Zhang Yumei, Song Limin, Liang Wenxing, Mu Ping, Wang Shu, Lin Qi
College of Agronomy, Shenyang Agricultural University, Shenyang, Liaoning 110866, China.
College of Agronomy and Plant Protection, Qingdao Agricultural University, Qingdao, Shandong 266109, China.
Sci Rep. 2016 Feb 15;6:21069. doi: 10.1038/srep21069.
Lysine acetylation of proteins, a dynamic and reversible post-translational modification, plays a critical regulatory role in both eukaryotes and prokaryotes. Several researches have been carried out on acetylproteome in plants. However, until now, there have been no data on common wheat, the major cereal crop in the world. In this study, we performed a global acetylproteome analysis of common wheat variety (Triticum aestivum L.), Chinese Spring. In total, 416 lysine modification sites were identified on 277 proteins, which are involved in a wide variety of biological processes. Consistent with previous studies, a large proportion of the acetylated proteins are involved in metabolic process. Interestingly, according to the functional enrichment analysis, 26 acetylated proteins are involved in photosynthesis and Calvin cycle, suggesting an important role of lysine acetylation in these processes. Moreover, protein interaction network analysis reveals that diverse interactions are modulated by protein acetylation. These data represent the first report of acetylome in common wheat and serve as an important resource for exploring the physiological role of lysine acetylation in this organism and likely in all plants.
蛋白质的赖氨酸乙酰化是一种动态且可逆的翻译后修饰，在真核生物和原核生物中均发挥着关键的调节作用。针对植物中的乙酰化蛋白质组已开展了多项研究。然而，截至目前，尚未有关于世界主要谷类作物普通小麦的相关数据。在本研究中，我们对普通小麦品种（Triticum aestivum L.）中国春进行了全乙酰化蛋白质组分析。总共在277种蛋白质上鉴定出416个赖氨酸修饰位点，这些蛋白质参与了各种各样的生物学过程。与先前的研究一致，很大一部分乙酰化蛋白质参与代谢过程。有趣的是，根据功能富集分析，有26种乙酰化蛋白质参与光合作用和卡尔文循环，这表明赖氨酸乙酰化在这些过程中发挥着重要作用。此外，蛋白质相互作用网络分析表明，蛋白质乙酰化调节了多种相互作用。这些数据代表了普通小麦乙酰化蛋白质组的首次报道，并为探索赖氨酸乙酰化在该生物体以及可能在所有植物中的生理作用提供了重要资源。
