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TRIM29 regulates the assembly of DNA repair proteins into damaged chromatin

Author

Listed:
  • 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
    Kansas University Medical Center)

  • Laurence Florens

    (Stowers Institute for Medical Research)

  • Ronald C. Conaway

    (Stowers Institute for Medical Research
    Kansas University Medical Center)

  • Joan W. Conaway

    (Stowers Institute for Medical Research
    Kansas University Medical Center)

  • Shigetsugu Hatakeyama

    (Hokkaido University Graduate School of Medicine)

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.

Suggested Citation

  • Yasushi Masuda & Hidehisa Takahashi & Shigeo Sato & Chieri Tomomori-Sato & Anita Saraf & Michael P. Washburn & Laurence Florens & Ronald C. Conaway & Joan W. Conaway & Shigetsugu Hatakeyama, 2015. "TRIM29 regulates the assembly of DNA repair proteins into damaged chromatin," Nature Communications, Nature, vol. 6(1), pages 1-13, November.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms8299
    DOI: 10.1038/ncomms8299
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    Cited by:

    1. Guozhen Gao & Simone Hausmann & Natasha M. Flores & Ana Morales Benitez & Jianjun Shen & Xiaojie Yang & Maria D. Person & Sitaram Gayatri & Donghang Cheng & Yue Lu & Bin Liu & Pawel K. Mazur & Mark T., 2023. "The NFIB/CARM1 partnership is a driver in preclinical models of small cell lung cancer," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

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