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TRIM29 regulates the assembly of DNA repair proteins into damaged chromatin

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Title: TRIM29 regulates the assembly of DNA repair proteins into damaged chromatin
Authors: Masuda, Yasushi Browse this author
Takahashi, Hidehisa Browse this author →KAKEN DB
Sato, Shigeo Browse this author
Tomomori-Sato, Chieri Browse this author
Saraf, Anita Browse this author
Washburn, Michael P. Browse this author
Florens, Laurence Browse this author
Conaway, Ronald C. Browse this author
Conaway, Joan W. Browse this author
Hatakeyama, Shigetsugu Browse this author →KAKEN DB
Issue Date: Jun-2015
Publisher: Nature Publishing Group
Journal Title: Nature communications
Volume: 6
Start Page: 7299
Publisher DOI: 10.1038/ncomms8299
PMID: 26095369
Abstract: 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.
Type: article
Appears in Collections:医学院・医学研究院 (Graduate School of Medicine / Faculty of Medicine) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 畠山 鎮次

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