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Proteasomal degradation of BRAHMA promotes Boron tolerance in Arabidopsis

Author

Listed:
  • Takuya Sakamoto

    (Tokyo University of Science
    The University of Tokyo)

  • Yayoi Tsujimoto-Inui

    (Tokyo University of Science
    The University of Tokyo)

  • Naoyuki Sotta

    (The University of Tokyo)

  • Takeshi Hirakawa

    (Tokyo University of Science)

  • Tomoko M. Matsunaga

    (Tokyo University of Science)

  • Yoichiro Fukao

    (Nara Institute of Science and Technology
    Ritsumeikan University)

  • Sachihiro Matsunaga

    (Tokyo University of Science)

  • Toru Fujiwara

    (The University of Tokyo)

Abstract

High levels of boron (B) induce DNA double-strand breaks (DSBs) in eukaryotes, including plants. Here we show a molecular pathway of high B-induced DSBs by characterizing Arabidopsis thaliana hypersensitive to excess boron mutants. Molecular analysis of the mutants revealed that degradation of a SWItch/Sucrose Non-Fermentable subunit, BRAHMA (BRM), by a 26S proteasome (26SP) with specific subunits is a key process for ameliorating high-B-induced DSBs. We also found that high-B treatment induces histone hyperacetylation, which increases susceptibility to DSBs. BRM binds to acetylated histone residues and opens chromatin. Accordingly, we propose that the 26SP limits chromatin opening by BRM in conjunction with histone hyperacetylation to maintain chromatin stability and avoid DSB formation under high-B conditions. Interestingly, a positive correlation between the extent of histone acetylation and DSB formation is evident in human cultured cells, suggesting that the mechanism of DSB induction is also valid in animals.

Suggested Citation

  • Takuya Sakamoto & Yayoi Tsujimoto-Inui & Naoyuki Sotta & Takeshi Hirakawa & Tomoko M. Matsunaga & Yoichiro Fukao & Sachihiro Matsunaga & Toru Fujiwara, 2018. "Proteasomal degradation of BRAHMA promotes Boron tolerance in Arabidopsis," Nature Communications, Nature, vol. 9(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07393-6
    DOI: 10.1038/s41467-018-07393-6
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