First comprehensive proteome analysis of lysine crotonylation in seedling leaves of Nicotiana tabacum.
First comprehensive proteome analysis of lysine crotonylation in seedling leaves of Nicotiana tabacum.
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DOI：
10.1038/s41598-017-03369-6
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发表时间：
2017-06-07
影响因子：
4.6
通讯作者：
Yang J
中科院分区：
文献类型：
--
作者：
Sun H;Liu X;Li F;Li W;Zhang J;Xiao Z;Shen L;Li Y;Wang F;Yang J
组蛋白巴托酰化是一种新的赖氨酸酰化类型的翻译后修饰（PTM），在酵母和哺乳动物细胞中富含活性基因启动子和潜在增强子。然而，赖氨酸巴豆酰化在非组蛋白和植物细胞中的作用尚未研究。在本研究中，我们使用高分辨率LC-MS/MS结合高灵敏度免疫亲和纯化技术对烟草进行了全局crotonylation蛋白质组学分析。共鉴定出分布在637种蛋白质上的2044个赖氨酸修饰位点，是目前报道的植物界赖氨酸酰化蛋白组中最丰富的。与植物中的赖氨酸乙酰化和琥珀酰化类似，赖氨酸巴豆酰化涉及多种代谢途径，如碳代谢、柠檬酸循环、糖酵解和氨基酸的生物合成。重要的是，72种蛋白质参与了光合作用的多个过程，大多数参与叶绿素合成的酶都通过巴豆酰化修饰。许多巴豆酰化蛋白通过泛素-蛋白酶体系统参与蛋白质的生物合成、折叠和降解。几个与染色质组织相关的巴豆酰化蛋白也在这里讨论。这些数据代表了全球巴豆酰化蛋白质组的首次报道，并为进一步研究非组蛋白巴豆酰化的功能提供了一个有希望的起点。
Histone crotonylation is a new lysine acylation type of post-translational modification (PTM) enriched at active gene promoters and potential enhancers in yeast and mammalian cells. However, lysine crotonylation in nonhistone proteins and plant cells has not yet been studied. In the present study, we performed a global crotonylation proteome analysis of Nicotiana tabacum (tobacco) using high-resolution LC-MS/MS coupled with highly sensitive immune-affinity purification. A total of 2044 lysine modification sites distributed on 637 proteins were identified, representing the most abundant lysine acylation proteome reported in the plant kingdom. Similar to lysine acetylation and succinylation in plants, lysine crotonylation was related to multiple metabolism pathways, such as carbon metabolism, the citrate cycle, glycolysis, and the biosynthesis of amino acids. Importantly, 72 proteins participated in multiple processes of photosynthesis, and most of the enzymes involved in chlorophyll synthesis were modified through crotonylation. Numerous crotonylated proteins were implicated in the biosynthesis, folding, and degradation of proteins through the ubiquitin-proteasome system. Several crotonylated proteins related to chromatin organization are also discussed here. These data represent the first report of a global crotonylation proteome and provide a promising starting point for further functional research of crotonylation in nonhistone proteins.