Liang Wenxing's team from Qingdao Agricultural University discovered a new mechanism for the regulation of sporulation of Fusarium oxysporum

Editor | Fusarium oxysporum (Fo, Fusarium oxysporum) is one of the most abundant and diverse fungal species found in soil, with a wide range of plant and animal hosts
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Conidia are the main mode of reproduction of many filamentous fungi, and the mechanism of spore production is currently very limited
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Lysine acetylation (Kac, lysine acetylation) is an evolutionarily conserved and extensive post-translational modification involved in the regulation of various metabolic processes, but whether it is involved in the regulation of fungal sporulation is unclear
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Recently, Liang Wenxing's team from the School of Phytomedicine, Qingdao Agricultural University published a research paper entitled Quantitative proteomic analysis reveals important roles of the acetylation of ER-resident molecular chaperones for conidiation in Fusarium oxysporum in Molecular & Cellular Proteomics, an international journal of proteomics.
From the perspective of acetylation modification, a new mechanism of Fo regulation of sporulation was revealed
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To unearth acetylated proteins that may affect sporulation, the team first performed quantitative acetylated proteome determination and analysis by comparing Fo sporulating mycelium (SM, sporulating mycelium) and non-sporulating mycelium (NM, nonsporulating mycelium), a total of 62 up-regulated and 49 down-regulated Kac proteins were identified
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These differentially acetylated proteins were significantly enriched in glycolytic pathways, ribosomal proteins and molecular chaperone proteins
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Among them, the changes in the acetylation levels of three molecular chaperone proteins, PDI, HSP70, and HSP40 located in the endoplasmic reticulum, can significantly affect the production of Fo conidia.

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Further biochemical experiments demonstrated that K70ac was essential for maintaining the protein stability and enzymatic activity of PDI; K604ac of HSP70 and K32ac of HSP40 inhibited the detoxification ability of HSP proteins, resulting in the accumulation of higher levels of protein aggregates
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During conidiogenesis, increased levels of PDIK70ac and decreased levels of HSP70K604ac, HSP40K32ac contribute to the correct processing of unfolded proteins and eliminate the accumulation of protein aggregates, which favors cellular remodeling during Fo conidia formation
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Endoplasmic reticulum chaperone protein acetylation regulates the sporulation of Fusarium oxysporum.
Associate Professor Zhang Ning and Professor Liang Wenxing from the School of Phytomedicine of Qingdao Agricultural University are the co-corresponding authors of the paper.
Graduate students Lv Fangjiao and Xu Yang of the research group are the co-first authors.
, Professor Dean W.
Gabriel of the University of Florida and others participated in this work
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The above research work was supported by the National Natural Science Foundation of China, the Shandong Provincial Double Hundred Program for Foreign Professionals, and the Taishan Scholars Post Construction Fund
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Paper link: https://