Guangdong Key Laboratory of Animal Conservation and Resource Utilization, Guangdong Public Laboratory of Wild Animal Conservation and Utilization, Institute of Zoology, Guangdong Academy of Science, Guangzhou, Guangdong Province, The People's Republic of China.
PLoS One. 2020 Dec 16;15(12):e0243787. doi: 10.1371/journal.pone.0243787. eCollection 2020.
Lysine acetylation (Kac) plays a critical role in the regulation of many important cellular processes. However, little is known about Kac in Solenopsis invicta, which is among the 100 most dangerous invasive species in the world. Kac in S. invicta was evaluated for the first time in this study. Altogether, 2387 Kac sites were tested in 992 proteins. The prediction of subcellular localization indicated that most identified proteins were located in the cytoplasm, mitochondria, and nucleus. Venom allergen Sol i 2, Sol i 3, and Sol i 4 were found to be located in the extracellular. The enriched Kac site motifs included Kac H, Kac Y, Kac G, Kac F, Kac T, and Kac W. H, Y, F, and W frequently occurred at the +1 position, whereas G, Y, and T frequently occurred at the -1 position. In the cellular component, acetylated proteins were enriched in the cytoplasmic part, mitochondrial matrix, and cytosolic ribosome. Furthermore, 25 pathways were detected to have significant enrichment. Interestingly, arginine and proline metabolism, as well as phagosome, which are related to immunity, involved several Kac proteins. Sequence alignment analyses demonstrated that V-type proton ATPase subunit G, tubulin alpha chain, and arginine kinase, the acetylated lysine residues, were evolutionarily conserved among different ant species. In the investigation of the interaction network, diverse interactions were adjusted by Kac. The results indicated that Kac may play an important role in the sensitization, cellular energy metabolism, immune response, nerve signal transduction, and response to biotic and abiotic stress of S. invicta. It may be useful to confirm the functions of Kac target proteins for the design of specific and effective drugs to prevent and control this dangerous invasive species.
赖氨酸乙酰化（Kac）在调节许多重要的细胞过程中起着关键作用。然而，对于世界上最危险的 100 种入侵物种之一的红火蚁（Solenopsis invicta）中的 Kac 知之甚少。本研究首次对 S. invicta 中的 Kac 进行了评估。总共在 992 种蛋白质中检测到 2387 个 Kac 位点。亚细胞定位预测表明，大多数鉴定出的蛋白质位于细胞质、线粒体和细胞核中。毒液过敏原 Sol i 2、Sol i 3 和 Sol i 4 被发现位于细胞外。富集的 Kac 位点基序包括 Kac H、Kac Y、Kac G、Kac F、Kac T 和 Kac W。H、Y、F 和 W 经常出现在+1 位，而 G、Y 和 T 经常出现在-1 位。在细胞成分中，乙酰化蛋白在细胞质部分、线粒体基质和胞质核糖体中富集。此外，检测到 25 条途径有显著富集。有趣的是，与免疫相关的精氨酸和脯氨酸代谢以及吞噬体涉及到几个 Kac 蛋白。序列比对分析表明，V 型质子 ATP 酶亚基 G、微管蛋白α链和精氨酸激酶，其乙酰化赖氨酸残基，在不同蚂蚁物种中是进化保守的。在互作网络的研究中，Kac 调节了不同的互作。结果表明，Kac 可能在红火蚁的致敏、细胞能量代谢、免疫反应、神经信号转导以及对生物和非生物胁迫的反应中发挥重要作用。这对于确认 Kac 靶蛋白的功能以设计针对这种危险入侵物种的特异性和有效的药物可能是有用的。
