Systematic Analysis of the Lysine Acetylome in Vibrio parahemolyticus
Systematic Analysis of the Lysine Acetylome in Vibrio parahemolyticus
复制标题
副溶血弧菌赖氨酸乙酰基组的系统分析
DOI：
10.1021/pr500133t
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发表时间：
2014-07-01
影响因子：
4.4
通讯作者：
Zhao, Fukun
中科院分区：
文献类型：
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作者：
Pan, Jianyi;Ye, Zhicang;Zhao, Fukun
蛋白质的赖氨酸乙酰化是一种主要的翻译后修饰，在细胞的几乎每个方面都发挥着重要的调节作用，无论是真核生物还是原核生物。副溶血性弧菌是一种典型的海洋细菌，是细菌性海鲜传播疾病的世界性病因。在这里，我们通过高灵敏的免疫亲和纯化和高分辨率的LC-MS/MS相结合的方法在该细菌中进行了第一次赖氨酸乙酰化组分，我们在656个蛋白质中鉴定了1413个赖氨酸乙酰化位点，占细胞总蛋白质的13.6%，这是迄今为止在细菌中鉴定出的最高比例的乙酰化蛋白质。乙酰化组的生物信息学分析表明，乙酰化蛋白参与了广泛的细胞功能，并表现出不同的亚细胞定位。更具体地说，与蛋白质生物合成和碳代谢相关的蛋白质是赖氨酸乙酰化的优先靶点。此外，乙酰组分析还揭示了两种类型的乙酰化基序，即+4/+5位的赖氨酸或精氨酸以及+1/+2位的酪氨酸、组氨酸或苯丙氨酸。此外，蛋白质相互作用网络分析表明，广泛的相互作用受到蛋白质乙酰化的调节。本研究为深入探讨赖氨酸乙酰化在副溶血性弧菌中的生理作用提供了重要的开端。
Lysine acetylation of proteins is a major post-translational modification that plays an important regulatory role in almost every aspect of cells, both eukaryotes and prokaryotes. Vibrio parahemolyticus, a model marine bacterium, is a worldwide cause of bacterial seafood-borne illness. Here, we conducted the first lysine acetylome in this bacterium through a combination of highly sensitive immune-affinity purification and high-resolution LC-MS/MS. Overall, we identified 1413 lysine acetylation sites in 656 proteins, which account for 13.6% of the total proteins in the cells; this is the highest ratio of acetyl proteins that has so far been identified in bacteria. The bioinformatics analysis of the acetylome showed that the acetylated proteins are involved in a wide range of cellular functions and exhibit diverse subcellular localizations. More specifically, proteins related to protein biosynthesis and carbon metabolism are the preferential targets of lysine acetylation. Moreover, two types of acetylation motifs, a lysine or arginine at the +4/+5 positions and a tyrosine, histidine, or phenylalanine at the +1/+2 positions, were revealed from the analysis of the acetylome. Additionally, protein interaction network analysis demonstrates that a wide range of interactions are modulated by protein acetylation. This study provides a significant beginning for the in-depth exploration of the physiological role of lysine acetylation in V. parahemolyticus.