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

Xue-Ming Wu, Bo-Sen Zhang, Yun-Long Zhao, Hua-Wei Wu, Feng Gao, Jie Zhang, Jian-Hua Zhao () and Hui-Shan Guo ()
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Xue-Ming Wu: Chinese Academy of Sciences
Bo-Sen Zhang: Chinese Academy of Sciences
Yun-Long Zhao: Chinese Academy of Sciences
Hua-Wei Wu: Chinese Academy of Sciences
Feng Gao: Chinese Academy of Sciences
Jie Zhang: Chinese Academy of Sciences
Jian-Hua Zhao: Chinese Academy of Sciences
Hui-Shan Guo: Chinese Academy of Sciences

Nature Communications, 2023, vol. 14, issue 1, 1-13

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-40384-w

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