Xeroderma pigmentosum group C protein interacts with histones: regulation by acetylated states of histone H3
Erina Kakumu, Seiya Nakanishi, Hiromi M. Shiratori, Akari Kato, Wataru Kobayashi, Shinichi Machida, Takeshi Yasuda, Naoko Adachi, Naoaki Saito, Tsuyoshi Ikura, Hitoshi Kurumizaka, Hiroshi Kimura, Masayuki Yokoi, Wataru Sakai and Kaoru Sugasawa
Version of Record online: 24 FEB 2017 | DOI: 10.1111/gtc.12479
XPC, the DNA damage recognition factor involved in mammalian nucleotide excision repair, has at least two interfaces for interactions with histone H3 and/or H1. The N-terminal tail of histone H3 plays a crucial role, and acetylation of histone H3 negatively regulates the interaction with XPC. Subnuclear localization and functions of XPC may be regulated by such interactions with non-acetylated chromatin regions.