free Energy for Nucleotide Flipping by Human Alkyladenine DNA Glycosylase. Biochemistry 50, 1864-1874.
    • (2011) Biochemistry , vol.50 , pp. 1864-1874
    • Hendershot, J.M.1    Wolfe, A.E.2    O'Brien, P.J.3
  • 39
    • 33644511436 scopus 로고    scopus 로고
    • Structure of a DNA glycosylase searching for lesions
    • Banerjee, A., Santos, W. L., and Verdine, G. L. (2006) Structure of a DNA glycosylase searching for lesions. Science 311, 1153-1157.
    • (2006) Science , vol.311 , pp. 1153-1157
    • Banerjee, A.1    Santos, W.L.2    Verdine, G.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.