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Volumn 109, Issue 41, 2012, Pages

Damaged DNA induced UV-damaged DNA-binding protein (UV-DDB) dimerization and its roles in chromatinized DNA repair

Author keywords

Ubiquitin proteosome system; UV damage; X ray crystallography

Indexed keywords

CULLIN; DNA BINDING PROTEIN; UBIQUITIN PROTEIN LIGASE E3;

EID: 84867376482     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1110067109     Document Type: Article
Times cited : (71)

References (53)
  • 1
    • 7944232104 scopus 로고    scopus 로고
    • (ASM Press, Washington, DC), 2nd Ed
    • Friedberg EC, et al. (2005) DNA Repair and Mutagenesis (ASM Press, Washington, DC), 2nd Ed, pp 1-1164.
    • (2005) DNA Repair and Mutagenesis , pp. 1-1164
    • Friedberg, E.C.1
  • 3
    • 0042379937 scopus 로고    scopus 로고
    • DDB complexities
    • DOI 10.1016/S1568-7864(03)00113-7
    • Wittschieben BO, Wood RD (2003) DDB complexities. DNA Repair (Amst) 2:1065-1069. (Pubitemid 37088165)
    • (2003) DNA Repair , vol.2 , Issue.9 , pp. 1065-1069
    • Wittschieben, B.O.1    Wood, R.D.2
  • 4
    • 16244423719 scopus 로고    scopus 로고
    • The UV-damaged DNA binding protein mediates efficient targeting of the nucleotide excision repair complex to UV-induced photo lesions
    • DOI 10.1016/j.dnarep.2005.01.001
    • Moser J, et al. (2005) The UV-damaged DNA binding protein mediates efficient targeting of the nucleotide excision repair complex to UV-induced photo lesions. DNA Repair (Amst) 4:571-582. (Pubitemid 40462045)
    • (2005) DNA Repair , vol.4 , Issue.5 , pp. 571-582
    • Moser, J.1    Volker, M.2    Kool, H.3    Alekseev, S.4    Vrieling, H.5    Yasui, A.6    Van Zeeland, A.A.7    Mullenders, L.H.F.8
  • 6
    • 0029165064 scopus 로고
    • Chromosomal localization and cDNA cloning of the genes (DDB1 and DDB2) for the p127 and p48 subunits of a human damage-specific DNA binding protein
    • Dualan R, et al. (1995) Chromosomal localization and cDNA cloning of the genes (DDB1 and DDB2) for the p127 and p48 subunits of a human damage-specific DNA binding protein. Genomics 29:62-69.
    • (1995) Genomics , vol.29 , pp. 62-69
    • Dualan, R.1
  • 7
    • 0038105065 scopus 로고    scopus 로고
    • True XP group E patients have a defective UV-damaged DNA binding protein complex and mutations in DDB2 which reveal the functional domains of its p48 product
    • DOI 10.1093/hmg/ddg174
    • Rapic-Otrin V, et al. (2003) True XP group E patients have a defective UV-damaged DNA binding protein complex and mutations in DDB2 which reveal the functional domains of its p48 product. Hum Mol Genet 12:1507-1522. (Pubitemid 36857299)
    • (2003) Human Molecular Genetics , vol.12 , Issue.13 , pp. 1507-1522
    • Rapic-Otrin, V.1    Navazza, V.2    Nardo, T.3    Botta, E.4    McLenigan, M.5    Bisi, D.C.6    Levine, A.S.7    Stefanini, M.8
  • 8
    • 0033176104 scopus 로고    scopus 로고
    • A nearly identified patient with clinical xeroderma pigmentosum phenotype has a non-sense mutation in the DDB2 gene and incomplete repair in (6-4) photoproducts
    • DOI 10.1046/j.1523-1747.1999.00652.x
    • Itoh T, Mori T, Ohkubo H, Yamaizumi M (1999) A newly identified patient with clinical xeroderma pigmentosum phenotype has a non-sense mutation in the DDB2 gene and incomplete repair in (6-4) photoproducts. J Invest Dermatol 113:251-257. (Pubitemid 30202531)
    • (1999) Journal of Investigative Dermatology , vol.113 , Issue.2 , pp. 251-257
    • Itoh, T.1    Mori, T.2    Ohkubo, H.3    Yamaizumi, M.4
  • 9
    • 0029768095 scopus 로고    scopus 로고
    • - phenotype
    • DOI 10.1074/jbc.271.40.24317
    • Nichols AF, Ong P, Linn S (1996) Mutations specific to the xeroderma pigmentosum group E Ddb-phenotype. J Biol Chem 271:24317-24320. (Pubitemid 26333157)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.40 , pp. 24317-24320
    • Nichols, A.F.1    Ong, P.2    Linn, S.3
  • 10
    • 28944440380 scopus 로고    scopus 로고
    • DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine dimer, mismatches, apurinic/apyrimidinic sites, and compound in DNA
    • DOI 10.1074/jbc.M507854200
    • Wittschieben BO, Iwai S, Wood RD (2005) DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine dimer, mis-matches, apurinic/apyrimidinic sites, and compound lesions in DNA. J Biol Chem 280:39982-39989. (Pubitemid 41782166)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.48 , pp. 39982-39989
    • Wittschieben, B.O.1    Iwai, S.2    Wood, R.D.3
  • 11
    • 57749198023 scopus 로고    scopus 로고
    • Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex
    • Scrima A, et al. (2008) Structural basis of UV DNA-damage recognition by the DDB1-DDB2 complex. Cell 135:1213-1223.
    • (2008) Cell , vol.135 , pp. 1213-1223
    • Scrima, A.1
  • 12
    • 0345306615 scopus 로고    scopus 로고
    • In Vivo Recruitment of XPC to UV-induced Cyclobutane Pyrimidine Dimers by the DDB2 Gene Product
    • DOI 10.1074/jbc.M307254200
    • Fitch ME, Nakajima S, Yasui A, Ford JM(2003) In vivo recruitment of XPC to UV-induced cyclobutane pyrimidine dimers by the DDB2 gene product. J Biol Chem 278:46906-46910. (Pubitemid 37452272)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.47 , pp. 46906-46910
    • Fitch, M.E.1    Nakajima, S.2    Yasui, A.3    Ford, J.M.4
  • 13
    • 77952620360 scopus 로고    scopus 로고
    • DDB2 complex-mediated ubiquitylation around DNA damage is oppositely regulated by XPC and Ku and contributes to the recruitment of XPA
    • Takedachi A, Saijo M, Tanaka Ke (2010) DDB2 complex-mediated ubiquitylation around DNA damage is oppositely regulated by XPC and Ku and contributes to the recruitment of XPA. Mol Cell Biol 30:2708-2723.
    • (2010) Mol Cell Biol , vol.30 , pp. 2708-2723
    • Takedachi, A.1    Saijo, M.2    Tanaka, K.3
  • 14
    • 63049106823 scopus 로고    scopus 로고
    • Regulation of DNA damage response pathways by the cullin- RING ubiquitin ligases
    • Hannah J, Zhou P (2009) Regulation of DNA damage response pathways by the cullin- RING ubiquitin ligases. DNA Repair (Amst) 8:536-543.
    • (2009) DNA Repair (Amst) , vol.8 , pp. 536-543
    • Hannah, J.1    Zhou, P.2
  • 15
    • 33750509178 scopus 로고    scopus 로고
    • CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation
    • DOI 10.1038/ncb1490, PII NCB1490
    • Higa LA, et al. (2006) CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation. Nat Cell Biol 8:1277-1283. (Pubitemid 44660593)
    • (2006) Nature Cell Biology , vol.8 , Issue.11 , pp. 1277-1283
    • Higa, L.A.1    Wu, M.2    Ye, T.3    Kobayashi, R.4    Sun, H.5    Zhang, H.6
  • 16
    • 48549085044 scopus 로고    scopus 로고
    • The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A
    • Guerrero-Santoro J, et al. (2008) The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A. Cancer Res 68:5014-5022.
    • (2008) Cancer Res , vol.68 , pp. 5014-5022
    • Guerrero-Santoro, J.1
  • 17
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • DOI 10.1038/nrm1547
    • Petroski MD, Deshaies RJ (2005) Function and regulation of cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol 6:9-20. (Pubitemid 40064895)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.1 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 19
    • 33749535905 scopus 로고    scopus 로고
    • Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery
    • DOI 10.1038/nature05175, PII NATURE05175
    • Angers S, et al. (2006) Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery. Nature 443:590-593. (Pubitemid 44527296)
    • (2006) Nature , vol.443 , Issue.7111 , pp. 590-593
    • Angers, S.1    Li, T.2    Yi, X.3    MacCoss, M.J.4    Moon, R.T.5    Zheng, N.6
  • 20
    • 33747831132 scopus 로고    scopus 로고
    • L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and regulates CDT1 proteolysis in response to DNA damage
    • Higa LA, et al. (2006) L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and regulates CDT1 proteolysis in response to DNA damage. Cell Cycle 5:1675-1680. (Pubitemid 44285255)
    • (2006) Cell Cycle , vol.5 , Issue.15 , pp. 1675-1680
    • Higa, L.A.1    Banks, D.2    Wu, M.3    Kobayashi, R.4    Sun, H.5    Zhang, H.6
  • 21
  • 22
    • 34248209547 scopus 로고    scopus 로고
    • Stealing the spotlight: CUL4-DDB1 ubiquitin ligase docks WD40-repeat proteins to destroy
    • Higa LA, Zhang H (2007) Stealing the spotlight: CUL4-DDB1 ubiquitin ligase docks WD40-repeat proteins to destroy. Cell Div 2:5.
    • (2007) Cell Div , vol.2 , pp. 5
    • Higa, L.A.1    Zhang, H.2
  • 24
    • 33644536070 scopus 로고    scopus 로고
    • The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group e and targets histone H2A at UV-damaged DNA sites
    • Kapetanaki MG, et al. (2006) The DDB1-CUL4ADDB2 ubiquitin ligase is deficient in xeroderma pigmentosum group E and targets histone H2A at UV-damaged DNA sites. Proc Natl Acad Sci USA 103:2588-2593.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 2588-2593
    • Kapetanaki, M.G.1
  • 27
    • 33744958177 scopus 로고    scopus 로고
    • Cullin 4A-mediated proteolysis of DDB2 protein at DNA damage sites regulates in vivo lesion recognition by XPC
    • El-Mahdy MA, et al. (2006) Cullin 4A-mediated proteolysis of DDB2 protein at DNA damage sites regulates in vivo lesion recognition by XPC. J Biol Chem 281:13404-13411.
    • (2006) J Biol Chem , vol.281 , pp. 13404-13411
    • El-Mahdy, M.A.1
  • 28
    • 0036606551 scopus 로고    scopus 로고
    • Sequential binding of UV DNA damage binding factor and degradation of the p48 subunit as early events after UV irradiation
    • Rapic-Otrin V, McLenigan MP, Bisi DC, Gonzalez M, Levine AS (2002) Sequential binding of UV DNA damage binding factor and degradation of the p48 subunit as early events after UV irradiation. Nucleic Acids Res 30:2588-2598. (Pubitemid 34619012)
    • (2002) Nucleic Acids Research , vol.30 , Issue.11 , pp. 2588-2598
    • Rapic-Otrin, V.1    McLenigan, M.P.2    Bisi, D.C.3    Gonzalez, M.4    Levine, A.S.5
  • 29
    • 0034813575 scopus 로고    scopus 로고
    • The xeroderma pigmentosum group E gene product DDB2 is a specific target of cullin 4A in mammalian cells
    • DOI 10.1128/MCB.21.20.6738-6747.2001
    • Nag A, Bondar T, Shiv S, Raychaudhuri P (2001) The xeroderma pigmentosum group E gene product DDB2 is a specific target of cullin 4A in mammalian cells. Mol Cell Biol 21:6738-6747. (Pubitemid 32911236)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.20 , pp. 6738-6747
    • Nag, A.1    Bondar, T.2    Shiv, S.3    Raychaudhuri, P.4
  • 30
    • 57349187165 scopus 로고    scopus 로고
    • Cellular concentrations of DDB2 regulate dynamic binding of DDB1 at UV-induced DNA damage
    • Alekseev S, et al. (2008) Cellular concentrations of DDB2 regulate dynamic binding of DDB1 at UV-induced DNA damage. Mol Cell Biol 28:7402-7413.
    • (2008) Mol Cell Biol , vol.28 , pp. 7402-7413
    • Alekseev, S.1
  • 31
    • 34948892722 scopus 로고    scopus 로고
    • Recognition of DNA damage by the Rad4 nucleotide excision repair protein
    • Min JH, Pavletich NP (2007) Recognition of DNA damage by the Rad4 nucleotide excision repair protein. Nature 449:570-575.
    • (2007) Nature , vol.449 , pp. 570-575
    • Min, J.H.1    Pavletich, N.P.2
  • 33
    • 43149102700 scopus 로고    scopus 로고
    • Versatile protection from mutagenic DNA lesions conferred by bipartite recognition in nucleotide excision repair
    • Maillard O, Camenisch U, Blagoev KB, Naegeli H (2008) Versatile protection from mutagenic DNA lesions conferred by bipartite recognition in nucleotide excision repair. Mutat Res 658:271-286.
    • (2008) Mutat Res , vol.658 , pp. 271-286
    • Maillard, O.1    Camenisch, U.2    Blagoev, K.B.3    Naegeli, H.4
  • 34
    • 69249202311 scopus 로고    scopus 로고
    • Two-stage dynamic DNA quality check by xeroderma pigmentosum group C protein
    • Camenisch U, et al. (2009) Two-stage dynamic DNA quality check by xeroderma pigmentosum group C protein. EMBO J 28:2387-2399.
    • (2009) EMBO J , vol.28 , pp. 2387-2399
    • Camenisch, U.1
  • 35
    • 0027408241 scopus 로고
    • Purification and characterization of a human protein that binds to damaged DNA
    • Hwang BJ, Chu G (1993) Purification and characterization of a human protein that binds to damaged DNA. Biochemistry 32:1657-1666.
    • (1993) Biochemistry , vol.32 , pp. 1657-1666
    • Hwang, B.J.1    Chu, G.2
  • 36
    • 36549054109 scopus 로고    scopus 로고
    • Calorimetric approaches to characterizing effects of additives on protein crystallization
    • Yeh JI, Beale SI (2007) Calorimetric approaches to characterizing effects of additives on protein crystallization. Cryst Growth Des 7:2134-2139.
    • (2007) Cryst Growth des , vol.7 , pp. 2134-2139
    • Yeh, J.I.1    Beale, S.I.2
  • 37
    • 30344460705 scopus 로고    scopus 로고
    • Structure of DDB1 in complex with a paramyxovirus V protein: Viral Hijack of a propeller cluster in ubiquitin ligase
    • DOI 10.1016/j.cell.2005.10.033, PII S009286740501233X
    • Li T, Chen X, Garbutt KC, Zhou P, Zheng N (2006) Structure of DDB1 in complex with a paramyxovirus V protein: Viral hijack of a propeller cluster in ubiquitin ligase. Cell 124:105-117. (Pubitemid 43069313)
    • (2006) Cell , vol.124 , Issue.1 , pp. 105-117
    • Li, T.1    Chen, X.2    Garbutt, K.C.3    Zhou, P.4    Zheng, N.5
  • 38
    • 0034616963 scopus 로고    scopus 로고
    • Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites
    • Batty D, Rapic'-Otrin V, Levine AS, Wood RD (2000) Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites. J Mol Biol 300:275-290.
    • (2000) J Mol Biol , vol.300 , pp. 275-290
    • Batty, D.1    Rapic'-Otrin, V.2    Levine, A.S.3    Wood, R.D.4
  • 39
    • 0037328523 scopus 로고    scopus 로고
    • Quantitative characterization of biomolecular assemblies and interactions using atomic force microscopy
    • DOI 10.1016/S1046-2023(02)00308-0, PII S1046202302003080
    • Yang Y, Wang H, Erie DA (2003) Quantitative characterization of biomolecular assemblies and interactions using atomic force microscopy. Methods 29:175-187. (Pubitemid 36269204)
    • (2003) Methods , vol.29 , Issue.2 , pp. 175-187
    • Yang, Y.1    Wang, H.2    Erie, D.A.3
  • 41
    • 77649264800 scopus 로고    scopus 로고
    • Collaborative dynamic DNA scanning by nucleotide excision repair proteins investigated by single-molecule imaging of quantum-dot-labeled proteins
    • Kad NM, Wang H, Kennedy GG, Warshaw DM, Van Houten B (2010) Collaborative dynamic DNA scanning by nucleotide excision repair proteins investigated by single-molecule imaging of quantum-dot-labeled proteins. Mol Cell 37:702-713.
    • (2010) Mol Cell , vol.37 , pp. 702-713
    • Kad, N.M.1    Wang, H.2    Kennedy, G.G.3    Warshaw, D.M.4    Van Houten, B.5
  • 42
    • 48449106541 scopus 로고    scopus 로고
    • Functional characterization and atomic force microscopy of a DNA repair protein conjugated to a quantum dot
    • Wang H, Tessmer I, Croteau DL, Erie DA, Van Houten B (2008) Functional characterization and atomic force microscopy of a DNA repair protein conjugated to a quantum dot. Nano Lett 8:1631-1637.
    • (2008) Nano Lett , vol.8 , pp. 1631-1637
    • Wang, H.1    Tessmer, I.2    Croteau, D.L.3    Erie, D.A.4    Van Houten, B.5
  • 43
    • 0033538572 scopus 로고    scopus 로고
    • Characterization of DNA recognition by the human UV-damaged DNA-binding protein
    • Fujiwara Y, et al. (1999) Characterization of DNA recognition by the human UV-damaged DNA-binding protein. J Biol Chem 274:20027-20033.
    • (1999) J Biol Chem , vol.274 , pp. 20027-20033
    • Fujiwara, Y.1
  • 45
    • 70349339322 scopus 로고    scopus 로고
    • Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization
    • Merlet J, Burger J, Gomes JE, Pintard L (2009) Regulation of cullin-RING E3 ubiquitin-ligases by neddylation and dimerization. Cell Mol Life Sci 66:1924-1938.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 1924-1938
    • Merlet, J.1    Burger, J.2    Gomes, J.E.3    Pintard, L.4
  • 48
    • 47949108983 scopus 로고    scopus 로고
    • Regulation of the transcription factor Ets-1 by DNA-mediated homo-dimerization
    • Lamber EP, et al. (2008) Regulation of the transcription factor Ets-1 by DNA-mediated homo-dimerization. EMBO J 27:2006-2017.
    • (2008) EMBO J , vol.27 , pp. 2006-2017
    • Lamber, E.P.1
  • 49
    • 40749153516 scopus 로고    scopus 로고
    • Cullin-RING ubiquitin ligases: Global regulation and activation cycles
    • Bosu DR, Kipreos ET (2008) Cullin-RING ubiquitin ligases: Global regulation and activation cycles. Cell Div 3:7.
    • (2008) Cell Div , vol.3 , pp. 7
    • Bosu, D.R.1    Kipreos, E.T.2
  • 51
    • 0031686766 scopus 로고    scopus 로고
    • Temperature and pH-dependent supramolecular self-assembly of amelogenin molecules: A dynamic light-scattering analysis
    • DOI 10.1006/jsbi.1998.4008
    • Moradian-Oldak J, Leung W, Fincham AG (1998) Temperature and pH-dependent supramolecular self-assembly of amelogenin molecules: A dynamic light-scattering analysis. J Struct Biol 122:320-327. (Pubitemid 28440995)
    • (1998) Journal of Structural Biology , vol.122 , Issue.3 , pp. 320-327
    • Moradian-Oldak, J.1    Leung, W.2    Fincham, A.G.3
  • 52
    • 48849092967 scopus 로고    scopus 로고
    • Using biacore to measure the binding kinetics of an antibody-antigen interaction
    • Murphy M, Jason-Moller L, Bruno J (2006) Using biacore to measure the binding kinetics of an antibody-antigen interaction. Curr Protoc Protein Sci 19:1-17.
    • (2006) Curr Protoc Protein Sci , vol.19 , pp. 1-17
    • Murphy, M.1    Jason-Moller, L.2    Bruno, J.3
  • 53
    • 81855227619 scopus 로고    scopus 로고
    • DDB2/CSA ubiquitin ligase architecture, targeting, and activation
    • DDB2/CSA ubiquitin ligase architecture, targeting, and activation. Cell 147:1024-1039.
    • (2011) Cell , vol.147 , pp. 1024-1039
    • Fischer, E.S.1


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