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Table_2_The Redox Proteome of Thiol Proteins in the Rice Blast Fungus Magnaporthe oryzae.xlsx

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NIAID Data Ecosystem2026-03-12 收录
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https://figshare.com/articles/dataset/Table_2_The_Redox_Proteome_of_Thiol_Proteins_in_the_Rice_Blast_Fungus_Magnaporthe_oryzae_xlsx/14189177
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Redox modification, a post-translational modification, has been demonstrated to be significant for many physiological pathways and biological processes in both eukaryotes and prokaryotes. However, little is known about the global profile of protein redox modification in fungi. To explore the roles of redox modification in the plant pathogenic fungi, a global thiol proteome survey was performed in the model fungal pathogen Magnaporthe oryzae. A total of 3713 redox modification sites from 1899 proteins were identified through a mix sample containing mycelia with or without oxidative stress, conidia, appressoria, and invasive hyphae of M. oryzae. The identified thiol-modified proteins were performed with protein domain, subcellular localization, functional classification, metabolic pathways, and protein–protein interaction network analyses, indicating that redox modification is associated with a wide range of biological and cellular functions. These results suggested that redox modification plays important roles in fungal growth, conidium formation, appressorium formation, as well as invasive growth. Interestingly, a large number of pathogenesis-related proteins were redox modification targets, suggesting the significant roles of redox modification in pathogenicity of M. oryzae. This work provides a global insight into the redox proteome of the pathogenic fungi, which built a groundwork and valuable resource for future studies of redox modification in fungi.

氧化还原修饰(redox modification)作为一种翻译后修饰(post-translational modification),已被证实对真核生物与原核生物的诸多生理通路及生物学过程具有重要意义。然而目前学界对真菌中蛋白质氧化还原修饰的全局图谱仍知之甚少。为探究氧化还原修饰在植物病原真菌中的作用,本研究以模式植物病原真菌稻瘟病菌(Magnaporthe oryzae)为对象,开展了全局性巯基蛋白质组(thiol proteome)分析。本研究通过混合稻瘟病菌的氧化应激与非氧化应激菌丝体、分生孢子(conidia)、附着胞(appressoria)及侵入菌丝(invasive hyphae)样本,共鉴定到1899个蛋白质上的3713个氧化还原修饰位点。研究人员对鉴定得到的巯基修饰蛋白质进行了蛋白质结构域、亚细胞定位、功能分类、代谢通路及蛋白质相互作用网络分析,结果显示氧化还原修饰与广泛的生物学及细胞功能密切相关。上述结果表明,氧化还原修饰在真菌生长、分生孢子形成、附着胞形成及侵入生长过程中均发挥重要作用。值得注意的是,大量致病相关蛋白质均为氧化还原修饰的靶标,这提示氧化还原修饰在稻瘟病菌的致病性中具有关键作用。本研究实现了对病原真菌氧化还原蛋白质组的全局性解析,为后续真菌氧化还原修饰的相关研究奠定了坚实基础并提供了宝贵的研究资源。
创建时间:
2021-03-10
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