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Cited by 428DNA Repair MechanismsGenomics and Rare DiseasesGenetic and rare skin diseases.

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Disorders of nucleotide excision repair: the genetic and molecular basis of heterogeneity

Cleaver, James E., Lam, Ernest T., Revet, Ingrid·2009·Nature Reviews Genetics
DOI 10.1038/nrg2663
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Abstract

Mutations in genes on the nucleotide excision repair pathway are associated with diseases, such as xeroderma pigmentosum, Cockayne syndrome and trichothiodystrophy, that involve skin cancer and developmental and neurological symptoms. These mutations cause the defective repair of damaged DNA and increased transcription arrest but, except for skin cancer, the links between repair and disease have not been obvious. Widely different clinical syndromes seem to result from mutations in the same gene, even when the mutations result in complete loss of function. The mapping of mutations in recently solved protein structures has begun to clarify the links between the molecular defects and phenotypes, but the identification of additional sources of clinical variability is still necessary.

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  1. De Weerd-Kastelein, E. A., Keijzer, W. & Bootsma, D. Genetic heterogeneity of xeroderma pigmentosum demonstrated by somatic cell hybridization. Nature New Biol. 238, 80–83 (1972). · DOI
  2. Wood, R. D., Mitchell, M., Sgouros, J. & Lindahl, T. Human DNA repair genes. Science 291, 1284–1289 (2001). · DOI
  3. Kraemer, K. H., Lee, M. M. & Scotto, J. Xeroderma pigmentosum. Cutaneous, ocular and neurological abnormalities in 830 published cases. Arch. Dermatol. 123, 241–250 (1987). This paper describes the time course of onset of clinical symptoms, including photosensitivity and cancer, in a large cohort of patients with XP. It clearly shows the early onset and increased level of skin cancer in most patients. · DOI
  4. Thompson, L. H. in DNA Repair in Higher Eukaryotes Vol. 2 (eds Nickoloff, J. A. & Hoekstra, M.) 335–393 (Humana, Totowa, 1998). · DOI
  5. Cleaver, J. E. & Revet, I. Clinical implications of the basic defects in Cockayne syndrome and xeroderma pigmentosum and the DNA lesions responsible for cancer, neurodegeneration and aging. Mech. Ageing Dev. 129, 492–497 (2008). · DOI
  6. Johnson, R. E., Kondratick, C. M., Prakash, S. & Prakash, L. hRAD30 mutations in the variant form of xeroderma pigmentosum. Science 264, 263–265 (1999). · DOI · Paper page
  7. Masutani, C. et al. The XPV (xeroderma pigmentosum variant) gene encodes human DNA polymerase η. Nature 399, 700–704 (1999). · DOI · Paper page
  8. Kraemer, K. H., Lee, M. M., Andrews, A. D. & Lambert, W. C. The role of sunlight and DNA repair in melanoma and nonmelanoma skin cancer. The xeroderma pigmentosum paradigm. Arch. Dermatol. 130, 1018–1021 (1994). · DOI · Paper page
  9. Kleijer, W. J. et al. Incidence of DNA repair deficiency disorders in western Europe: xeroderma pigmentosum, Cockayne syndrome and trichothiodystrophy. DNA Repair (Amst.) 7, 744–750 (2008). · DOI
  10. Nishigori, C., Moriwaki, S., Takebe, H., Tanaka, T. & Imamura, S. Gene alterations and clinical characteristics of xeroderma pigmentosum group A patients in Japan. Arch. Dermatol. 130, 191–197 (1994). · DOI
  11. Cleaver, J. E. DNA repair deficiencies and cellular senescence are unrelated in xeroderma pigmentosum cell lines. Mech. Ageing Dev. 27, 189–196 (1984). · DOI
  12. Kraemer, K. H., Lee, M. M. & Scotto, J. DNA repair protects against cutaneous and internal neoplasia: evidence from xeroderma pigmentosum. Carcinogenesis 5, 511–514 (1984). · DOI · Paper page
  13. Sollitto, R. B., Kraemer, K. H. & DiGiovanna, J. J. Normal vitamin D levels can be maintained despite rigorous photoprotection: six years' experience with xeroderma pigmentosum. J. Am. Acad. Dermatol. 37, 942–947 (1997). · DOI
  14. Dixon, K. M. et al. Skin cancer prevention: a possible role of 1,25dihydroxyvitamin D3 and its analogs. J. Steroid Biochem. Mol. Biol. 97, 137–143 (2005). · DOI
  15. Spina, C. S. et al. Vitamin D and cancer. Anticancer Res. 26, 2515–2524 (2006).
  16. Wijnhoven, S. W., Hoogervorst, E. M., de Waard, H., van der Horst, G. T. & van Steeg, H. Tissue specific mutagenic and carcinogenic responses in NER defective mouse models. Mutat. Res. 614, 77–94 (2007). · DOI
  17. Nance, M. A. & Berry, S. A. Cockayne syndrome: review of 140 cases. Am. J. Med. Genet. 42, 68–84 (1992). This paper is an extensive description of the skin, neurological and developmental abnormalities in a large cohort of patients with CS. · DOI · Paper page
  18. Colella, S. et al. Alterations in the CSB gene in three Italian patients with the severe form of Cockayne syndrome (CS) but without clinical photosensitivity. Hum. Mol. Genet. 8, 935–941 (1999). · DOI
  19. Cleaver, J. E., Charles, W. C., McDowell, M., Karentz, D. & Thomas, G. H. in DNA Repair Mechanisms Vol. 35 (eds Bohr, V. A., Wasserman, K. & Kraemer, K. H.) 56–67 (Munksgaard, Copenhagen, 1992).
  20. Fujiwara, Y., Ichihashi, M., Kano, Y., Goto, K. & Shimuzu, K. A new human photosensitive subject with a defect in the recovery of DNA synthesis after ultraviolet-light irradiation. J. Invest. Dermatol. 77, 256–263 (1981). · DOI
  21. Itoh, T., Ono, T. & Yamaizumi, M. A new UV-sensitive syndrome not belonging to any complementation groups of xeroderma pigmentosum or Cockayne syndrome: siblings showing biochemical characteristics of Cockayne syndrome without typical clinical manifestations. Mutat. Res. 314, 233–248 (1994). · DOI
  22. Itoh, T., Fujiwara, Y., Ono, T. & Yamaizumi, M. UVs syndrome, a new general category of photosensitive disorder with defective DNA repair, is distinct from xeroderma pigmentosum variant and rodent complementation group I. Am. J. Hum. Genet. 56, 1267–1276 (1995).
  23. Gorodetsky, E., Calkins, S., Ahn, J. & Brooks, P. J. ATM, the Mre11/Rad50/Nbs1 complex, and topoisomerase I are concentrated in the nucleus of Purkinje neurons in the juvenile human brain. DNA Repair (Amst.) 6, 1698–1707 (2007). · DOI
  24. Laposa, R. R., Huang, E. J. & Cleaver, J. E. Increased apoptosis, p53 up-regulation, and cerebellar neuronal degeneration in repair-deficient Cockayne syndrome mice. Proc. Natl Acad. Sci. USA 104, 1389–1394 (2007). · DOI
  25. Mayne, L. V. & Lehmann, A. R. Failure of RNA synthesis to recover after UV irradiation: an early defect in cells from individuals with Cockayne's syndrome and xeroderma pigmentosum. Cancer Res. 42, 1473–1478 (1982).
  26. Rapin, I. et al. Cockayne syndrome in adults: review with clinical and pathologic study of a new case. J. Child Neurol. 21, 991–1006 (2006). · DOI · Paper page
  27. Miyauchi, H. et al. Cockayne syndrome in two adult siblings. J. Am. Acad. Dermatol. 30, 329–335 (1994). · DOI
  28. Itin, P. H., Sarasin, A. & Pittelkow, M. R. Trichothiodystrophy: update on the sulfur-deficient brittle hair syndromes. J. Am. Acad. Dermatol. 44, 891–920 (2001). · DOI
  29. Liang, C. et al. Structural and molecular hair abnormalities in trichothiodystrophy. J. Invest. Dermatol. 126, 2210–2216 (2006). · DOI
  30. Faghri, S., Tamura, D., Kraemer, K. H. & Digiovanna, J. J. Trichothiodystrophy: a systematic review of 112 published cases characterizes a wide spectrum of clinical manifestations. J. Med. Genet. 45, 609–621 (2008). This paper is an extensive description of the skin, neurological and developmental abnormalities in a large cohort of patients with TTD. · DOI · Paper page
  31. Broughton, B. C. et al. Relationship between pyrimidine dimers, 6–4 photoproducts, repair synthesis and cell survival: studies using cells from patients with trichothiodystrophy. Mutat. Res. 235, 33–40 (1990). · DOI
  32. Ranish, J. A. et al. Identification of TFB5, a new component of general transcription and DNA repair factor IIH. Nature Genet. 36, 707–713 (2004). · DOI
  33. Giglia-Mari, G. et al. A new, tenth subunit of TFIIH is responsible for the DNA repair syndrome trichothiodystrophy group A. Nature Genet. 36, 714–719 (2004). · DOI
  34. Botta, E. et al. Mutations in the C7orf11 (TTDN1) gene in six nonphotosensitive trichothiodystrophy patients: no obvious genotype–phenotype relationships. Hum. Mutat. 28, 92–96 (2007). · DOI
  35. de Boer, J. et al. A mouse model for the basal transcription/DNA repair syndrome trichothiodystrophy. Mol. Cell 1, 981–990 (1998). · DOI
  36. de Boer, J., Donker, I., de Wit, J., Hoeijmakers, J. H. J. & Weeda, G. Disruption of the mouse xeroderma pigmentosum group D DNA repair/basal transcription gene results in preimplantation lethality. Cancer Res. 58, 89–94 (1998).
  37. Karentz, D. & Cleaver, J. E. Excision repair in xeroderma pigmentosum group C but not group D is clustered in a small fraction of the total genome. Mutat. Res. 165, 165–174 (1986).
  38. Scrima, A. et al. Structural basis of UV DNA-damage recognition by the DDB1–DDB2 complex. Cell 135, 1213–1223 (2009). · DOI · Paper page
  39. Zelle, B. & Lohman, P. H. Repair of UV-endonuclease-susceptible sites in the 7 complementation groups of xeroderma pigmentosum A through G. Mutat. Res. 62, 363–368 (1979). · DOI
  40. Tang, J. & Chu, G. Xeroderma pigmentosum complementation group E and UV-damaged DNA-binding protein. DNA Repair 1, 601–616 (2002). · DOI
  41. Cleaver, J. E., Feeney, L., Tang, J. Y. & Tuttle, P. Xeroderma pigmentosum group C in an isolated region of Guatemala. J. Invest. Dermatol. 127, 493–496 (2007). · DOI
  42. Khan, S. G. et al. XPC initiation codon mutation in xeroderma pigmentosum patients with and without neurological symptoms. DNA Repair (Amst.) 8, 114–125 (2009). · DOI
  43. Bernardes de Jesus, B. M., Bjørås, M., Coin, F. & Egly, J. M. Dissection of the molecular defects caused by pathogenic mutations in the DNA repair factor XPC. Mol. Cell. Biol. 28, 7225–7235 (2008). · DOI
  44. Hananian, J. & Cleaver, J. E. Xeroderma pigmentosum exhibiting neurological disorders and systemic lupus erythematosus. Clin. Genet. 17, 39–45 (1980). · DOI
  45. Chavanne, F. et al. Mutations in the XPC gene in families with xeroderma pigmentosum and consequences at the cell, protein, and transcript levels. Cancer Res. 60, 1974–1982 (2000).
  46. Khan, S. G. et al. The human XPC DNA repair gene: arrangement, splice site information content and influence of a single nucleotide polymorphism in a splice acceptor site on alternative splicing and function. Nucleic Acids Res. 30, 3624–3631 (2002). · DOI
  47. Khan, S. G. et al. Two essential splice lariat branchpoint sequences in one intron in a xeroderma pigmentosum DNA repair gene: mutations result in reduced XPC mRNA levels that correlate with cancer risk. Hum. Mol. Genet. 13, 343–352 (2004). · DOI
  48. Emmert, S., Kobayashi, N., Khan, S. G. & Kraemer, K. H. The xeroderma pigmentosum group C gene leads to selective repair of cyclobutane pyrimidine dimers rather than 6–4 photoproducts. Proc. Natl Acad. Sci. USA 97, 2151–2156 (2000). · DOI
  49. Bunick, C. G., Miller, M. R., Fuller, B. E., Fanning, E. & Chazin, W. J. Biochemical and structural domain analysis of xeroderma pigmentosum complementation group C protein. Biochemistry 45, 14965–14979 (2006). · DOI
  50. Khan, S. G. et al. Reduced XPC DNA repair gene mRNA levels in clinically normal parents of xeroderma pigmentosum patients. Carcinogenesis 27, 84–94 (2006). · DOI
  51. Melis, J. P. et al. Mouse models for xeroderma pigmentosum group A and group C show divergent cancer phenotypes. Cancer Res. 68, 1347–1353 (2008). · DOI
  52. Yasuda, G. et al. In vivo destabilization and functional defects of the xeroderma pigmentosum C protein caused by a pathogenic missense mutation. Mol. Cell. Biol. 27, 6606–6614 (2007). · DOI
  53. Maillard, O., Solyom, S. & Naegeli, H. An aromatic sensor with aversion to damaged strands confers versatility to DNA repair. PloS Biol. 5, e79 (2007). · DOI
  54. Min, J. H. & Pavletich, N. P. Recognition of DNA damage by the Rad4 nucleotide excision repair protein. Nature 449, 570–575 (2007). · DOI
  55. Sugasawa, K. et al. UV-induced ubiquitylation of XPC protein mediated by UV-DDB–ubiquitin ligase complex. Cell 121, 387–400 (2005). · DOI · Paper page
  56. Sugasawa, K. & Hanaoka, F. Sensing of DNA damage by XPC/Rad4: one protein for many lesions. Nature Struct. Mol. Biol. 14, 887–888 (2007). · DOI
  57. Groisman, R. et al. The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage. Cell 113, 357–367 (2003). · DOI
  58. Bregman, D. B. et al. UV-induced ubiquitination of RNA polymerase II: a novel modification deficient in Cockayne syndrome cells. Proc. Natl Acad. Sci. USA 93, 11586–11590 (1996). · DOI
  59. Svejstrup, J. Q. Rescue of arrested RNA polymerase II complexes. J. Cell Sci. 116, 447–451 (2003). · DOI
  60. Tantin, D., Kansal, A. & Carey, M. Recruitment of the putative repair coupling factor CSB/ERCC6 to RNA polymerase elongation complex. Mol. Cell. Biol. 17, 6803–6814 (1997). · DOI
  61. Lehmann, A. R., Kirk-Bell, S. & Mayne, L. Abnormal kinetics of DNA synthesis in ultraviolet light-irradiated cells from patients with Cockayne's syndrome. Cancer Res. 39, 4237–4241 (1979).
  62. Licht, C. L., Stevnser, T. & Bohr, V. A. Cockayne syndrome group B cellular and biochemical functions. Am. J. Hum. Genet. 73, 1217–1239 (2003). This paper provides an extensive review of the cellular properties of CS cells in culture, including their sensitivity to DNA-damaging agents, repair deficiencies and protein interactions. · DOI
  63. Ljungman, M. & Zhang, F. Blockage of RNA polymerase as a possible trigger for u.v. light-induced apoptosis. Oncogene 13, 823–831 (1996).
  64. Parris, C. H. & Kraemer, K. H. Ultraviolet-light induced mutations in Cockayne syndrome cells are primarily caused by cyclobutane dimer photoproducts while repair of other photoproducts is normal. Proc. Natl Acad. Sci. USA 90, 7260–7264 (1993). · DOI · Paper page
  65. Yuan, X., Feng, W., Imhof, A., Grummt, I. & Zhou, Y. Activation of RNA polymerase I transcription by cockayne syndrome group B protein and histone methyltransferase G9a. Mol. Cell 27, 585–595 (2007). · DOI
  66. Balajee, A. S., Dianova, I. & Bohr, V. A. Oxidative damage-induced PCNA complex formation is efficient in xeroderma pigmentosum group A but reduced in Cockayne syndrome group B cells. Nucleic Acids Res. 27, 4476–4482 (1999). · DOI
  67. Frosina, G. Oxidatively damaged DNA repair defect in cockayne syndrome and its complementation by heterologous repair proteins. Curr. Med. Chem. 15, 940–953 (2008). · DOI
  68. Tuo, J., Jaruga, P., Rodriguez, H., Bohr, V. A. & Dizdaroglu, M. Primary fibroblasts of Cockayne syndrome patients are defective in cellular repair of 8-hydroxyguanine and 8-hydroxyadenine resulting from oxidative stress. FASEB J. 17, 668–674 (2003). · DOI
  69. Niedernhofer, L. J., Daniels, J. S., Rouzer, C. A., Greene, R. E. & Marnett, L. J. Malondialdehyde, a product of lipid peroxidation, is mutagenic in human cells. J. Biol. Chem. 278, 31426–31433 (2003). · DOI
  70. Maddukuri, L. et al. Cockayne syndrome group B protein is engaged in processing of DNA adducts of lipid peroxidation product trans-4-hydroxy-2-nonenal. Mutat. Res. 666, 23–31 (2009). · DOI
  71. de Waard, H. et al. Different effects of CSA and CSB deficiency on sensitivity to oxidative damage. Mol. Cell. Biol. 24, 7941–7948 (2004). · DOI
  72. Kyng, K. J. et al. The transcriptional response after oxidative stress is defective in Cockayne syndrome group B cells. Oncogene 22, 1135–1149 (2003). · DOI
  73. Citterio, E. et al. Biochemical and biological characterization of wild-type and ATPase-deficient Cockayne syndrome B repair protein. J. Biol. Chem. 273, 11844–11851 (1998). · DOI
  74. Selby, C. P. & Sancar, A. Cockayne syndrome group B protein enhances elongation by RNA polymerase II. Proc. Natl Acad. Sci. USA 94, 11205–11209 (1997). · DOI
  75. Newman, J. C., Bailey, A. D. & Weiner, A. M. Cockayne syndrome group B protein (CSB) plays a general role in chromatin maintenance and remodeling. Proc. Natl Acad. Sci. USA 103, 9613–9618 (2006). · DOI
  76. Muftuoglu, M. et al. Cockayne syndrome group B protein has novel strand annealing and exchange activities. Nucleic Acids Res. 34, 295–304 (2006). · DOI
  77. Frontini, M. & Proietti- De-Santis, L. Cockayne syndrome B protein (CSB): linking p53, HIF-1 and p300 to robustness, lifespan, cancer and cell fate decisions. Cell Cycle 8, 693–696 (2009). · DOI
  78. Imam, S. Z. et al. Cockayne syndrome protein B interacts with and is phosphorylated by c-Abl tyrosine kinase. Nucleic Acids Res. 35, 4941–4951 (2007). · DOI
  79. Thorsland, T. et al. Cooperation of the Cockayne syndrome group B protein and poly(ADP-ribose) polymerase I in the response to oxidative damage. Mol. Cell. Biol. 25, 7625–7636 (2005). · DOI
  80. Mallery, D. L. et al. Molecular analysis of mutations in the CSB (ERCC6) gene in patients with Cockayne syndrome. Am. J. Hum. Genet. 62, 77–85 (1998). · DOI
  81. Khobta, A., Kitsera, N., Speckmann, B. & Epe, B. 8-Oxoguanine DNA glycosylase (Ogg1) causes a transcriptional inactivation of damaged DNA in the absence of functional Cockayne syndrome B (Csb) protein. DNA Repair (Amst.) 8, 309–317 (2009). · DOI
  82. Stevnsner, T. et al. Mitochondrial repair of 8-oxoguanine is deficient in Cockayne syndrome group B. Oncogene 21, 8675–8682 (2002). · DOI
  83. Colella, S., Nardo, T., Botta, E., Lehmann, A. R. & Stefanini, M. Identical mutations in the CSB gene associated with either Cockayne syndrome or the DeSanctis–Cacchione variant of xeroderma pigmentosum. Hum. Mol. Genet. 9, 1171–1175 (2000). · DOI
  84. Horibata, K. et al. Complete absence of Cockayne syndrome group B gene product gives rise to UV-sensitive syndrome but not Cockayne syndrome. Proc. Natl Acad. Sci. USA 101, 15410–15415 (2004). · DOI
  85. Laugel, V. et al. COFS syndrome: three additional cases with CSB mutations, new diagnostic criteria and an approach to investigation. J. Med. Genet. 45, 564–571 (2008). · DOI
  86. Newman, J. C., Bailey, A. D., Fan, H. Y., Pavelitz, T. & Weiner, A. M. An abundant evolutionarily conserved CSB–PiggyBac fusion protein expressed in Cockayne syndrome. PLoS Genet. 4, e1000031 (2008). · DOI
  87. Laugel, V. et al. Deletion of 5′ sequences of the CSB gene provides insight into the pathophysiology of Cockayne syndrome. Eur. J. Hum. Genet. 16, 320–327 (2008). · DOI
  88. Nardo, T. et al. A UV-sensitive syndrome patient with a specific CSA mutation reveals separable roles for CSA in response to UV and oxidative DNA damage. Proc. Natl Acad. Sci. USA 106, 6209–6214 (2009). · DOI
  89. Hayashi, M. et al. Oxidative stress and disturbed glutamate transport in hereditary nucleotide repair disorders. J. Neuropathol. Exp. Neurol. 60, 350–356 (2001). · DOI
  90. Vuillaume, M. et al. Striking differences in cellular catalase activity between two DNA repair-deficient diseases: xeroderma pigmentosum and trichothiodystrophy. Carcinogenesis 13, 321–328 (1992). · DOI
  91. Kuraoka, I. et al. RNA polymerase II bypasses 8-oxoguanine in the presence of transcription elongation factor TFIIS. DNA Repair (Amst.) 6, 841–851 (2007). · DOI
  92. Kathe, S. D., Shen, G. P. & Wallace, S. S. Single-stranded breaks in DNA but not oxidative DNA base damages block transcriptional elongation by RNA polymerase II in HeLa cell nuclear extracts. J. Biol. Chem. 279, 18511–18520 (2004). · DOI
  93. Brooks, P. J. The case for 8,5′-cyclopurine-2′-deoxynucleosides as endogenous DNA lesions that cause neurodegeneration in xeroderma pigmentosum. Neuroscience 145, 1407–1417 (2007). · DOI
  94. Botta, E. et al. Analysis of mutations in the XPD gene in Italian patients with trichothiodystrophy: site of mutation correlates with repair deficiency, but gene dosage appears to determine clinical severity. Am. J. Hum. Genet. 63, 1036–1048 (1998). · DOI
  95. Stefanini, M. et al. Genetic heterogeneity of the excision repair defect associated with trichothiodystrophy. Carcinogenesis 14, 1101–1105 (1993). · DOI
  96. Cleaver, J. E. Splitting hairs — discovery of a new DNA repair and transcription factor for the human disease trichothiodystrophy. DNA Repair 4, 285–287 (2005). · DOI
  97. Vitorino, M. et al. Solution structure and self-association properties of the p8 TFIIH subunit responsible for trichothiodystrophy. J. Mol. Biol. 368, 473–480 (2007). · DOI
  98. Kainov, D. E., Vitorino, M., Cavarelli, J., Poterszman, A. & Egly, J.-M. Structural basis for group A trichothiodystrophy. Nature Struct. Mol. Biol. 15, 980–984 (2008). · DOI
  99. Taylor, E. M. et al. Xeroderma pigmentosum and trichothiodystrophy are associated with different mutations in the XPD (ERCC2) repair/transcription gene. Proc. Natl Acad. Sci. USA 94, 8658–8663 (1997). · DOI
  100. Liu, H. et al. Structure of the DNA repair helicase XPD. Cell 133, 801–812 (2008). · DOI
  101. Wolski, S. C. et al. Crystal structure of the FeS cluster-containing nucleotide excision repair helicase XPD. PLoS Biol. 6, 1332–1342 (2008). References 107–109 describe the crystal structures of three different archaean XPD homologues, which provide clues to the reasons why different mutations in the corresponding human protein can give rise to a wide range of clinical disorders through different changes of function. · DOI
  102. Dubaele, S. et al. Basal transcription defect discriminates between xeroderma pigmentosum and trichothiodystrophy in XPD patients. Mol. Cell 11, 1635–1646 (2003). · DOI
  103. Koonin, E. V. Escherichia coli dinG gene encodes a putative DNA helicase related to a group of eukaryotic helicases including Rad3 protein. Nucleic Acids Res. 21, 1497–1503 (1993). · DOI
  104. Coin, F. et al. Mutations in the XPD helicase gene result in XP and TTD phenotypes, preventing interaction between XPD and the p44 subunit of TFIIH. Nature Genet. 20, 184–188 (1998). · DOI
  105. Chen, D. et al. Activation of estrogen receptor α by S118 phosphorylation involves a ligand-dependent interaction with TFIIH and participation of CDK7. Mol. Cell 6, 127–137 (2000). · DOI
  106. Compe, E. et al. Dysregulation of the peroxisome proliferator-activated receptor target genes by XPD mutations. Mol. Cell. Biol. 25, 6065–6076 (2005). · DOI
  107. Ito, S. et al. XPG stabilizes TFIIH, allowing transactivation of nuclear receptors: implications for Cockayne syndrome in XP-G/CS patients. Mol. Cell 26, 231–243 (2007). · DOI
  108. Boyle, J. et al. Persistence of repair proteins at unrepaired DNA damage distinguishes diseases with ERCC2 (XPD) mutations: cancer-prone xeroderma pigmentosum vs. non-cancer-prone trichothiodystrophy. Hum. Mutat. 29, 1194–1208 (2008). · DOI
  109. Vermeulen, W. et al. A temperature-sensitive disorder in basal transcription and DNA repair in humans. Nature Genet. 27, 299–303 (2001). · DOI
  110. Berneburg, M. & Lehmann, A. R. Xeroderma pigmentosum and related disorders: defects in DNA repair and transcription. Adv. Genet. 43, 71–102 (2001). · DOI
  111. Broughton, B. C. et al. Two individuals with features of both xeroderma pigmentosum and trichothiodystrophy highlight the complexity of the clinical outcomes of mutations in the XPD gene. Hum. Mol. Genet. 10, 2539–2547 (2001). · DOI
  112. Fujimoto, M. et al. Two new XPD patients compound heterozygous for the same mutation demonstrate diverse clinical features. J. Invest. Dermatol. 125, 86–92 (2005). · DOI
  113. Gorgels, T. G. et al. Retinal degeneration and ionizing radiation hypersensitivity in a mouse model for Cockayne syndrome. Mol. Cell. Biol. 27, 1433–1441 (2007). · DOI
  114. van der Pluijm, I. et al. Impaired genome maintenance suppresses the growth hormone–insulin-like growth factor 1 axis in mice with Cockayne syndrome. PLoS Biol. 5, e2 (2006). · DOI
  115. Susa, D. et al. Congenital DNA repair deficiency results in protection against renal ischemia reperfusion injury in mice. Aging Cell 8, 192–200 (2009). · DOI
  116. Szabó, C. Roles of poly(ADP-ribose) polymerase activation in the pathogenesis of diabetes mellitus and its complications. Pharmacol. Res. 52, 60–71 (2005). · DOI
  117. Robbins, J. H., Brumback, R. A. & Moshell, A. N. Clinically asymptomatic xeroderma pigmentosum neurological disease in an adult: evidence for a neurodegeneration in later life caused by defective DNA repair. Eur. Neurol. 33, 188–190 (1993). · DOI
  118. Dizdaroglu, M. & Teebor, G. W. Targeted deletion of the genes encoding NTH1 and NEIL1 DNA N-glycosylases reveals the existence of novel carcinogenic oxidative damage to DNA. DNA Repair (Amst.) 8, 786–794 (2009). · DOI
  119. Klungland, A. & Bjelland, S. Oxidative damage to purines in DNA: role of mammalian Ogg1. DNA Repair (Amst.) 6, 481–488 (2007). · DOI
  120. Laposa, R. R., Feeney, L., Crowley, E., de Feraudy, S. & Cleaver, J. E. p53 suppression overwhelms DNA polymerase h deficiency in determining the cellular UV DNA damage response. DNA Repair 6, 1794–1804 (2007). · DOI
  121. Gueven, N. et al. Dramatic extension of tumor latency and correction of neurobehavioral phenotype in Atm-mutant mice with a nitroxide antioxidant. Free Radic. Biol. Med. 41, 992–1000 (2006). · DOI
  122. Reardon, J. T. & Sancar, A. Nucleotide excision repair. Prog. Nucleic Acid Res. Mol. Biol. 79, 183–235 (2005). This is an extensive review of the biochemistry of NER with special emphasis on the mechanisms by which proteins of low inherent affinity can have specificity in detecting and binding to damaged DNA. · DOI · Paper page
  123. Cleaver, J. E. & Mitchell, D. L. in Cancer Medicine Vol. 1 Ch. 17 (eds Kufe, D. W. et al.) 283–291 (BC Deckker, Ontario, 2006).
  124. Wang, Y. et al. Evidence of ultraviolet type mutations in xeroderma pigmentosum melanomas. Proc. Natl Acad. Sci. USA 106, 6279–6284 (2009). · DOI
  125. Suarez, H. G. et al. Activated oncogenes in human skin tumors from a repair-deficient syndrome, xeroderma pigmentosum. Cancer Res. 49, 1223–1228 (1989).
  126. Giglia, G. et al. p53 mutations in skin and internal tumors of xeroderma pigmentosum patients belonging to the complementation group C. Cancer Res. 58, 4402–4409 (1998).
  127. Bodak, N. et al. High levels of patched gene mutations in basal-cell carcinomas from patients with xeroderma pigmentosum. Proc. Natl Acad. Sci. USA 96, 5117–5122 (1999). · DOI
  128. Niedernhofer, L. J. et al. A new progeroid syndrome reveals that genotoxic stress suppresses the somatotroph axis. Nature 444, 1038–1043 (2006). · DOI · Paper page
  129. Yang, L. J., Jiang, H. & Rangel, K. M. RNA polymerase II stalled on a DNA template during transcription elongation is ubiquitinated and the ubiquitination facilitates displacement of the elongation complex. Int. J. Oncol. 22, 683–689 (2003).
  130. Sugasawa, K. et al. Xeroderma pigmentosum group C protein complex is the initiator of global nucleotide excision repair. Mol. Cell 2, 223–232 (1998). · DOI · Paper page
  131. Wakasugi, M. & Sancar, A. Assembly, subunit composition, and footprint of human DNA repair excision nuclease. Proc. Natl Acad. Sci. USA 95, 6669–6674 (1998). · DOI
  132. Oh, K. S., Imoto, K., Boyle, J., Khan, S. G. & Kraemer, K. H. Influence of XPB helicase on recruitment and redistribution of nucleotide excision repair proteins at sites of UV-induced DNA damage. DNA Repair (Amst.) 6, 1359–1370 (2007). · DOI
  133. Coin, F., Oksenych, V. & Egly, J.-M. Distinct roles for the XPB/p52 and XPD/p44 subcomplexes of TFIIH in damaged DNA opening during nucleotide excision repair. Mol. Cell 26, 245–256 (2007). · DOI
  134. Staresincic, L. et al. Coordination of dual incision and repair synthesis in human nucleotide excision repair. EMBO J. 28, 1111–1120 (2009). · DOI · Paper page
  135. Scharer, O. D. Achieving broad substrate specificity in damage recognition by binding to accessible nondamaged DNA. Cell 28, 184–186 (2007). This paper describes the ribbon structure of the DNA-binding region of yeast Rad4 and shows that the mechanism of damage recognition involves the extrusion of the damaged site to an extrahelical position.

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Metadata

Authors
Cleaver, J. E., Lam, E. T., & Revet, I.
Affiliations
University of California, San Francisco (US)
Corresponding author
Cleaver, James E.
ORCID
Cleaver, James E.
Venue
Nature Reviews Genetics
Publisher
Springer Science and Business Media LLC
Published
2009-10-07
Volume
10
Issue
11
Pages
756-768
ISSN
  • 1471-0056 (ISSN-L)
  • 1471-0064
DOI
10.1038/nrg2663
OpenAlex
W2026776398
Cited by
428
References
0
Citations by year
2026: 7 · 2025: 16 · 2024: 9 · 2023: 14 · 2022: 23 · 2021: 20 · 2020: 30 · 2019: 24 · 2018: 24 · 2017: 29 · 2016: 35 · 2015: 30 · 2014: 43 · 2013: 38 · 2012: 33
FWCI
2.12
Type
journal article
Language
en
Open access
closed
Licence
Locations
  • Nature Reviews Genetics (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Iris O'Brien Foundation
  • National Institute of Neurological Disorders and Stroke (R01NS052781)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genomics and Rare Diseases
  • Health Sciences › Medicine › Dermatology › Genetic and rare skin diseases.
Keywords
nucleotide excision repair, genetic heterogeneity, xeroderma pigmentosum, Cockayne syndrome, trichothiodystrophy, transcription arrest, DNA repair deficiency, skin cancer predisposition, neurological symptoms, developmental abnormalities, loss-of-function mutations, protein structure, genotype-phenotype correlation
MeSH terms
Animals, Cockayne Syndrome, DNA Repair, Humans, Genetic Variation, Xeroderma Pigmentosum, Trichothiodystrophy Syndromes

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