Table_2_Systematic Analysis of Lysine Lactylation in the Plant Fungal Pathogen Botrytis cinerea.XLSX

Lysine lactylation (Kla) is a newly discovered histone post-translational modification (PTM), playing important roles in regulating transcription in macrophages. However, the extent of this PTM in non-histone proteins remains unknown. Here, we report the first proteomic survey of this modification in Botrytis cinerea, a destructive necrotrophic fungal pathogen distributed worldwide. After a global lysine lactylome analysis using LC-MS/MS, we identified 273 Kla sites in 166 proteins, of which contained in 4 types of modification motifs. Our results show that the majority of lactylated proteins were distributed in nucleus (36%), mitochondria (27%), and cytoplasm (25%). The identified proteins were found to be involved in diverse cellular processes. Most strikingly, Kla was found in 43 structural constituent proteins of ribosome, indicating an impact of Kla in protein synthesis. Moreover, 12 lactylated proteins participated in fungal pathogenicity, suggesting a potential role for Kla in this process. Protein interaction network analysis suggested that a mass of protein interactions are regulated by lactylation. The combined data sets represent the first report of the lactylome of B. cinerea and provide a good foundation for further explorations of Kla in plant fungal pathogens.

赖氨酸乳酸化（Kla）是一种新近发现的组蛋白翻译后修饰（PTM），在调节巨噬细胞转录中发挥着重要作用。然而，这种PTM在非组蛋白中的程度尚不清楚。在本研究中，我们报告了首次对全球赖氨酸乳酸ome在灰葡萄孢菌（Botrytis cinerea）中的蛋白质组学调查，灰葡萄孢菌是一种分布全球的毁灭性坏死性真菌病原体。通过使用液相色谱-串联质谱（LC-MS/MS）进行全局赖氨酸乳酸ome分析后，我们在166种蛋白质中识别出273个Kla位点，这些位点包含4种修饰基序类型。我们的研究结果揭示，大多数乳酸化蛋白质分布于细胞核（36%）、线粒体（27%）和细胞质（25%）。所识别的蛋白质被发现参与多种细胞过程。最引人注目的是，Kla存在于43种核糖体结构组成蛋白中，这表明Kla在蛋白质合成中具有影响。此外，12种乳酸化蛋白质参与了真菌致病性，暗示Kla在这一过程中可能具有潜在作用。蛋白质相互作用网络分析表明，大量的蛋白质相互作用受乳酸化调控。综合数据集代表了灰葡萄孢菌乳酸ome的第一份报告，为今后对植物真菌病原体中Kla的进一步研究提供了良好的基础。