메뉴 건너뛰기




Volumn 107, Issue 41, 2010, Pages 17545-17550

Strand- and site-specific DNA lesion demarcation by the xeroderma pigmentosum group D helicase

Author keywords

Cancer; DNA damage responses; Molecular recognition; Ultraviolet light

Indexed keywords

ADENOSINE TRIPHOSPHATASE; GLYCOSYLASE; GLYCOSYLTRANSFERASE; HELICASE; UNCLASSIFIED DRUG; XERODERMA PIGMENTOSUM GROUP D PROTEIN;

EID: 78049274322     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1004339107     Document Type: Article
Times cited : (74)

References (41)
  • 1
    • 0024049251 scopus 로고
    • The relative cytotoxicity of (6-4) photoproducts and cyclobutane dimers in mammalian cells
    • Mitchell DL (1988) The relative cytotoxicity of (6-4) photoproducts and cyclobutane dimers in mammalian cells. Photochem Photobiol 48:51-57.
    • (1988) Photochem Photobiol , vol.48 , pp. 51-57
    • Mitchell, D.L.1
  • 3
    • 19944431173 scopus 로고    scopus 로고
    • Powerful skin cancer protection by a CPD-photolyase transgene
    • Jans J, et al. (2005) Powerful skin cancer protection by a CPD-photolyase transgene. Curr Biol 15:105-115.
    • (2005) Curr Biol , vol.15 , pp. 105-115
    • Jans, J.1
  • 4
    • 27844470581 scopus 로고    scopus 로고
    • Transcriptome analysis reveals cyclobutane pyrimidine dimers as a major source of UV-induced DNA breaks
    • Garinis GA, et al. (2005) Transcriptome analysis reveals cyclobutane pyrimidine dimers as a major source of UV-induced DNA breaks. EMBO J 24:3952-3962.
    • (2005) EMBO J , vol.24 , pp. 3952-3962
    • Garinis, G.A.1
  • 5
    • 0004228157 scopus 로고    scopus 로고
    • American Society for Microbiology, Washington, DC
    • Friedberg EC, et al. (2006) DNA Repair and Mutagenesis (American Society for Microbiology, Washington, DC), pp 865-894.
    • (2006) DNA Repair and Mutagenesis , pp. 865-894
    • Friedberg, E.C.1
  • 6
    • 0142059994 scopus 로고    scopus 로고
    • Recognition and repair of the cyclobutane thymine dimer, a major cause of skin cancers, by the human excision nuclease
    • Reardon JT, Sancar A (2003) Recognition and repair of the cyclobutane thymine dimer, a major cause of skin cancers, by the human excision nuclease. Genes Dev 17:2539-2551.
    • (2003) Genes Dev , vol.17 , pp. 2539-2551
    • Reardon, J.T.1    Sancar, A.2
  • 7
    • 70349859881 scopus 로고    scopus 로고
    • DNA damage, aging, and cancer
    • Hoeijmakers JH (2009) DNA damage, aging, and cancer. New Engl J Med 361:1475-1485.
    • (2009) New Engl J Med , vol.361 , pp. 1475-1485
    • Hoeijmakers, J.H.1
  • 8
    • 0035495386 scopus 로고    scopus 로고
    • How nucleotide excision repair protects against cancer
    • Friedberg EC (2001) How nucleotide excision repair protects against cancer. Nat Rev Cancer 1:22-33.
    • (2001) Nat Rev Cancer , vol.1 , pp. 22-33
    • Friedberg, E.C.1
  • 9
    • 21744452376 scopus 로고    scopus 로고
    • Cancer in xeroderma pigmentosum and related disorders of DNA repair
    • Cleaver JE (2005) Cancer in xeroderma pigmentosum and related disorders of DNA repair. Nat Rev Cancer 5:564-573.
    • (2005) Nat Rev Cancer , vol.5 , pp. 564-573
    • Cleaver, J.E.1
  • 10
    • 32344450087 scopus 로고    scopus 로고
    • Pre-steady-state binding of damaged DNA by XPC-hHR23B reveals a kinetic mechanism for damage discrimination
    • Trego KS, Turchi JJ (2006) Pre-steady-state binding of damaged DNA by XPC-hHR23B reveals a kinetic mechanism for damage discrimination. Biochemistry 45:1961-1969.
    • (2006) Biochemistry , vol.45 , pp. 1961-1969
    • Trego, K.S.1    Turchi, J.J.2
  • 11
    • 34948892722 scopus 로고    scopus 로고
    • Recognition of DNA damage by the Rad4 nucleotide excision repair protein
    • Min J-H, 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
  • 12
    • 0030732132 scopus 로고    scopus 로고
    • Mechanism of open complex and dual incision formation by human nucleotide excision repair factors
    • Evans E, Moggs JG, Hwang JR, Egly J-M, Wood RD (1997) Mechanism of open complex and dual incision formation by human nucleotide excision repair factors. EMBO J 16:6559-6573.
    • (1997) EMBO J , vol.16 , pp. 6559-6573
    • Evans, E.1    Moggs, J.G.2    Hwang, J.R.3    Egly, J.-M.4    Wood, R.D.5
  • 13
    • 0030716255 scopus 로고    scopus 로고
    • Characterization of reaction intermediates of human excision repair nuclease
    • DOI 10.1074/jbc.272.46.28971
    • Mu D, Wakasugi M, Hsu DS, Sancar A (1997) Characterization of reaction intermediates of human excision repair nuclease. J Biol Chem 272:28971-28979. (Pubitemid 27498182)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.46 , pp. 28971-28979
    • Mu, D.1    Wakasugi, M.2    Hsu, D.S.3    Sancar, A.4
  • 14
    • 0029338999 scopus 로고
    • Contrasting structural impacts induced by cys-syncyclobutane dimer and (6-4) adduct in DNA duplex decamers: Implication in mutagenesis and repair activity
    • Kim J-K, Patel D, Choi B-S (1995) Contrasting structural impacts induced by cys-syncyclobutane dimer and (6-4) adduct in DNA duplex decamers: Implication in mutagenesis and repair activity. Photochem Photobiol 62:44-50.
    • (1995) Photochem Photobiol , vol.62 , pp. 44-50
    • Kim, J.-K.1    Patel, D.2    Choi, B.-S.3
  • 15
    • 0032500623 scopus 로고    scopus 로고
    • Solution-state structure of a DNA dodecamer duplex containing a cis-syn thymine cyclobutane dimer, the major UV photoproduct of DNA
    • McAteer K, Jing Y, Kao J, Taylor J-S, Kennedy MA (1998) Solution-state structure of a DNA dodecamer duplex containing a cis-syn thymine cyclobutane dimer, the major UV photoproduct of DNA. J Mol Biol 282:1013-1032.
    • (1998) J Mol Biol , vol.282 , pp. 1013-1032
    • McAteer, K.1    Jing, Y.2    Kao, J.3    Taylor, J.-S.4    Kennedy, M.A.5
  • 16
    • 0027483739 scopus 로고
    • Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA
    • Jones CJ, Wood RD (1993) Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA. Biochemistry 32:12096-12104.
    • (1993) Biochemistry , vol.32 , pp. 12096-12104
    • Jones, C.J.1    Wood, R.D.2
  • 17
    • 0029943633 scopus 로고    scopus 로고
    • An affinity of human replication protein A for ultraviolet-damaged DNA
    • Burns JL, Guzder SN, Sung P, Prakash S, Prakash L (1996) An affinity of human replication protein A for ultraviolet-damaged DNA. J Biol Chem 271:11607-11610.
    • (1996) J Biol Chem , vol.271 , pp. 11607-11610
    • Burns, J.L.1    Guzder, S.N.2    Sung, P.3    Prakash, S.4    Prakash, L.5
  • 19
    • 0034647734 scopus 로고    scopus 로고
    • Human damage-specific DNA-binding protein p48
    • Nichols AF, et al. (2000) Human damage-specific DNA-binding protein p48. J Biol Chem 275:21422-21428.
    • (2000) J Biol Chem , vol.275 , pp. 21422-21428
    • Nichols, A.F.1
  • 20
    • 0033636515 scopus 로고    scopus 로고
    • Xeroderma pigmentosum p48 gene enhances global genomic repair and suppresses UV-induced mutagenesis
    • Tang JY, Hwang BJ, Ford JM, Hanawalt PC, Chu G (2000) Xeroderma pigmentosum p48 gene enhances global genomic repair and suppresses UV-induced mutagenesis. Mol Cell 5:737-744.
    • (2000) Mol Cell , vol.5 , pp. 737-744
    • Tang, J.Y.1    Hwang, B.J.2    Ford, J.M.3    Hanawalt, P.C.4    Chu, G.5
  • 21
    • 21044442126 scopus 로고    scopus 로고
    • UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex
    • Sugasawa K, et al. (2005) UV-induced ubiquitylation of XPC protein mediated by UV-DDB-ubiquitin ligase complex. Cell 121:387-400.
    • (2005) Cell , vol.121 , pp. 387-400
    • Sugasawa, K.1
  • 22
    • 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
    • Rapić-Otrin V, McLenigan MP, Bisi DC, Gonzales 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.
    • (2002) Nucleic Acids Res , vol.30 , pp. 2588-2598
    • Rapić-Otrin, V.1    McLenigan, M.P.2    Bisi, D.C.3    Gonzales, M.4    Levine, A.S.5
  • 23
    • 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
    • C Wittschieben BO, Iwai S, Wood RD (2005) DDB1-DDB2 (xeroderma pigmentosum group E) protein complex recognizes a cyclobutane pyrimidine dimer, mismatches, 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
  • 24
    • 0031666241 scopus 로고    scopus 로고
    • Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interactions between XPD and the p44 subunit of TFIIH
    • Coin F, et al. (1998) Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interactions between XPD and the p44 subunit of TFIIH. Nat Genet 20:184-188.
    • (1998) Nat Genet , vol.20 , pp. 184-188
    • Coin, F.1
  • 25
    • 0040435451 scopus 로고    scopus 로고
    • TFIIH with inactive XPD helicase functions in transcription initiation but is defective in DNA repair
    • Winkler GS, et al. (2000) TFIIH with inactive XPD helicase functions in transcription initiation but is defective in DNA repair. J Biol Chem 275:4258-4266.
    • (2000) J Biol Chem , vol.275 , pp. 4258-4266
    • Winkler, G.S.1
  • 26
    • 34247513888 scopus 로고    scopus 로고
    • Distinct roles for the XPB/p52 and XPD7p44 subcomplexes of TFIIH in damaged DNA opening during nucleotide excision repair
    • Coin F, Oksenych V, Egly J-M (2007) Distinct roles for the XPB/p52 and XPD7p44 subcomplexes of TFIIH in damaged DNA opening during nucleotide excision repair. Mol Cell 26:245-256.
    • (2007) Mol Cell , vol.26 , pp. 245-256
    • Coin, F.1    Oksenych, V.2    Egly, J.-M.3
  • 27
    • 53149104726 scopus 로고    scopus 로고
    • XPD structure reveals its secrets
    • Lehman AR (2008) XPD structure reveals its secrets. DNA Repair 7:1912-1915.
    • (2008) DNA Repair , vol.7 , pp. 1912-1915
    • Lehman, A.R.1
  • 28
    • 70350566800 scopus 로고    scopus 로고
    • Molecular insights into the recruitment of TFIIH to sites of DNA damage
    • Oksenych V, de Jesus BB, Zhovmer A, Egly J-M, Coin F (2009) Molecular insights into the recruitment of TFIIH to sites of DNA damage. EMBO J 28:2971-2980.
    • (2009) EMBO J , vol.28 , pp. 2971-2980
    • Oksenych, V.1    De Jesus, B.B.2    Zhovmer, A.3    Egly, J.-M.4    Coin, F.5
  • 29
    • 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
  • 30
    • 38349091095 scopus 로고    scopus 로고
    • The iron-containing domain is essential in Rad3 helicases for coupling of ATP hydrolysis to DNA translocation and for targeting the helicase to the ssDNA-dsDNA junction
    • Pugh RA, et al. (2007) The iron-containing domain is essential in Rad3 helicases for coupling of ATP hydrolysis to DNA translocation and for targeting the helicase to the ssDNA-dsDNA junction. J Biol Chem 283:1732-1743.
    • (2007) J Biol Chem , vol.283 , pp. 1732-1743
    • Pugh, R.A.1
  • 31
    • 0019285806 scopus 로고
    • Comparison of the cleavage of pyrimidine dimers by the bacteriophage T4 and Micrococcus luteus UV-specific endonucleases
    • Gordon LK, Haseltine WA (1980) Comparison of the cleavage of pyrimidine dimers by the bacteriophage T4 and Micrococcus luteus UV-specific endonucleases. J Biol Chem 255:12047-12050.
    • (1980) J Biol Chem , vol.255 , pp. 12047-12050
    • Gordon, L.K.1    Haseltine, W.A.2
  • 33
    • 70449717367 scopus 로고    scopus 로고
    • Two-step recognition of DNA damage for mammalian nucleotide excision repair: Directional binding of the XPC complex and DNA strand scanning
    • Sugasawa K, Akagi J, Nishi R, Iwai S, Hanaoka F (2009) Two-step recognition of DNA damage for mammalian nucleotide excision repair: Directional binding of the XPC complex and DNA strand scanning. Mol Cell 36:642-653.
    • (2009) Mol Cell , vol.36 , pp. 642-653
    • Sugasawa, K.1    Akagi, J.2    Nishi, R.3    Iwai, S.4    Hanaoka, F.5
  • 34
    • 0027391296 scopus 로고
    • Inhibition of Rad3 DNA helicase activity by DNA adducts and abasic sites: Implications for the role of a DNA helicase in damage-specific incision of DNA
    • DOI 10.1021/bi00053a029
    • Naegeli H, Bardwell L, Friedberg EC (1993) Inhibition of Rad3 DNA helicase activity by DNA adducts and abasic sites: Implications for the role of a DNA helicase in damage-specific incision of DNA. Biochemistry 32:613-621. (Pubitemid 23034901)
    • (1993) Biochemistry , vol.32 , Issue.2 , pp. 613-621
    • Naegeli, H.1    Bardwell, L.2    Friedberg, E.C.3
  • 35
    • 43949110271 scopus 로고    scopus 로고
    • Structure of the DNA repair helicase XPD
    • Liu H, et al. (2008) Structure of the DNA repair helicase XPD. Cell 133:801-812.
    • (2008) Cell , vol.133 , pp. 801-812
    • Liu, H.1
  • 36
    • 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:e149.
    • (2008) PLoS Biol , vol.6
    • Wolski, S.C.1
  • 37
    • 44149094083 scopus 로고    scopus 로고
    • XPD helicase structures and activities: Insights into the cancer and aging phenotypes from XPD mutations
    • Fan L, et al. (2008) XPD helicase structures and activities: Insights into the cancer and aging phenotypes from XPD mutations. Cell 133:789-800.
    • (2008) Cell , vol.133 , pp. 789-800
    • Fan, L.1
  • 38
    • 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
    • 10.1093/nar/gkp1058
    • Rudolf J, Rouillon C, Schwarz-Linek U, White MF (2009) 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 10.1093/nar/gkp1058.
    • (2009) Nucleic Acids Res , vol.38 , pp. 931-941
    • Rudolf, J.1    Rouillon, C.2    Schwarz-Linek, U.3    White, M.F.4
  • 39
    • 31444444611 scopus 로고    scopus 로고
    • Initiation of DNA repair mediated by a stalled RNA polymerase IIO
    • Lainé J-P, Egly J-M (2006) Initiation of DNA repair mediated by a stalled RNA polymerase IIO. EMBO J 25:387-397.
    • (2006) EMBO J , vol.25 , pp. 387-397
    • Lainé, J.-P.1    Egly, J.-M.2
  • 40
    • 56749157389 scopus 로고    scopus 로고
    • Transcription-coupled DNA repair: Two decades of progress and surprises
    • Hanawalt PC, Spivak G (2008) Transcription-coupled DNA repair: Two decades of progress and surprises. Nat Rev Mol Cell Biol 9:958-970.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 958-970
    • Hanawalt, P.C.1    Spivak, G.2
  • 41
    • 0037059785 scopus 로고    scopus 로고
    • The β-hairpin motif of UvrB is essential for DNA binding, damage processing, and UvrC-mediated incisions
    • Skorvaga M, Theis K, Mandavilli BS, Kisker C, Van Houten B (2002) The β-hairpin motif of UvrB is essential for DNA binding, damage processing, and UvrC-mediated incisions. J Biol Chem 277:1553-1559.
    • (2002) J Biol Chem , vol.277 , pp. 1553-1559
    • Skorvaga, M.1    Theis, K.2    Mandavilli, B.S.3    Kisker, C.4    Van Houten, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.