Global Lysine Acetylation and 2-Hydroxyisobutyrylation Profiling Reveals the Metabolism Conversion Mechanism in Giardia lamblia.
Global Lysine Acetylation and 2-Hydroxyisobutyrylation Profiling Reveals the Metabolism Conversion Mechanism in Giardia lamblia.
复制标题
整体赖氨酸乙酰化和 2-羟基异丁酰化分析揭示了贾第鞭毛虫的代谢转换机制
DOI：
10.1074/mcp.ra120.002353
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发表时间：
2021
期刊：
影响因子：
--
通讯作者：
Feng X
中科院分区：
文献类型：
--
作者：
Zhu W;Jiang X;Sun H;Li Y;Shi W;Zheng M;Liu D;Ma A;Feng X
摘要蓝氏贾第鞭毛虫（Giardia lamblia，G.蓝氏贾第虫病是一种影响世界普通人群的常见感染。尽管由于它们自身的新陈代谢，G.蓝氏藻已经存活下来并进化以适应各种环境。然而，对G. Lamblia有限。本研究旨在揭示G.通过检测赖氨酸乙酰化（Kac）和2-羟基异丁酰化（Khib）位点结合定量蛋白质组学分析，对糖饥饿下的蓝氏藻进行了研究。在糖饥饿条件下，956个蛋白质上共有2999个乙酰化位点，1546个蛋白质上共有8877个2-羟基异丁酰基位点。综合Kac和Khib数据显示，修饰的蛋白质与精氨酸生物合成，糖酵解/代谢，丙氨酸，天冬氨酸和谷氨酸代谢。这些结果表明，Kac和Khib普遍存在，并为深入了解G. lamblia在糖饥饿。总之，这些结果有助于阐明G.揭示了从原核生物到真核生物的进化规律。
Abstract Giardia lamblia (G. lamblia) is the cause of giardiasis, a common infection that affects the general population of the world. Despite the constant possibility of damage because of their own metabolism, G. lamblia has survived and evolved to adapt to various environments. However, research on energy-metabolism conversion in G. lamblia is limited. This study aimed to reveal the dynamic metabolism conversion mechanism in G. lamblia under sugar starvation by detecting global lysine acetylation (Kac) and 2-hydroxyisobutyrylation (Khib) sites combined with quantitative proteome analyses. A total of 2999 acetylation sites on 956 proteins and 8877 2-hydroxyisobutyryl sites on 1546 proteins were quantified under sugar starvation. Integrated Kac and Khib data revealed that modified proteins were associated with arginine biosynthesis, glycolysis/gluconeogenesis, and alanine, aspartate, and glutamate metabolisms. These findings suggest that Kac and Khib were ubiquitous and provide deep insight into the metabolism conversion mechanism in G. lamblia under sugar starvation. Overall, these results can help delineate the biology of G. lamblia infections and reveal the evolutionary rule from prokaryote to eukaryote.