Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites - PubMed (original) (raw)
. 2000 Jul 7;300(2):275-90.
doi: 10.1006/jmbi.2000.3857.
Affiliations
- PMID: 10873465
- DOI: 10.1006/jmbi.2000.3857
Stable binding of human XPC complex to irradiated DNA confers strong discrimination for damaged sites
D Batty et al. J Mol Biol. 2000.
Abstract
Nucleotide excision repair (NER) of DNA damage requires an efficient means of discrimination between damaged and non-damaged DNA. Cells from humans with xeroderma pigmentosum group C do not perform NER in the bulk of the genome and are corrected by XPC protein, which forms a complex with hHR23B protein. This complex preferentially binds to some types of damaged DNA, but the extent of discrimination in comparison to other NER proteins has not been clear. Recombinant XPC, hHR23B, and XPC-hHR23B complex were purified. In a reconstituted repair system, hHR23B stimulated XPC activity tenfold. Electrophoretic mobility-shift competition measurements revealed a 400-fold preference for binding of XPC-hHR23B to UV damaged over non-damaged DNA. This damage preference is much greater than displayed by the XPA protein. The discrimination power is similar to that determined here in parallel for the XP-E factor UV-DDB, despite the considerably greater molar affinity of UV-DDB for DNA. Binding of XPC-hHR23B to UV damaged DNA was very fast. Damaged DNA-XPC-hHR23B complexes were stable, with half of the complexes remaining four hours after challenge with excess UV-damaged DNA at 30 degrees C. XPC-hHR23B had a higher level of affinity for (6-4) photoproducts than cyclobutane pyrimidine dimers, and some affinity for DNA treated with cisplatin and alkylating agents. XPC-hHR23B could bind to single-stranded M13 DNA, but only poorly to single-stranded homopolymers. The strong preference of XPC complex for structures in damaged duplex DNA indicates its importance as a primary damage recognition factor in non-transcribed DNA during human NER.
Copyright 2000 Academic Press.
Similar articles
- The UV-damaged DNA binding protein mediates efficient targeting of the nucleotide excision repair complex to UV-induced photo lesions.
Moser J, Volker M, Kool H, Alekseev S, Vrieling H, Yasui A, van Zeeland AA, Mullenders LH. Moser J, et al. DNA Repair (Amst). 2005 May 2;4(5):571-82. doi: 10.1016/j.dnarep.2005.01.001. DNA Repair (Amst). 2005. PMID: 15811629 - In vivo destabilization and functional defects of the xeroderma pigmentosum C protein caused by a pathogenic missense mutation.
Yasuda G, Nishi R, Watanabe E, Mori T, Iwai S, Orioli D, Stefanini M, Hanaoka F, Sugasawa K. Yasuda G, et al. Mol Cell Biol. 2007 Oct;27(19):6606-14. doi: 10.1128/MCB.02166-06. Epub 2007 Aug 6. Mol Cell Biol. 2007. PMID: 17682058 Free PMC article. - Pre-steady-state binding of damaged DNA by XPC-hHR23B reveals a kinetic mechanism for damage discrimination.
Trego KS, Turchi JJ. Trego KS, et al. Biochemistry. 2006 Feb 14;45(6):1961-9. doi: 10.1021/bi051936t. Biochemistry. 2006. PMID: 16460043 Free PMC article. - Critical DNA damage recognition functions of XPC-hHR23B and XPA-RPA in nucleotide excision repair.
Thoma BS, Vasquez KM. Thoma BS, et al. Mol Carcinog. 2003 Sep;38(1):1-13. doi: 10.1002/mc.10143. Mol Carcinog. 2003. PMID: 12949838 Review. - The protein shuffle. Sequential interactions among components of the human nucleotide excision repair pathway.
Park CJ, Choi BS. Park CJ, et al. FEBS J. 2006 Apr;273(8):1600-8. doi: 10.1111/j.1742-4658.2006.05189.x. FEBS J. 2006. PMID: 16623697 Review.
Cited by
- Differing structures and dynamics of two photolesions portray verification differences by the human XPD helicase.
Fu I, Geacintov NE, Broyde S. Fu I, et al. Nucleic Acids Res. 2023 Dec 11;51(22):12261-12274. doi: 10.1093/nar/gkad974. Nucleic Acids Res. 2023. PMID: 37933861 Free PMC article. - ASH1L-MRG15 methyltransferase deposits H3K4me3 and FACT for damage verification in nucleotide excision repair.
Maritz C, Khaleghi R, Yancoskie MN, Diethelm S, BrĂ¼lisauer S, Ferreira NS, Jiang Y, Sturla SJ, Naegeli H. Maritz C, et al. Nat Commun. 2023 Jul 1;14(1):3892. doi: 10.1038/s41467-023-39635-7. Nat Commun. 2023. PMID: 37393406 Free PMC article. - Nucleotide excision repair: a versatile and smart toolkit.
Zhang X, Yin M, Hu J. Zhang X, et al. Acta Biochim Biophys Sin (Shanghai). 2022 May 25;54(6):807-819. doi: 10.3724/abbs.2022054. Acta Biochim Biophys Sin (Shanghai). 2022. PMID: 35975604 Free PMC article. Review. - Histone deacetylation regulates nucleotide excision repair through an interaction with the XPC protein.
Kusakabe M, Kakumu E, Kurihara F, Tsuchida K, Maeda T, Tada H, Kusao K, Kato A, Yasuda T, Matsuda T, Nakao M, Yokoi M, Sakai W, Sugasawa K. Kusakabe M, et al. iScience. 2022 Mar 9;25(4):104040. doi: 10.1016/j.isci.2022.104040. eCollection 2022 Apr 15. iScience. 2022. PMID: 35330687 Free PMC article. - Structural evolution of a DNA repair self-resistance mechanism targeting genotoxic secondary metabolites.
Mullins EA, Dorival J, Tang GL, Boger DL, Eichman BF. Mullins EA, et al. Nat Commun. 2021 Nov 26;12(1):6942. doi: 10.1038/s41467-021-27284-7. Nat Commun. 2021. PMID: 34836957 Free PMC article.
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Miscellaneous