Global Proteomic Analysis of Lysine Malonylation in Toxoplasma gondii
Global Proteomic Analysis of Lysine Malonylation in Toxoplasma gondii
复制标题
弓形虫赖氨酸丙酰化的整体蛋白质组学分析。
DOI：
10.3389/fmicb.2020.00776
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发表时间：
2020-04-28
影响因子：
5.2
通讯作者：
Zhu, Xing-Quan
中科院分区：
文献类型：
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作者：
Nie, Lan-Bi;Liang, Qin-Li;Zhu, Xing-Quan
赖氨酸丙二酰化（Lysine malonylation, Kmal）是一种新的翻译后修饰（PTM），已在几种原核和真核生物中报道。虽然Kmal可以调节各种生物的许多生物过程，但对顶复合体寄生虫弓形虫中这种重要的PTM的了解有限。在这项研究中，我们使用亲和富集和液相色谱-串联质谱（LC-MS/MS）分析首次对弓形虫速殖子的丙二酰化蛋白进行了全局分析。三个串联实验分别在203、236、230个丙二酰化蛋白上发现了294、345、352个Kmal位点。计算分析表明，鉴定的丙二酰化蛋白定位于不同的亚细胞区室，并参与许多细胞功能，特别是线粒体功能。此外，还检测到一个对半胱氨酸有强烈偏倚的保守Kmal基序。综上所述，这些发现首次报道了Kmal基因在弓形虫体内的分布，为研究Kmal在弓形虫体内的生理作用提供了重要的资源。
Lysine malonylation (Kmal) is a new post-translational modification (PTM), which has been reported in several prokaryotic and eukaryotic species. Although Kmal can regulate many and diverse biological processes in various organisms, knowledge about this important PTM in the apicomplexan parasite Toxoplasma gondii is limited. In this study, we performed the first global profiling of malonylated proteins in T. gondii tachyzoites using affinity enrichment and Liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis. Three experiments performed in tandem revealed 294, 345, 352 Kmal sites on 203, 236, 230 malonylated proteins, respectively. Computational analysis showed the identified malonylated proteins to be localized in various subcellular compartments and involved in many cellular functions, particularly mitochondrial function. Additionally, one conserved Kmal motif with a strong bias for cysteine was detected. Taken together, these findings provide the first report of Kmal profile in T. gondii and should be an important resource for studying the physiological roles of Kmal in this parasite.