메뉴 건너뛰기




Volumn 2, Issue 3, 2003, Pages 325-336

DNA bending by the human damage recognition complex XPC-HR23B

Author keywords

Damage recognition; DNA bending; Nucleotide excision repair; Scanning force microscopy; XPC

Indexed keywords

BINDING PROTEIN; CURVED DNA; DNA; UNCLASSIFIED DRUG; XPC HR23B PROTEIN;

EID: 0037353459     PISSN: 15687864     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1568-7864(02)00222-7     Document Type: Article
Times cited : (88)

References (31)
  • 2
    • 0032742715 scopus 로고    scopus 로고
    • DNA damage recognition during nucleotide excision repair in mammalian cells
    • Wood R.D. DNA damage recognition during nucleotide excision repair in mammalian cells. Biochimie. 81:1999;39-44.
    • (1999) Biochimie , vol.81 , pp. 39-44
    • Wood, R.D.1
  • 3
    • 0028269240 scopus 로고
    • Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23
    • Masutani C., Sugasawa K., Yanagisawa J., Sonoyama T., Ui M., Enomoto T., Takio K., Tanaka K., van der Spek P.J., Bootsma D. Purification and cloning of a nucleotide excision repair complex involving the xeroderma pigmentosum group C protein and a human homologue of yeast RAD23. EMBO J. 13:1994;1831-1843.
    • (1994) EMBO J. , vol.13 , pp. 1831-1843
    • Masutani, C.1    Sugasawa, K.2    Yanagisawa, J.3    Sonoyama, T.4    Ui, M.5    Enomoto, T.6    Takio, K.7    Tanaka, K.8    Van der Spek, P.J.9    Bootsma, D.10
  • 4
    • 0035374836 scopus 로고    scopus 로고
    • Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair
    • Araki M., Masutani C., Takemura M., Uchida A., Sugasawa K., Kondoh J., Ohkuma Y., Hanaoka F. Centrosome protein centrin 2/caltractin 1 is part of the xeroderma pigmentosum group C complex that initiates global genome nucleotide excision repair. J. Biol. Chem. 276:2001;18665-18672.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18665-18672
    • Araki, M.1    Masutani, C.2    Takemura, M.3    Uchida, A.4    Sugasawa, K.5    Kondoh, J.6    Ohkuma, Y.7    Hanaoka, F.8
  • 6
    • 0028896837 scopus 로고
    • Reconstitution of human DNA repair excision nuclease in a highly defined system
    • Mu D., Park C.H., Matsunaga T., Hsu D.S., Reardon J.T., Sancar A. Reconstitution of human DNA repair excision nuclease in a highly defined system. J. Biol. Chem. 270:1995;2415-2418.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2415-2418
    • Mu, D.1    Park, C.H.2    Matsunaga, T.3    Hsu, D.S.4    Reardon, J.T.5    Sancar, A.6
  • 9
    • 0035282109 scopus 로고    scopus 로고
    • A multistep damage recognition mechanism for global genomic nucleotide excision repair
    • Sugasawa K., Okamoto T., Shimizu Y., Masutani C., Iwai S., Hanaoka F. A multistep damage recognition mechanism for global genomic nucleotide excision repair. Genes Dev. 15:2001;507-521.
    • (2001) Genes Dev. , vol.15 , pp. 507-521
    • Sugasawa, K.1    Okamoto, T.2    Shimizu, Y.3    Masutani, C.4    Iwai, S.5    Hanaoka, F.6
  • 11
    • 0037188408 scopus 로고    scopus 로고
    • The XPC-HR23B complex displays high affinity and specificity for damaged DNA in a true-equilibrium fluorescence assay
    • Hey T., Lipps G., Sugasawa K., Iwai S., Hanaoka F., Krauss G. The XPC-HR23B complex displays high affinity and specificity for damaged DNA in a true-equilibrium fluorescence assay. Biochemistry. 41:2002;6583-6587.
    • (2002) Biochemistry , vol.41 , pp. 6583-6587
    • Hey, T.1    Lipps, G.2    Sugasawa, K.3    Iwai, S.4    Hanaoka, F.5    Krauss, G.6
  • 12
    • 0026076553 scopus 로고
    • Complementation of DNA repair in xeroderma pigmentosum group A cell extracts by a protein with affinity for damaged DNA
    • Robins P., Jones C.J., Biggerstaff M., Lindahl T., Wood R.D. Complementation of DNA repair in xeroderma pigmentosum group A cell extracts by a protein with affinity for damaged DNA. EMBO J. 10:1991;3912-3913.
    • (1991) EMBO J. , vol.10 , pp. 3912-3913
    • Robins, P.1    Jones, C.J.2    Biggerstaff, M.3    Lindahl, T.4    Wood, R.D.5
  • 14
    • 0027483739 scopus 로고
    • Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA
    • Jones C.J., Wood R.D. Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA. Biochemistry. 32:1993;12096-12104.
    • (1993) Biochemistry , vol.32 , pp. 12096-12104
    • Jones, C.J.1    Wood, R.D.2
  • 15
    • 0035814930 scopus 로고    scopus 로고
    • Binding of XPA and RPA to damaged DNA investigated by fluorescence anisotropy
    • Hey T., Lipps G., Krauss G. Binding of XPA and RPA to damaged DNA investigated by fluorescence anisotropy. Biochemistry. 40:2001;2901-2910.
    • (2001) Biochemistry , vol.40 , pp. 2901-2910
    • Hey, T.1    Lipps, G.2    Krauss, G.3
  • 16
    • 0035796455 scopus 로고    scopus 로고
    • Double-check probing of DNA bending and unwinding by XPA-RPA: An architectural function in DNA repair
    • Missura M., Buterin T., Hindges R., Hübscher U., Kaspáková J., Brabec V., Naegeli H. Double-check probing of DNA bending and unwinding by XPA-RPA: an architectural function in DNA repair. EMBO J. 20:2001;3554-3564.
    • (2001) EMBO J. , vol.20 , pp. 3554-3564
    • Missura, M.1    Buterin, T.2    Hindges, R.3    Hübscher, U.4    Kaspáková, J.5    Brabec, V.6    Naegeli, H.7
  • 17
    • 0029840823 scopus 로고    scopus 로고
    • Recognition of DNA adducts by human nucleotide excision repair. Evidence for a thermodynamic probing mechanism
    • Gunz D., Hess M.T., Naegeli H. Recognition of DNA adducts by human nucleotide excision repair. Evidence for a thermodynamic probing mechanism. J. Biol. Chem. 271:1996;25089-25098.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25089-25098
    • Gunz, D.1    Hess, M.T.2    Naegeli, H.3
  • 18
    • 0035254673 scopus 로고    scopus 로고
    • Architecture of nucleotide excision repair complexes: DNA is wrapped by UvrB before and after damage recognition
    • Verhoeven E.E., Wyman C., Moolenaar G.F., Hoeijmakers J.H., Goosen N. Architecture of nucleotide excision repair complexes: DNA is wrapped by UvrB before and after damage recognition. EMBO J. 20:2001;601-611.
    • (2001) EMBO J. , vol.20 , pp. 601-611
    • Verhoeven, E.E.1    Wyman, C.2    Moolenaar, G.F.3    Hoeijmakers, J.H.4    Goosen, N.5
  • 20
    • 0030596081 scopus 로고    scopus 로고
    • Scanning force microscopy of DNA deposited onto mica: Equilibration versus kinetic trapping studied by statistical polymer chain analysis
    • Rivetti C., Guthold M., Bustamante C. Scanning force microscopy of DNA deposited onto mica: equilibration versus kinetic trapping studied by statistical polymer chain analysis. J. Mol. Biol. 264:1996;919-932.
    • (1996) J. Mol. Biol. , vol.264 , pp. 919-932
    • Rivetti, C.1    Guthold, M.2    Bustamante, C.3
  • 21
    • 0029870677 scopus 로고    scopus 로고
    • Reaction mechanism of human DNA repair excision nuclease
    • Mu D., Hsu D.S., Sancar A. Reaction mechanism of human DNA repair excision nuclease. J. Biol. Chem. 271:1996;8285-8294.
    • (1996) J. Biol. Chem. , vol.271 , pp. 8285-8294
    • Mu, D.1    Hsu, D.S.2    Sancar, A.3
  • 22
    • 0032491461 scopus 로고    scopus 로고
    • Scanning force microscopy of Escherichia coli RNA polymerase-sigma54 holoenzyme complexes with DNA in buffer and in air
    • Schulz A., Mucke N., Langowski J., Rippe K. Scanning force microscopy of Escherichia coli RNA polymerase-sigma54 holoenzyme complexes with DNA in buffer and in air. J. Mol. Biol. 283:1998;821-836.
    • (1998) J. Mol. Biol. , vol.283 , pp. 821-836
    • Schulz, A.1    Mucke, N.2    Langowski, J.3    Rippe, K.4
  • 23
    • 0028631162 scopus 로고
    • DNA bending by Cro protein in specific and nonspecific complexes: Implications for protein site recognition and specificity
    • Erie D.A., Schultz H.C., Bustamante C. DNA bending by Cro protein in specific and nonspecific complexes: implications for protein site recognition and specificity. Science. 266:1994;1562-1566.
    • (1994) Science , vol.266 , pp. 1562-1566
    • Erie, D.A.1    Schultz, H.C.2    Bustamante, C.3
  • 24
    • 0033215330 scopus 로고    scopus 로고
    • DNA bending by photolyase in specific and non-specific complexes studied by atomic force microscopy
    • van Noort J., Orsini F., Eker A., Wyman C., de Grooth B., Greve J. DNA bending by photolyase in specific and non-specific complexes studied by atomic force microscopy. Nucleic Acids Res. 27:1999;3875-3880.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 3875-3880
    • Van Noort, J.1    Orsini, F.2    Eker, A.3    Wyman, C.4    De Grooth, B.5    Greve, J.6
  • 25
    • 0034737426 scopus 로고    scopus 로고
    • The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA
    • Yokoi M., Masutani C., Maekawa T., Sugasawa K., Ohkuma Y., Hanaoka F. The xeroderma pigmentosum group C protein complex XPC-HR23B plays an important role in the recruitment of transcription factor IIH to damaged DNA. J. Biol. Chem. 275:2000;9870-9875.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9870-9875
    • Yokoi, M.1    Masutani, C.2    Maekawa, T.3    Sugasawa, K.4    Ohkuma, Y.5    Hanaoka, F.6
  • 26
    • 0035102950 scopus 로고    scopus 로고
    • Strong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled repairosome
    • Araujo S.J., Nigg E.A., Wood R.D. Strong functional interactions of TFIIH with XPC and XPG in human DNA nucleotide excision repair, without a preassembled repairosome. Mol. Cell. Biol. 21:2001;2281-2291.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 2281-2291
    • Araujo, S.J.1    Nigg, E.A.2    Wood, R.D.3
  • 28
    • 0036012799 scopus 로고    scopus 로고
    • A molecular mechanism for DNA damage recognition by the xeroderma pigmentosum group C protein complex
    • Sugasawa K., Shimizu Y., Iwai S., Hanaoka F. A molecular mechanism for DNA damage recognition by the xeroderma pigmentosum group C protein complex. DNA Repair. 1:2002;95-107.
    • (2002) DNA Repair , vol.1 , pp. 95-107
    • Sugasawa, K.1    Shimizu, Y.2    Iwai, S.3    Hanaoka, F.4
  • 29
    • 0036682613 scopus 로고    scopus 로고
    • The presence of two UvrB subunits in the UvrAB complex ensures damage detection in both DNA strands
    • Verhoeven E.E.A., Wyman C., F Moolenaar G., Goosen N. The presence of two UvrB subunits in the UvrAB complex ensures damage detection in both DNA strands. EMBO J. 21:2002;4196-4205.
    • (2002) EMBO J. , vol.21 , pp. 4196-4205
    • Verhoeven, E.E.A.1    Wyman, C.2    Moolenaar, G.F.3    Goosen, N.4
  • 30
    • 0026536763 scopus 로고
    • The DNA helicase and adenosine triphosphatase activities of yeast Rad3 protein are inhibited by DNA damage. A potential mechanism for damage-specific recognition
    • Naegeli H., Bardwell L., Friedberg E.C. The DNA helicase and adenosine triphosphatase activities of yeast Rad3 protein are inhibited by DNA damage. A potential mechanism for damage-specific recognition. J. Biol. Chem. 267:1992;392-398.
    • (1992) J. Biol. Chem. , vol.267 , pp. 392-398
    • Naegeli, H.1    Bardwell, L.2    Friedberg, E.C.3
  • 31
    • 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
    • Naegeli H., Bardwell L., Friedberg E.C. 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. 32:1993;613-621.
    • (1993) Biochemistry , vol.32 , pp. 613-621
    • Naegeli, H.1    Bardwell, L.2    Friedberg, E.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.