• Medientyp: E-Artikel
  • Titel: XPC–PARP complexes engage the chromatin remodeler ALC1 to catalyze global genome DNA damage repair
  • Beteiligte: Blessing, Charlotte; Apelt, Katja; van den Heuvel, Diana; Gonzalez-Leal, Claudia; Rother, Magdalena B.; van der Woude, Melanie; González-Prieto, Román; Yifrach, Adi; Parnas, Avital; Shah, Rashmi G.; Kuo, Tia Tyrsett; Boer, Daphne E. C.; Cai, Jin; Kragten, Angela; Kim, Hyun-Suk; Schärer, Orlando D.; Vertegaal, Alfred C. O.; Shah, Girish M.; Adar, Sheera; Lans, Hannes; van Attikum, Haico; Ladurner, Andreas G.; Luijsterburg, Martijn S.
  • Erschienen: Springer Science and Business Media LLC, 2022
  • Erschienen in: Nature Communications
  • Sprache: Englisch
  • DOI: 10.1038/s41467-022-31820-4
  • ISSN: 2041-1723
  • Schlagwörter: General Physics and Astronomy ; General Biochemistry, Genetics and Molecular Biology ; General Chemistry ; Multidisciplinary
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  • Beschreibung: <jats:title>Abstract</jats:title><jats:p>Cells employ global genome nucleotide excision repair (GGR) to eliminate a broad spectrum of DNA lesions, including those induced by UV light. The lesion-recognition factor XPC initiates repair of helix-destabilizing DNA lesions, but binds poorly to lesions such as CPDs that do not destabilize DNA. How difficult-to-repair lesions are detected in chromatin is unknown. Here, we identify the poly-(ADP-ribose) polymerases PARP1 and PARP2 as constitutive interactors of XPC. Their interaction results in the XPC-stimulated synthesis of poly-(ADP-ribose) (PAR) by PARP1 at UV lesions, which in turn enables the recruitment and activation of the PAR-regulated chromatin remodeler ALC1. PARP2, on the other hand, modulates the retention of ALC1 at DNA damage sites. Notably, ALC1 mediates chromatin expansion at UV-induced DNA lesions, leading to the timely clearing of CPD lesions. Thus, we reveal how chromatin containing difficult-to-repair DNA lesions is primed for repair, providing insight into mechanisms of chromatin plasticity during GGR.</jats:p>
  • Zugangsstatus: Freier Zugang