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Volumn 109, Issue 6, 2012, Pages

DNA charge transport as a first step in coordinating the detection of lesions by repair proteins

Author keywords

DNA electron transfer; Iron sulfur clusters; Oxidative damage

Indexed keywords

DEOXYRIBONUCLEOPROTEIN; ENDONUCLEASE; GLYCOSYLATED ALBUMIN; HELICASE;

EID: 84857127226     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1120063109     Document Type: Article
Times cited : (97)

References (56)
  • 2
    • 3943107573 scopus 로고    scopus 로고
    • Molecular mechanisms of mammalian DNA repair and the DNA damage checkpoints
    • DOI 10.1146/annurev.biochem.73.011303.073723
    • Sancar A, Lindsey-Boltz A, Ünsal-Kaçmaz K, Linn S (2004) Molecular mechanisms of mammalian dna repair and the DNA damage checkpoints. Annu Rev Biochem 73:39-85. (Pubitemid 39050363)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 39-85
    • Sancar, A.1    Lindsey-Boltz, L.A.2    Unsal-Kacmaz, K.3    Linn, S.4
  • 3
    • 0001473891 scopus 로고    scopus 로고
    • Chemistry of glycosylases and endonucleases involved in base-excision repair
    • David SS, Williams SD (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
    • 34250900982 scopus 로고    scopus 로고
    • Base-excision repair of oxidative DNA damage
    • DOI 10.1038/nature05978, PII NATURE05978
    • David SS, O'Shea VL, Kundu S (2007) Base-excision repair of oxidative DNA damage. Nature 447:941-950. (Pubitemid 46975761)
    • (2007) Nature , vol.447 , Issue.7147 , pp. 941-950
    • David, S.S.1    O'Shea, V.L.2    Kundu, S.3
  • 6
    • 0033079847 scopus 로고    scopus 로고
    • Long-range oxidative damage to DNA: Effects of distance and sequence
    • DOI 10.1016/S1074-5521(99)80005-2
    • Nunez ME, Hall DB, Barton JK (1999) Long range oxidative damage to DNA: effects of distance and sequence. Chem Biol 6:85-97. (Pubitemid 29363159)
    • (1999) Chemistry and Biology , vol.6 , Issue.2 , pp. 85-97
    • Nunez, M.E.1    Hall, D.B.2    Barton, J.K.3
  • 8
    • 15244353024 scopus 로고    scopus 로고
    • Electrochemical detection of lesions in DNA
    • DOI 10.1021/bc0497362
    • Boal AK, Barton JK (2005) Electrochemical detection of lesions in DNA. Bioconjugate Chem 16:312-321. (Pubitemid 40388206)
    • (2005) Bioconjugate Chemistry , vol.16 , Issue.2 , pp. 312-321
    • Boal, A.K.1    Barton, J.K.2
  • 9
    • 76149146090 scopus 로고    scopus 로고
    • DNA-mediated charge transport in redox sensing and signaling
    • Genereux JC, Boal AK, Barton JK (2010) DNA-mediated charge transport in redox sensing and signaling. J Am Chem Soc 132:891-905.
    • (2010) J Am Chem Soc , vol.132 , pp. 891-905
    • Genereux, J.C.1    Boal, A.K.2    Barton, J.K.3
  • 11
    • 79952104649 scopus 로고    scopus 로고
    • Metal complexes for DNA-mediated charge transport
    • Barton JK, Olmon ED, Sontz PA (2011) Metal complexes for DNA-mediated charge transport. Coord Chem Rev 255:619-634.
    • (2011) Coord Chem Rev , vol.255 , pp. 619-634
    • Barton, J.K.1    Olmon, E.D.2    Sontz, P.A.3
  • 12
    • 0026499118 scopus 로고
    • Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III
    • Kuo CF, et al. (1992) Atomic structure of the DNA repair [4Fe-4S] enzyme endonuclease III. Science 258:434-440.
    • (1992) Science , vol.258 , pp. 434-440
    • Kuo, C.F.1
  • 13
    • 0029119097 scopus 로고
    • Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure
    • Thayer MM, Ahern H, Xing D, Cunningham RP, Tainer JA (1995) Novel DNA binding motifs in the DNA repair enzyme endonuclease III crystal structure. EMBO J 14:4108-4120.
    • (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
  • 14
    • 33748790129 scopus 로고    scopus 로고
    • Direct electrochemistry of endonuclease III in the presence and absence of DNA
    • DOI 10.1021/ja064784d
    • Gorodetsky AA, Boal AK, Barton JK (2006) Direct electrochemistry of endonuclease III in the presence and absence of DNA. J Am Chem Soc 128:12082-12083. (Pubitemid 44413836)
    • (2006) Journal of the American Chemical Society , vol.128 , Issue.37 , pp. 12082-12083
    • Gorodetsky, A.A.1    Boal, A.K.2    Barton, J.K.3
  • 16
    • 16344377473 scopus 로고    scopus 로고
    • A role for iron-sulfur clusters in DNA repair
    • DOI 10.1016/j.cbpa.2005.02.006, Bioorganic Chemistry / Biocatalysis and Biotransformation
    • Lukianova OA, David SS (2005) A role for iron-sulfur clusters in DNA repair. Curr Opin Chem Biol 9:145-151. (Pubitemid 40467576)
    • (2005) Current Opinion in Chemical Biology , vol.9 , Issue.2 , pp. 145-151
    • Lukianova, O.A.1    David, S.S.2
  • 17
    • 0037925462 scopus 로고    scopus 로고
    • Structure of a trapped endonuclease III-DNA covalent intermediate
    • DOI 10.1093/emboj/cdg311
    • Fromme JC, Verdine GL (2003) Structure of a trapped endonuclease III- DNA covalent intermediate. EMBO J 22:3461-3471. (Pubitemid 36834876)
    • (2003) EMBO Journal , vol.22 , Issue.13 , pp. 3461-3471
    • Fromme, J.C.1    Verdine, G.L.2
  • 18
    • 76149146090 scopus 로고    scopus 로고
    • DNA-mediated charge transport in redox sensing and signaling
    • Genereux JC, Boal AK, Barton JK (2010) DNA-mediated charge transport in redox sensing and signaling. J Am Chem Soc 132:891-905.
    • (2010) J Am Chem Soc , vol.132 , pp. 891-905
    • Genereux, J.C.1    Boal, A.K.2    Barton, J.K.3
  • 19
    • 1342304229 scopus 로고    scopus 로고
    • Structural basis for removal of adenine mispaired with 8-oxoguanine by MutY adenine DNA glycosylase
    • DOI 10.1038/nature02306
    • Fromme JC, Banerjee A, Huang SJ, Verdine GL (2004) Structural basis for removal of adenine mispaired with 8- oxoguanine by MutY adenine DNA glycosylase. Nature 427:652-656. (Pubitemid 38248487)
    • (2004) Nature , vol.427 , Issue.6975 , pp. 652-656
    • Christopher, F.J.1    Banerjee, A.2    Huang, S.J.3    Verdine, G.L.4
  • 20
    • 33847333956 scopus 로고    scopus 로고
    • MUTYH-associated polyposis-From defect in base excision repair to clinical genetic testing
    • DOI 10.1016/j.dnarep.2006.11.001, PII S156878640600334X
    • Cheadle JP, Sampson JR (2007) MUTYH-associated polyposis-from defect in base excision repair to clinical genetic testing. DNA Repair 6:274-279. (Pubitemid 46329613)
    • (2007) DNA Repair , vol.6 , Issue.3 , pp. 274-279
    • Cheadle, J.P.1    Sampson, J.R.2
  • 21
    • 0036224749 scopus 로고    scopus 로고
    • The APC gene in colorectal cancer
    • Fodde R (2002) The APC gene in colorectal cancer. Eur J Cancer 38:867-871.
    • (2002) Eur J Cancer , vol.38 , pp. 867-871
    • Fodde, R.1
  • 22
    • 70349303816 scopus 로고    scopus 로고
    • Redox signaling between DNA Repair Proteins for efficient lesion detection
    • Boal AK, et al. (2009) Redox signaling between DNA Repair Proteins for efficient lesion detection. Proc Natl Acad Sci USA 106:15237-15242.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 15237-15242
    • Boal, A.K.1
  • 23
    • 79959941676 scopus 로고    scopus 로고
    • Mutants of the base excision repair glycosylase, endonuclease III: DNA charge transport as a first step in lesion detection
    • Romano CA, Sontz PA, Barton JK (2011) Mutants of the base excision repair glycosylase, endonuclease III: DNA charge transport as a first step in lesion detection. Biochemistry 50:6133-6145.
    • (2011) Biochemistry , vol.50 , pp. 6133-6145
    • Romano, C.A.1    Sontz, P.A.2    Barton, J.K.3
  • 24
    • 0027182114 scopus 로고
    • Helicases: Amino acid sequence comparisons and structure-function relationships
    • Gorbalenya AE, Koonin EV (1993) Helicases: amino acid sequence comparisons and structure-function relationships. Curr Opin Struct Biol 3:419-429. (Pubitemid 23207576)
    • (1993) Current Opinion in Structural Biology , vol.3 , Issue.3 , pp. 419-429
    • Gorbalenya, A.E.1    Koonin, E.V.2
  • 25
    • 44149094083 scopus 로고    scopus 로고
    • XPD Helicase Structures and Activities: Insights into the Cancer and Aging Phenotypes from XPD Mutations
    • DOI 10.1016/j.cell.2008.04.030, PII S0092867408005606
    • Fan L, et al. (2008) XPD helicase structures and activities: insights into the cancer and aging phenotypes from XPD mutations. Cell 133:789-800. (Pubitemid 351715395)
    • (2008) Cell , vol.133 , Issue.5 , pp. 789-800
    • Fan, L.1    Fuss, J.O.2    Cheng, Q.J.3    Arvai, A.S.4    Hammel, M.5    Roberts, V.A.6    Cooper, P.K.7    Tainer, J.A.8
  • 28
    • 53149104726 scopus 로고    scopus 로고
    • XPD structure reveals its secrets
    • Lehmann AR (2008) XPD structure reveals its secrets. DNA Repair 7:1912-1915.
    • (2008) DNA Repair , vol.7 , pp. 1912-1915
    • Lehmann, A.R.1
  • 29
    • 79960377998 scopus 로고    scopus 로고
    • XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase DNA repair
    • Fuss JO, Tainer JA (2011) XPB and XPD helicases in TFIIH orchestrate DNA duplex opening and damage verification to coordinate repair with transcription and cell cycle via CAK kinase DNA repair. DNA Repair 10:697-713.
    • (2011) DNA Repair , vol.10 , pp. 697-713
    • Fuss, J.O.1    Tainer, J.A.2
  • 32
    • 33748428875 scopus 로고    scopus 로고
    • The DNA Repair Helicases XPD and FancJ Have Essential Iron-Sulfur Domains
    • DOI 10.1016/j.molcel.2006.07.019, PII S1097276506005168
    • Rudolf J, Makrantoni V, Ingledew WJ, Stark MJR, White MF (2006) The DNA repair helicases XPD and FancJ have essential iron-sulfur domains. Mol Cell 23:801-808. (Pubitemid 44344515)
    • (2006) Molecular Cell , vol.23 , Issue.6 , pp. 801-808
    • Rudolf, J.1    Makrantoni, V.2    Ingledew, W.J.3    Stark, M.J.R.4    White, M.F.5
  • 33
    • 45849119445 scopus 로고    scopus 로고
    • Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD
    • Wolski SC, et al. (2008) Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD. PLos Biol 6:1332-1341.
    • (2008) PLos Biol , vol.6 , pp. 1332-1341
    • Wolski, S.C.1
  • 34
    • 80054726392 scopus 로고    scopus 로고
    • ATP-stimulated, DNA-mediated redox signaling by XPD, a DNA repair and transcription helicase
    • Mui TP, Fuss JO, Ishida JP, Tainer JA, Barton JK (2011) ATP-stimulated, DNA-mediated redox signaling by XPD, a DNA repair and transcription helicase. J Am Chem Soc 133:16378-16381.
    • (2011) J Am Chem Soc , vol.133 , pp. 16378-16381
    • Mui, T.P.1    Fuss, J.O.2    Ishida, J.P.3    Tainer, J.A.4    Barton, J.K.5
  • 35
    • 77950366206 scopus 로고    scopus 로고
    • The helicase XPD unwinds bubble structures and is not stalled by DNA lesions removed by the nucleotide excision repair pathway
    • Rudolf J, Rouillon C, Schwarz-Linek U, White MF (2010) The helicase XPD unwinds bubble structures and is not stalled by DNA lesions removed by the nucleotide excision repair pathway. Nucleic Acids Res 38:931-941.
    • (2010) Nucleic Acids Res , vol.38 , pp. 931-941
    • Rudolf, J.1    Rouillon, C.2    Schwarz-Linek, U.3    White, M.F.4
  • 36
    • 0001320568 scopus 로고    scopus 로고
    • MutS-mediated detection of DNA mismatches using atomic force microscopy
    • DOI 10.1021/ac991263i
    • Sun HB, Yokota H (2000) MutS-mediated detection of DNA mismatches using atomic force microscopy. Anal Chem 72:3138-3141. (Pubitemid 30482482)
    • (2000) Analytical Chemistry , vol.72 , Issue.14 , pp. 3138-3141
    • Sun, H.B.1    Yokota, H.2
  • 37
    • 33845443638 scopus 로고    scopus 로고
    • The EcoRI-DNA complex as a model for investigating protein-DNA interactions by atomic force microscopy
    • DOI 10.1021/bi060293u
    • Sorel I, et al. (2006) The EcoRI-DNA complex as a model for investigating protein-DNA interactions by atomic force microscopy. Biochemistry 45:14675-14682. (Pubitemid 44906983)
    • (2006) Biochemistry , vol.45 , Issue.49 , pp. 14675-14682
    • Sorel, I.1    Pietrement, O.2    Hamon, L.3    Baconnais, S.4    Le, C.E.5    Pastre, D.6
  • 38
    • 77149140805 scopus 로고    scopus 로고
    • Specific DNA-protein interactions on mica investigated by atomic force microscopy
    • Pastré D, et al. (2010) Specific DNA-protein interactions on mica investigated by atomic force microscopy. Langmuir 26:2618-2623.
    • (2010) Langmuir , vol.26 , pp. 2618-2623
    • Pastré, D.1
  • 39
    • 79960627586 scopus 로고    scopus 로고
    • Atomic force microscopy captures MutS tetramers initiating DNA mismatch repair
    • Jiang Y, Marszalek PE (2011) Atomic force microscopy captures MutS tetramers initiating DNA mismatch repair. EMBO J 30:2881-2893.
    • (2011) EMBO J , vol.30 , pp. 2881-2893
    • Jiang, Y.1    Marszalek, P.E.2
  • 41
    • 0037106080 scopus 로고    scopus 로고
    • Rapid gene cloning using terminator primers and modular vectors
    • Donahue WF, Turczyk BM, Jarrell KA (2002) Rapid gene cloning using terminator primers and modular vectors. Nucl Acid Res 30:e95.
    • (2002) Nucl Acid Res , vol.30
    • Donahue, W.F.1    Turczyk, B.M.2    Jarrell, K.A.3
  • 44
    • 0019887628 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids, 1 Models and theory
    • Berg OG, Winter RB, von Hippel PH (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
  • 49
    • 0036238830 scopus 로고    scopus 로고
    • Oxidative charge transport through DNA in nucleosome core particles
    • DOI 10.1016/S1074-5521(02)00121-7, PII S1074552102001217
    • Nunez ME, Noyes KT, Barton JK (2002) Oxidative charge transport through DNA in nucleosome core particles. Chem Biol 9:403-415. (Pubitemid 34439760)
    • (2002) Chemistry and Biology , vol.9 , Issue.4 , pp. 403-415
    • Nunez, M.E.1    Noyes, K.T.2    Barton, J.K.3
  • 50
    • 69449087074 scopus 로고    scopus 로고
    • DNA-mediated redox signaling for transcriptional activation of SoxR
    • Lee PE, Demple B, Barton JK (2009) DNA-mediated redox signaling for transcriptional activation of SoxR. Proc Natl Acad Sci USA 106:13164-13168.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 13164-13168
    • Lee, P.E.1    Demple, B.2    Barton, J.K.3
  • 51
    • 37649023948 scopus 로고    scopus 로고
    • A role for DNA-mediated charge transport in regulating p53: Oxidation of the DNA-bound protein from a distance
    • Augustyn KE, Merino EJ, Barton JK (2007) A role for DNA-mediated charge transport in regulating p53: Oxidation of the DNA-bound protein from a distance. Proc Natl Acad Sci USA 104:18907-18912.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 18907-18912
    • Augustyn, K.E.1    Merino, E.J.2    Barton, J.K.3
  • 52
    • 38949129784 scopus 로고    scopus 로고
    • DNA oxidation by charge transport in mitochondria
    • DOI 10.1021/bi701775s
    • Merino EJ, Barton JK (2008) DNA oxidation by charge transport in mitochondria. Biochemistry 47:1511-1517. (Pubitemid 351231202)
    • (2008) Biochemistry , vol.47 , Issue.6 , pp. 1511-1517
    • Merino, E.J.1    Barton, J.K.2
  • 53
    • 34548492954 scopus 로고    scopus 로고
    • An iron-sulfur domain of the eukaryotic primase is essential for RNA primer synthesis
    • DOI 10.1038/nsmb1288, PII NSMB1288
    • Klinge S, Hirst J, Maman JD, Krude T, Pellegrini L (2007) An iron-sulfur domain of the eukaryotic primase is essential for initiation of RNA primer synthesis. Nat Struct Mol Biol 14:875-877. (Pubitemid 47373835)
    • (2007) Nature Structural and Molecular Biology , vol.14 , Issue.9 , pp. 875-877
    • Klinge, S.1    Hirst, J.2    Maman, J.D.3    Krude, T.4    Pellegrini, L.5
  • 56
    • 34047109564 scopus 로고    scopus 로고
    • WSXM: A software for scanning probe microscopy and a tool for nanotechnology
    • Horcas I, et al. (2007) WSXM: a software for scanning probe microscopy and a tool for nanotechnology. Rev Sci Instrum 78:013705.
    • (2007) Rev Sci Instrum , vol.78 , pp. 013705
    • Horcas, I.1


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