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DeSUMOylation of a Verticillium dahliae enolase facilitates virulence by derepressing the expression of the effector VdSCP8

Author

Listed:
  • Xue-Ming Wu

    (Chinese Academy of Sciences
    University of the Chinese Academy of Sciences)

  • Bo-Sen Zhang

    (Chinese Academy of Sciences
    University of the Chinese Academy of Sciences)

  • Yun-Long Zhao

    (Chinese Academy of Sciences
    University of California, San Diego)

  • Hua-Wei Wu

    (Chinese Academy of Sciences
    University of the Chinese Academy of Sciences)

  • Feng Gao

    (Chinese Academy of Sciences
    University of the Chinese Academy of Sciences)

  • Jie Zhang

    (Chinese Academy of Sciences
    University of the Chinese Academy of Sciences)

  • Jian-Hua Zhao

    (Chinese Academy of Sciences
    University of the Chinese Academy of Sciences)

  • Hui-Shan Guo

    (Chinese Academy of Sciences
    University of the Chinese Academy of Sciences)

Abstract

The soil-borne fungus Verticillium dahliae, the most notorious plant pathogen of the Verticillium genus, causes vascular wilts in a wide variety of economically important crops. The molecular mechanism of V. dahliae pathogenesis remains largely elusive. Here, we identify a small ubiquitin-like modifier (SUMO)-specific protease (VdUlpB) from V. dahliae, and find that VdUlpB facilitates V. dahliae virulence by deconjugating SUMO from V. dahliae enolase (VdEno). We identify five lysine residues (K96, K254, K259, K313 and K434) that mediate VdEno SUMOylation, and SUMOylated VdEno preferentially localized in nucleus where it functions as a transcription repressor to inhibit the expression of an effector VdSCP8. Importantly, VdUlpB mediates deSUMOylation of VdEno facilitates its cytoplasmic distribution, which allows it to function as a glycolytic enzyme. Our study reveals a sophisticated pathogenic mechanism of VdUlpB-mediated enolase deSUMOylation, which fortifies glycolytic pathway for growth and contributes to V. dahliae virulence through derepressing the expression of an effector.

Suggested Citation

  • Xue-Ming Wu & Bo-Sen Zhang & Yun-Long Zhao & Hua-Wei Wu & Feng Gao & Jie Zhang & Jian-Hua Zhao & Hui-Shan Guo, 2023. "DeSUMOylation of a Verticillium dahliae enolase facilitates virulence by derepressing the expression of the effector VdSCP8," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-40384-w
    DOI: 10.1038/s41467-023-40384-w
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    References listed on IDEAS

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    1. Shyr-Jiann Li & Mark Hochstrasser, 1999. "A new protease required for cell-cycle progression in yeast," Nature, Nature, vol. 398(6724), pages 246-251, March.
    2. Yongliang Zhang & Gaoyuan Song & Neeraj K. Lal & Ugrappa Nagalakshmi & Yuanyuan Li & Wenjie Zheng & Pin-jui Huang & Tess C. Branon & Alice Y. Ting & Justin W. Walley & Savithramma P. Dinesh-Kumar, 2019. "TurboID-based proximity labeling reveals that UBR7 is a regulator of N NLR immune receptor-mediated immunity," Nature Communications, Nature, vol. 10(1), pages 1-17, December.
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