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Xeroderma pigmentosum group C protein interacts with histones: regulation by acetylated states of histone H3
Author(s) -
Kakumu Erina,
Nakanishi Seiya,
Shiratori Hiromi M.,
Kato Akari,
Kobayashi Wataru,
Machida Shinichi,
Yasuda Takeshi,
Adachi Naoko,
Saito Naoaki,
Ikura Tsuyoshi,
Kurumizaka Hitoshi,
Kimura Hiroshi,
Yokoi Masayuki,
Sakai Wataru,
Sugasawa Kaoru
Publication year - 2017
Publication title -
genes to cells
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.912
H-Index - 115
eISSN - 1365-2443
pISSN - 1356-9597
DOI - 10.1111/gtc.12479
Subject(s) - histone , biology , xeroderma pigmentosum , acetylation , nucleotide excision repair , chromatin , histone code , histone h2a , microbiology and biotechnology , dna damage , histone modifying enzymes , epigenetics , chromatin remodeling , genetics , dna , nucleosome , gene
In the mammalian global genome nucleotide excision repair pathway, two damage recognition factors, XPC and UV‐DDB, play pivotal roles in the initiation of the repair reaction. 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‐induced 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‐terminal tail of histone H3. In addition, histone H1 also interacted with XPC. Importantly, acetylation of histone H3 markedly attenuated the interaction with XPC in vitro , 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.