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PARylation of 14-3-3 proteins controls the virulence of Magnaporthe oryzae

Author

Listed:
  • Xiuqin Gao

    (Fujian Agriculture and Forestry University
    Fujian Agriculture and Forestry University)

  • Gaigai Gao

    (Fujian Agriculture and Forestry University)

  • Weifeng Zheng

    (Fujian Agriculture and Forestry University)

  • Haibing Liu

    (Fujian Agriculture and Forestry University
    Fujian Agriculture and Forestry University)

  • Wenbo Pan

    (Fujian Agriculture and Forestry University)

  • Xi Xia

    (Fujian Agriculture and Forestry University)

  • Dongmei Zhang

    (Fujian Agriculture and Forestry University)

  • Wenwei Lin

    (Fujian Agriculture and Forestry University
    Haixia Institute of Science and Technology, Fujian Agriculture and Forestry University)

  • Zonghua Wang

    (Fujian Agriculture and Forestry University
    Minjiang University)

  • Baomin Feng

    (Fujian Agriculture and Forestry University)

Abstract

Magnaporthe oryzae is a devastating fungal pathogen that causes the rice blast disease worldwide. The post-translational modification of ADP-ribosylation holds significant importance in various fundamental biological processes. However, the specific function of this modification in M. oryzae remains unknown. This study revealed that Poly(ADP-ribosyl)ation (PARylation) executes a critical function in M. oryzae. M. oryzae Poly(ADP-ribose) polymerase 1 (PARP1) exhibits robust PARylation activity. Disruption of PARylation by PARP1 knock-out or chemical inhibition reveals its involvement in M. oryzae virulence, particularly in appressorium formation. Furthermore, we identified two M. oryzae 14-3-3 proteins, GRF1 and GRF2, as substrates of PARP1. Deletion of GRF1 or GRF2 results in delayed and dysfunctional appressorium, diminished plant penetration, and reduced virulence of the fungus. Biochemical and genetic evidence suggest that PARylation of 14-3-3s is essential for its function in M. oryzae virulence. Moreover, PARylation regulates 14-3-3 dimerization and is required for the activation of the mitogen-activated protein kinases (MAPKs), Pmk1 and Mps1. GRF1 interacts with both Mst7 and Pmk1, and bridges their interaction in a PARylation-dependent manner. This study unveils a distinctive mechanism that PARylation of 14-3-3 proteins controls appressorium formation through MAPK activation, and could facilitate the development of new strategies of rice blast disease control.

Suggested Citation

  • Xiuqin Gao & Gaigai Gao & Weifeng Zheng & Haibing Liu & Wenbo Pan & Xi Xia & Dongmei Zhang & Wenwei Lin & Zonghua Wang & Baomin Feng, 2024. "PARylation of 14-3-3 proteins controls the virulence of Magnaporthe oryzae," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-51955-w
    DOI: 10.1038/s41467-024-51955-w
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    References listed on IDEAS

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    1. Lauren S. Ryder & Yasin F. Dagdas & Michael J. Kershaw & Chandrasekhar Venkataraman & Anotida Madzvamuse & Xia Yan & Neftaly Cruz-Mireles & Darren M. Soanes & Miriam Oses-Ruiz & Vanessa Styles & Jan S, 2019. "A sensor kinase controls turgor-driven plant infection by the rice blast fungus," Nature, Nature, vol. 574(7778), pages 423-427, October.
    2. Ezeogo Obaji & Mirko M. Maksimainen & Albert Galera-Prat & Lari Lehtiö, 2021. "Activation of PARP2/ARTD2 by DNA damage induces conformational changes relieving enzyme autoinhibition," Nature Communications, Nature, vol. 12(1), pages 1-8, December.
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