Systematic analysis of the lysine malonylome in common wheat.
Systematic analysis of the lysine malonylome in common wheat.
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DOI：
10.1186/s12864-018-4535-y
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发表时间：
2018-03-20
期刊：
影响因子：
4.4
通讯作者：
Song L
中科院分区：
文献类型：
--
作者：
Liu J;Wang G;Lin Q;Liang W;Gao Z;Mu P;Li G;Song L
蛋白质赖氨酸丙二酸化是新近发现的一种翻译后修饰(PTM)，在真核生物和原核生物的多种代谢过程中都发挥着重要作用。普通小麦是全球主要的粮食作物。然而，赖氨酸丙二酰化的功能在这种作物中相对未知。在这里，进行了小麦赖氨酸丙二酰化的全球分析。在233种蛋白质中，共鉴定出342个赖氨酸丙二酸化位点。生物信息学分析表明，精氨酸(R)在+ 1位置的频率最高，并鉴定出一个修饰基序KmaR。丙二酸化蛋白定位于多个亚细胞室，尤其是胞浆(45%)和叶绿体(30%)。已鉴定的蛋白质参与了不同的途径，如碳代谢、卡尔文循环和氨基酸的生物合成，这表明赖氨酸丙二酰化在这些过程中起着重要作用。蛋白质相互作用网络分析揭示了8个高度相连的丙二酸化蛋白质簇，137个丙二酸化蛋白质被定位到蛋白质网络数据库中。此外，5种蛋白质同时被赖氨酸丙二酸化、乙酰化和琥珀酸化修饰，这表明这三种PTM可能协同调节普通小麦中许多蛋白质的功能。我们的结果表明，赖氨酸丙二酸化参与了多种生物过程，特别是光合作用生物的碳固定。这些数据首次报道了普通小麦中赖氨酸丙二酰化的情况，为进一步研究赖氨酸丙二酰化在小麦乃至所有植物中的生理作用提供了重要的数据集。本文的在线版本(10.1186/s12864-0184535-y)包含补充材料，可供授权用户使用。
Protein lysine malonylation, a newly discovered post-translational modification (PTM), plays an important role in diverse metabolic processes in both eukaryotes and prokaryotes. Common wheat is a major global cereal crop. However, the functions of lysine malonylation are relatively unknown in this crop. Here, a global analysis of lysine malonylation was performed in wheat. In total, 342 lysine malonylated sites were identified in 233 proteins. Bioinformatics analysis showed that the frequency of arginine (R) in position + 1 was highest, and a modification motif, KmaR, was identified. The malonylated proteins were located in multiple subcellular compartments, especially in the cytosol (45%) and chloroplast (30%). The identified proteins were found to be involved in diverse pathways, such as carbon metabolism, the Calvin cycle, and the biosynthesis of amino acids, suggesting an important role for lysine malonylation in these processes. Protein interaction network analysis revealed eight highly interconnected clusters of malonylated proteins, and 137 malonylated proteins were mapped to the protein network database. Moreover, five proteins were simultaneously modified by lysine malonylation, acetylation and succinylation, suggesting that these three PTMs may coordinately regulate the function of many proteins in common wheat. Our results suggest that lysine malonylation is involved in a variety of biological processes, especially carbon fixation in photosynthetic organisms. These data represent the first report of the lysine malonylome in common wheat and provide an important dataset for further exploring the physiological role of lysine malonylation in wheat and likely all plants. The online version of this article (10.1186/s12864-018-4535-y) contains supplementary material, which is available to authorized users.
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