Proteome-wide analysis of lysine acetylation in the plant pathogen Botrytis cinerea.
Proteome-wide analysis of lysine acetylation in the plant pathogen Botrytis cinerea.
复制标题
植物病原体灰葡萄孢中赖氨酸乙酰化的全蛋白质组分析
DOI：
10.1038/srep29313
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发表时间：
2016-07-06
影响因子：
4.6
通讯作者：
Song L
中科院分区：
文献类型：
--
作者：
Lv B;Yang Q;Li D;Liang W;Song L
赖氨酸乙酰化是一种动态的、可逆的翻译后修饰，在多种细胞过程中起着重要作用。灰葡萄孢因其广泛的寄主范围和巨大的经济影响而成为研究最深入的坏死营养型物种。然而，到目前为止，对赖氨酸乙酰化在该植物病原体中的功能知之甚少。在本研究中，我们测定了B的赖氨酸乙酰组。通过亲和富集和高分辨率LC-MS/MS分析的组合，对灰葡萄属植物进行了鉴定。总共在954个蛋白质中鉴定了1582个赖氨酸乙酰化位点。生物信息学分析表明，乙酰化蛋白参与多种生物学功能，并显示出多种细胞定位。在该生物体中鉴定了几种优选靠近乙酰化位点的特定氨基酸，包括KacY、KacH、Kac*R、KacF、FKac和Kac*K。蛋白质相互作用网络分析表明，各种相互作用的蛋白质乙酰化调制。有趣的是，有6个蛋白参与了B的毒力。包括高渗透压甘油途径的3个关键组分在内的灰葡萄糖被乙酰化，表明赖氨酸乙酰化在发病机制中起调节作用。这些数据提供了B的乙酰组的第一个全面视图。cinerea中的赖氨酸乙酰化的功能分析，并作为丰富的资源，在这种植物病原体。
Lysine acetylation is a dynamic and reversible post-translational modification that plays an important role in diverse cellular processes. Botrytis cinerea is the most thoroughly studied necrotrophic species due to its broad host range and huge economic impact. However, to date, little is known about the functions of lysine acetylation in this plant pathogen. In this study, we determined the lysine acetylome of B. cinerea through the combination of affinity enrichment and high-resolution LC-MS/MS analysis. Overall, 1582 lysine acetylation sites in 954 proteins were identified. Bioinformatics analysis shows that the acetylated proteins are involved in diverse biological functions and show multiple cellular localizations. Several particular amino acids preferred near acetylation sites, including KacY, KacH, Kac***R, KacF, FKac and Kac***K, were identified in this organism. Protein interaction network analysis demonstrates that a variety of interactions are modulated by protein acetylation. Interestingly, 6 proteins involved in virulence of B. cinerea, including 3 key components of the high-osmolarity glycerol pathway, were found to be acetylated, suggesting that lysine acetylation plays regulatory roles in pathogenesis. These data provides the first comprehensive view of the acetylome of B. cinerea and serves as a rich resource for functional analysis of lysine acetylation in this plant pathogen.