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However, the molecular mechanisms underlying regulation of the lesion recognition process in the context of chromatin structures remain to be understood. Here, we show evidence that damage recognition factors tend to associate with chromatin regions devoid of certain types of acetylated histones. Treatment of cells with histone deacetylase inhibitors retarded recruitment of XPC to sites of UV\u2010induced DNA damage and the subsequent repair process. Biochemical studies showed novel multifaceted interactions of XPC with histone H3, which were profoundly impaired by deletion of the N\u2010terminal tail of histone H3. In addition, histone H1 also interacted with XPC. Importantly, acetylation of histone H3 markedly attenuated the interaction with XPC <jats:italic>in\u00a0vitro<\/jats:italic>, and local UV irradiation of cells decreased the level of H3K27ac in the damaged areas. Our results suggest that histone deacetylation plays a significant role in the process of DNA damage recognition for nucleotide excision repair and that the localization and functions of XPC can be regulated by acetylated states of histones.<\/jats:p>","DOI":"10.1111\/gtc.12479","type":"journal-article","created":{"date-parts":[[2017,2,24]],"date-time":"2017-02-24T07:17:54Z","timestamp":1487920674000},"page":"310-327","source":"Crossref","is-referenced-by-count":29,"title":["Xeroderma pigmentosum group C protein interacts with histones: regulation by acetylated states of histone H3"],"prefix":"10.1111","volume":"22","author":[{"given":"Erina","family":"Kakumu","sequence":"first","affiliation":[{"name":"Division of Genomic Functions and Dynamics, Biosignal Research Center Kobe University  1\u20101 Rokkodai\u2010cho, Nada\u2010ku Kobe Hyogo 657\u20108501 Japan"},{"name":"Department of Biology, Graduate School of Science Kobe University  1\u20101 Rokkodai\u2010cho, Nada\u2010ku Kobe Hyogo 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