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Molecular Determinants of Damage Recognition by Mammalian Nucleotide Excision Repair

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Mechanisms of DNA Damage Recognition in Mammalian Cells

Part of the book series: Molecular Biology Intelligence Unit ((MBIU))

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Abstract

The mechanism by which XPA, RPA, XPC-HHR23B, TFIIH and possibly other factors discriminate a wide range of chemically dissimilar DNA lesions as substrates of mammalian nucleotide excision repair is poorly understood. The striking versatility of nucleotide excision repair led to the assumption that its recognition subunits detect conformational changes imposed on DNA at sites of damage rather than specific base modifications.1-5 As indicated in Figure 7.1, this hypothesis was prompted by the observation that many base lesions alter the helical parameters of DNA by inducing kinks,6,7 bends8 or localized unwinding,9 suggesting that damage-induced conformational distortion may constitute an important determinant of recognition by the nucleotide excision repair system.

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References

  1. Sancar A. Excision repair in mammalian cells. J Biol Chem 1995; 270:15915–15918.

    Google Scholar 

  2. Sancar A. DNA excision repair. Annu Rev Biochem 1996; 65:43–81.

    Article  Google Scholar 

  3. Hoeijmakers JHJ. Nucleotide excision repair II: from yeast to mammals. Trends Genet 1993; 9:211–217.

    Article  Google Scholar 

  4. Grossman L, Thiangalingam S. Nucleotide excision repair, a tracking mechanism in search of damage. J Biol Chem 1993; 268:16871–16874.

    Google Scholar 

  5. Van Houten B. Nucleotide excision repair in Escherichia coli. Microbiol Rev 1990; 54:18–51.

    Google Scholar 

  6. Kim J-K, Choi B-S. The solution structure of DNA duplex-decamer containing the (6-4) photoproduct of thymidylyl(3′→5′)thymidine by NMR and relaxation matrix refinement. Eur J Biochem 1995; 228:849–854.

    Article  Google Scholar 

  7. Takahara PM, Rosenzweig AC, Frederick CA et al. Crystal structure of doublestranded DNA containing the major adduct of the anticancer drug cisplatin. Nature 1995; 377:649–652.

    Article  Google Scholar 

  8. Lee C-S, Sun D, Kizu R et al. Determination of the structural features of (+)-CC-1065 that are responsible for bending and winding of DNA. Chem Res Toxicol 1991; 4:203–213.

    Article  Google Scholar 

  9. Xu R, Birke S, Carberry SE et al. Differences in unwinding of supercoiled DNA induced by the two enantiomers of antibenzo[a]pyrene diol epoxide. Nucleic Acids Res 1992; 20:6167–6176.

    Article  Google Scholar 

  10. Krugh TR, Graves DE, Stone MP. Twodimensional NMR studies on the anthramycin-d(ATGCAT)2 adduct. Biochemistry 1989; 28:9988–9994.

    Article  Google Scholar 

  11. Crothers DM, Haran TE, Nadeau JG. Intrinsically bent DNA. J Biol Chem 1990; 265:7093–7096.

    Google Scholar 

  12. Hagerman PJ. Sequence-directed curvature of DNA. Annu Rev Biochem 1990; 59:755–781.

    Article  Google Scholar 

  13. Gunz D, Hess MT, Naegeli H. Recognition of DNA adducts by human nucleotide excision repair: evidence for a thermodynamic probing mechanism. J Biol Chem 1996; 271:25089–25098.

    Article  Google Scholar 

  14. O’Handley SF, Sanford SG, Xu R et al. Structural characterization of an N-acetyl-2-aminofluorene (AAF) modified DNA oligomer by NMR, energy minimization, and molecular dynamics. Biochemistry 1993; 32:2481–2497.

    Article  Google Scholar 

  15. Garcia A, Lambert IB, Fuchs RP. DNA adduct-induced stabilization of slipped frameshift intermediates within repetitive sequences: implications for mutagenesis. Proc Natl Acad Sci USA 1993; 90:5989–5993.

    Article  Google Scholar 

  16. Zou Y, Liu T-M, Geacintov NE et al. Interaction of the UvrABC nuclease system with a DNA duplex containing a single stereoisomer of dG-(+)-or dG(-)-anti-BPDE. Biochemistry 1995; 34:13582–13593.

    Article  Google Scholar 

  17. Taylor J-S, Garrett DS, Brockie IR et al. 1H NMR assignment and melting temperature study of cis-syn and trans-syn thymine dimer containing duplexes of d(CGTATTATGC) (GCATAATACG). Biochemistry 1990; 29:8858–8866.

    Article  Google Scholar 

  18. Shi YB, Hearst JE. Thermostability of double-stranded deoxyribonucleic acids: effects of covalent additions of a psoralen. Biochemistry 1986; 25:5895–5902.

    Article  Google Scholar 

  19. Shi Y-B, Griffith J, Hearst JE. Evidence for structural deformation of the DNA helix by a psoralen diadduct but not by a monoadduct. Nucleic Acids Res 1988; 16:8945–8952.

    Article  Google Scholar 

  20. Hurley LH, Petrusek R. Proposed structure of the anthramycin-DNA adduct. Nature 1979; 282:529–531.

    Article  Google Scholar 

  21. Swenson DH, Li LH, Hurley, LH. Mechanism of interaction of CC-1065 (NSC 298223) with DNA. Cancer Res 1982; 42:2821–2828.

    Google Scholar 

  22. Schwartz A, Marrot L, Leng M. The DNA bending by acetylaminofluorene residues and by apurinic sites. J Mol Biol 1989; 207:445–450.

    Article  Google Scholar 

  23. de los Santos C, Cosman M, Hingerty BE et al. Influence of benzo[a]pyrene diol epoxide chirality on solution conformations of DNA covalent adducts: the (-)-trans-anti-[BP]GC adduct structure and comparison with the (+)-trsuis-anti-[BP]GC enantiomer. Biochemistry 1992; 31:5245–5252.

    Article  Google Scholar 

  24. Cosman M, de los Santos C, Fiala R et al. Solution conformation of the (+)-cis-anti-[BP]dG adduct in a DNA duplex: intercalation of the covalently attached benzo[a]pyrenyl ring into the helix and displacement of the modified deoxyguanosine. Biochemistry 1993; 32:4146–4155.

    Google Scholar 

  25. Cosman M, Hingerty BE, Luneva N et al. Solution conformation of the (-)-cisanti-benzo[a]pyrenyl-dG adduct opposite dC in a DNA duplex: intercalation of the covalently attached BP ring into the helix with base displacement of the modified deoxyguanosine into the major groove. Biochemistry 1996; 35:9850–9863.

    Article  Google Scholar 

  26. Hearst JE, Isaacs ST, Kanne D et al. The reaction of psoralens with deoxyribonucleic acid. Quart Rev Biophys 1984; 17:1–44.

    Article  Google Scholar 

  27. Spielmann HP, Dwyer TJ, Hearst JE et al. Solution structures of psoralen monoadducted and cross-linked DNA oligomers by NMR spectroscopy and restrained molecular dynamics. Biochemistry 1995; 34:12937–12953.

    Article  Google Scholar 

  28. Reynolds VL, McGovren JP, Hurley LH. The chemistry, mechanism of action and biological properties of CC-1065, a potent antitumor antibiotic. J Antibiotics 1986; 39:319–334.

    Article  Google Scholar 

  29. Gunz D, Naegeli H. A noncovalent binding-translocation mechanism for site-specific CC-1065-DNA recognition. Biochem Pharmacol 1996; 52:447–453.

    Article  Google Scholar 

  30. Hess MT, Gunz D, Naegeli H. A repair competition assay to assess recognition by human nucleotide excision repair. Nucleic Acids Res 1996; 24:824–828.

    Article  Google Scholar 

  31. Manley JL, Fire A, Samuels M et al. In vitro transcription: whole cell extract. Meth Enzymol 1983; 101:568–582.

    Article  Google Scholar 

  32. Wood RD, Robins P, Lindahl T. Complementation of the xeroderma pigmentosum DNA repair defect in cell-free extracts. Cell 1988; 53:97–106.

    Article  Google Scholar 

  33. Challberg MD, Kelly TJ. Animal virus DNA replication. Annu Rev Biochem 1989; 58:671–717.

    Article  Google Scholar 

  34. Jones CJ, Wood RD. Preferential binding of the xeroderma pigmentosum group A complementing protein to damaged DNA. Biochemistry 1993; 32:12096–12104.

    Article  Google Scholar 

  35. He Z, Henricksen LA, Wold MS et al. RPA involvement in the damage-recognition and incision steps of nucleotide excision repair. Nature 1995; 374:566–568.

    Article  Google Scholar 

  36. Li L, Lu X, Peterson CA et al. An interaction between the DNA repair factor XPA and replication protein A appears essential for nucleotide excision repair. Mol Cell Biol 1995; 15:5396–5402.

    Google Scholar 

  37. Huang J-C, Hsu DS, Kazantsev A et al. Substrate spectrum of human exci-nuclease: repair of abasic sites, methylated bases, mismatches, and bulky adducts. Proc Natl Acad Sci USA 1994; 91:12213–12217.

    Article  Google Scholar 

  38. Nazimiec M, Grossman L, Tang M-S. A comparison of the rates of reaction and function of UVRB in UVRAB-mediated anthramycin-N 2-guanine-DNA repair. J Biol Chem 1992; 267:24716–24724.

    Google Scholar 

  39. Tang M-S, Lee C-S, Doisy R et al. Recognition and repair of the CC-1065-(N3-adenine)-DNA adduct by the UVRABC nucleases. Biochemistry 1988; 27:893–901.

    Article  Google Scholar 

  40. Selby CP, Sancar A. ABC Excinuclease incises both 5′ and 3′ to the CC-1065-DNA adduct and its incision activity is stimulated by DNA helicase II and DNA polymerase I. Biochemistry 1988; 27:7184–7188.

    Article  Google Scholar 

  41. Mu D, Park C-H, Matsunaga T et al. Reconstitution of human DNA repair excision nuclease in a highly defined system. J Biol Chem 1995; 270:2415–2418.

    Article  Google Scholar 

  42. Hess MT, Schwitter U, Petretta M et al. Site-specific DNA substrates for human excision repair: comparison between deoxyribose and base adducts. Chem Biol 1996; 3:121–128.

    Article  Google Scholar 

  43. Huang J-C, Svoboda DL, Reardon JT et al. Human nucleotide excision nuclease removes thymine dimers from DNA by incising the 22nd phosphodiester bond 5′ and the 6th phosphodiester bond 3′ to the photodimer. Proc Natl Acad Sci USA 1992; 89:3664–3668.

    Article  Google Scholar 

  44. Newbold RF, Brookes P. Exceptional mutagenicity of a benzo [a] pyrene diol epoxide in cultured mammalian cells. Nature 1976; 261:52–54.

    Article  Google Scholar 

  45. Buening MK, Wislocki PG, Levin W et al. Tumorigenicity of the optical enantiomers of the diastereomeric benzo [a] pyrene 7,8-diol-9,10-epoxides in newborn mice: exceptional activity of (+)-7β,8α-dihydroxy-9α, 1 Oα-epoxy-7,8,9,10-tetrahydrobenzo-[a]pyrene. Proc Natl Acad Sci USA 1978; 75:5358–5361.

    Article  Google Scholar 

  46. Cosman M, de los Santos C, Fiala R et al. Solution conformation of the major adduct between the carcinogen (+)-anti-benzo[a]pyrene diol epoxide and DNA. Proc Natl Acad Sci USA 1992; 89:1914–1918.

    Article  Google Scholar 

  47. Slaga TJ, Bracken WJ, Gleason G et al. Marked differences in the skin tumor-initiating activities of the optical enantiomers of the diastereomeric benzo [a] pyrene 7,8-diol-9,10-epoxides. Cancer Res 1979; 394:67–71.

    Google Scholar 

  48. Wood AW, Chang RL, Levin W et al. Differences in mutagenicity of the optical enantiomers of the diastereomeric benzo[a]pyrene 7,8-diol-9,10-epoxides. Biochem. Biophys Res Commun 1977; 77:1389–1396.

    Article  Google Scholar 

  49. Wei SJC, Chang RL, Wong C-Q et al. Dose-dependent differences in the profile of mutations induced by an ultimate carcinogen from benzo[a] pyrene. Proc Natl Acad Sci USA 1991; 88:11227–11230.

    Article  Google Scholar 

  50. Stevens CW, Bouck N, Burgess JA et al. Benzo[a] pyrene diol-epoxides: different mutagenic efficiency in human and bacterial cells. Mutat Res 1985; 152:5–14.

    Article  Google Scholar 

  51. Shibutani S, Margulis LA, Geacintov NE et al. Translesion synthesis on a DNA template containing a single stereoisomer of dG-(+)-or dG(-)-anti-BVDE (7,8-dihydroxy-anti-9,10-epoxy-7.8,9,10-tetra-hydrobenzo [a] pyrene. Biochemistry 1993; 32:7531–7541.

    Article  Google Scholar 

  52. Suh M, Ariese F, Small GJ et al. Formation and persistence of benzo[a]pyrene-DNA adducts in mouse epidermis in vivo: importance of adduct conformation. Carcinogenesis 1995; 16:2561–2569.

    Article  Google Scholar 

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  1. Institute of Pharmacology and Toxicology, University of Zürich-Tierspital, Zürich, Switzerland

    Hanspeter Naegeli D.V.M.

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  1. Hanspeter Naegeli D.V.M.
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Naegeli, H. (1997). Molecular Determinants of Damage Recognition by Mammalian Nucleotide Excision Repair. In: Mechanisms of DNA Damage Recognition in Mammalian Cells. Molecular Biology Intelligence Unit. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6468-9_7

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  • DOI: https://doi.org/10.1007/978-1-4684-6468-9_7

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-6470-2

  • Online ISBN: 978-1-4684-6468-9

  • eBook Packages: Springer Book Archive

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