As a signaling molecule, nitric oxide (NO) regulates the development and stress response in different organisms. The major biological activity of NO is protein S‐nitrosylation, whose function in fungi remains largely unclear. Here, it is found in the rice blast fungus Magnaporthe oryzae, de‐nitrosylation process is essential for functional appressorium formation during infection. Nitrosative stress caused by excessive accumulation of NO is harmful for fungal infection. While the S‐nitrosoglutathione reductase GSNOR‐mediated de‐nitrosylation removes excess NO toxicity during appressorium formation to promote infection. Through an indoTMT switch labeling proteomics technique, 741 S‐nitrosylation sites in 483 proteins are identified. Key appressorial proteins, such as Mgb1, MagB, Sps1, Cdc42, and septins, are activated by GSNOR through de‐nitrosylation. Removing S‐nitrosylation sites of above proteins is essential for proper protein structure and appressorial function. Therefore, GSNOR‐mediated de‐nitrosylation is an essential regulator for appressorium formation. It is also shown that breaking NO homeostasis by NO donors, NO scavengers, as well as chemical inhibitor of GSNOR, shall be effective methods for fungal disease control.

中文翻译：

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去亚硝基化协调附着胞功能对稻瘟病菌感染的影响

作为一种信号分子，一氧化氮 (NO) 调节不同生物体的发育和应激反应。 NO 的主要生物活性是蛋白质 S-亚硝基化，其在真菌中的功能仍不清楚。在这里，它是在稻瘟病菌中发现的稻瘟病菌，去亚硝基化过程对于感染期间功能性附着胞的形成至关重要。 NO过度积累引起的亚硝化应激对真菌感染有害。而 S-亚硝基谷胱甘肽还原酶 GSNOR 介导的去亚硝基化作用可消除附着细胞形成过程中过量的 NO 毒性，从而促进感染。通过 indoTMT 开关标记蛋白质组学技术，鉴定了 483 个蛋白质中的 741 个 S-亚硝基化位点。关键的附着蛋白，如 Mgb1、MagB、Sps1、Cdc42 和 septins，由 GSNOR 通过去亚硝基化激活。去除上述蛋白质的 S-亚硝基化位点对于正确的蛋白质结构和附着功能至关重要。因此，GSNOR 介导的去亚硝基化是附着胞形成的重要调节因子。研究还表明，通过NO供体、NO清除剂以及GSNOR化学抑制剂打破NO稳态，将是控制真菌病害的有效方法。