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Acetylome Analysis Reveals Population Differentiation of the Pacific Oyster Crassostrea gigas in Response to Heat Stress.
Marine Biotechnology ( IF 2.6 ) Pub Date : 2020-01-29 , DOI: 10.1007/s10126-020-09947-6
Ao Li 1, 2, 3, 4 , Li Li 1, 2, 3, 5 , Wei Wang 1, 2, 3, 5 , Guofan Zhang 1, 3, 5
Affiliation  

Lysine acetylation of proteins is a highly conserved post-translational modification that plays an important regulatory role in almost every aspect of metabolic processes in both terrestrial and aquatic species. Pacific oyster, Crassostrea gigas, a model marine species, is distributed worldwide and is economically and ecologically important. However, little is known about the role of acetylation in the adaptive response of oyster to heterogeneous intertidal environments. Here, we conducted the first-ever lysine acetylome analysis in two genetically and physiologically differentiated oyster populations, using a highly sensitive immune-affinity purification and high-resolution mass spectrometry. Overall, we identified 1054 lysine acetylation sites in 664 proteins, which account for 2.37% of the oyster proteome analysed in the current study. The modified proteins are involved in a wide range of biological processes and are localised in multiple cellular compartments. Motif analysis revealed that hydrophilic and polar amino acids histidine, lysine and arginine were the most enriched residues in the positions + 1 and + 2 of the acetylated sites. Further, the two oyster populations exhibited divergent acetylomic regulations of several biological pathways, particularly energy metabolism and glycine and serine amino acid metabolism, in response to thermal stress and differentiated acetylation patters of candidate heat-responsive proteins, e.g. molecular chaperone and myosin. These observations suggest that lysine acetylation plays a critical role in different thermal responses of these two oyster populations. These findings provide an important resource for in-depth exploration of the physiological role of lysine acetylation in adaptive evolution of marine invertebrates.

中文翻译:

乙酰组学分析揭示了太平洋牡蛎Crassostrea gigas对热应激的种群分化。

蛋白质的赖氨酸乙酰化是高度保守的翻译后修饰,在陆生和水生物种的代谢过程的几乎每个方面都起着重要的调节作用。太平洋牡蛎,Crassostrea gigas是一种典型的海洋物种,分布于世界各地,在经济和生态上都很重要。然而,关于乙酰化在牡蛎对异质潮间环境的适应性反应中的作用了解甚少。在这里,我们使用高度灵敏的免疫亲和纯化和高分辨率质谱技术,在两个遗传和生理上不同的牡蛎种群中进行了有史以来的首次赖氨酸乙酰化酶组分析。总体而言,我们在664种蛋白质中鉴定了1054个赖氨酸乙酰化位点,占本研究中分析的牡蛎蛋白质组的2.37%。修饰的蛋白质参与广泛的生物学过程,并位于多个细胞区室中。图案分析表明,亲水性和极性氨基酸组氨酸,赖氨酸和精氨酸是乙酰化位点+1和+2位最富集的残基。此外,响应于热应激和候选热响应蛋白(例如分子伴侣和肌球蛋白)的乙酰化模式的差异,两个牡蛎种群对几种生物途径,尤其是能量代谢以及甘氨酸和丝氨酸氨基酸代谢表现出不同的乙酰组学规律。这些观察结果表明,赖氨酸乙酰化在这两个牡蛎种群的不同热响应中起着关键作用。这些发现为深入探究赖氨酸乙酰化在海洋无脊椎动物适应性进化中的生理作用提供了重要的资源。这两个牡蛎种群对几种生物途径表现出不同的乙酰组学规律,特别是能量代谢以及甘氨酸和丝氨酸氨基酸代谢,响应于热应激和候选热响应蛋白(例如分子伴侣和肌球蛋白)的乙酰化模式。这些观察结果表明,赖氨酸乙酰化在这两个牡蛎种群的不同热响应中起着关键作用。这些发现为深入探究赖氨酸乙酰化在海洋无脊椎动物适应性进化中的生理作用提供了重要的资源。响应热应激和候选热响应蛋白(例如分子伴侣和肌球蛋白)的不同乙酰化模式,这两个牡蛎种群在几种生物途径(尤其是能量代谢以及甘氨酸和丝氨酸氨基酸代谢)中表现出不同的乙酰组学规律。这些观察结果表明,赖氨酸乙酰化在这两个牡蛎种群的不同热响应中起着关键作用。这些发现为深入探究赖氨酸乙酰化在海洋无脊椎动物适应性进化中的生理作用提供了重要的资源。G。分子伴侣和肌球蛋白。这些观察结果表明,赖氨酸乙酰化在这两个牡蛎种群的不同热响应中起着关键作用。这些发现为深入探究赖氨酸乙酰化在海洋无脊椎动物适应性进化中的生理作用提供了重要的资源。G。分子伴侣和肌球蛋白。这些观察结果表明,赖氨酸乙酰化在这两个牡蛎种群的不同热响应中起着关键作用。这些发现为深入探究赖氨酸乙酰化在海洋无脊椎动物适应性进化中的生理作用提供了重要的资源。
更新日期:2020-01-29
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