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TRIM29 regulates the assembly of DNA repair proteins into damaged chromatin


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タイトル: TRIM29 regulates the assembly of DNA repair proteins into damaged chromatin
著者: Masuda, Yasushi 著作を一覧する
Takahashi, Hidehisa 著作を一覧する
Sato, Shigeo 著作を一覧する
Tomomori-Sato, Chieri 著作を一覧する
Saraf, Anita 著作を一覧する
Washburn, Michael P. 著作を一覧する
Florens, Laurence 著作を一覧する
Conaway, Ronald C. 著作を一覧する
Conaway, Joan W. 著作を一覧する
Hatakeyama, Shigetsugu 著作を一覧する
発行日: 2015年 6月
出版者: Nature Publishing Group
誌名: Nature communications
巻: 6
開始ページ: 7299
出版社 DOI: 10.1038/ncomms8299
抄録: Although DNA double-strand break (DSB) repair is mediated by numerous proteins accumulated at DSB sites, how DNA repair proteins are assembled into damaged chromatin has not been fully elucidated. Here we show that a member of the tripartite motif protein family, TRIM29, is a histone-binding protein responsible for DNA damage response (DDR). We found that TRIM29 interacts with BRCA1-associated surveillance complex, cohesion, DNA-PKcs and components of TIP60 complex. The dynamics of the TRIM29-containing complex on H2AX nucleosomes is coordinated by a cross-talk between histone modifications. TRIM29 binds to modified histone H3 and H4 tails in the context of nucleosomes. Furthermore, chromatin binding of TRIM29 is required for the phosphorylation of H2AX and cell viability in response to ionizing radiation. Our results suggest that TRIM29 functions as a scaffold protein to assemble DNA repair proteins into chromatin followed by efficient activation of DDR.
資料タイプ: article
出現コレクション:雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

提供者: 畠山 鎮次


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