TRIM29 regulates the assembly of DNA repair proteins into damaged chromatin

Yasushi Masuda, Hidehisa Takahashi, Shigeo Sato, Chieri Tomomori-Sato, Anita Saraf, Michael P. Washburn, Laurence Florens, Ronald C. Conaway, Joan W. Conaway and Shigetsugu Hatakeyama ()
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Yasushi Masuda: Hokkaido University Graduate School of Medicine
Hidehisa Takahashi: Hokkaido University Graduate School of Medicine
Shigeo Sato: Stowers Institute for Medical Research
Chieri Tomomori-Sato: Stowers Institute for Medical Research
Anita Saraf: Stowers Institute for Medical Research
Michael P. Washburn: Stowers Institute for Medical Research
Laurence Florens: Stowers Institute for Medical Research
Ronald C. Conaway: Stowers Institute for Medical Research
Joan W. Conaway: Stowers Institute for Medical Research
Shigetsugu Hatakeyama: Hokkaido University Graduate School of Medicine

Nature Communications, 2015, vol. 6, issue 1, 1-13

Abstract: 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.

Date: 2015
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DOI: 10.1038/ncomms8299

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