Laboratory of Marine Organism Taxonomy and Phylogeny, Institute of Oceanology, Chinese Academy of Sciences, Qingdao, 266071, China.
University of Chinese Academy of Sciences, Beijing, 100049, China.
BMC Genomics. 2018 May 10;19(1):352. doi: 10.1186/s12864-018-4745-3.
Deep-sea hydrothermal vents are unique chemoautotrophic ecosystems with harsh conditions. Alvinocaris longirostris is one of the dominant crustacean species inhabiting in these extreme environments. It is significant to clarify mechanisms in their adaptation to the vents. Lysine acetylation has been known to play critical roles in the regulation of many cellular processes. However, its function in A. longirostris and even marine invertebrates remains elusive. Our study is the first, to our knowledge, to comprehensively investigate lysine acetylome in A. longirostris.
In total, 501 unique acetylation sites from 206 proteins were identified by combination of affinity enrichment and high-sensitive-massspectrometer. It was revealed that Arg, His and Lys occurred most frequently at the + 1 position downstream of the acetylation sites, which were all alkaline amino acids and positively charged. Functional analysis revealed that the protein acetylation was involved in diverse cellular processes, such as biosynthesis of amino acids, citrate cycle, fatty acid degradation and oxidative phosphorylation. Acetylated proteins were found enriched in mitochondrion and peroxisome, and many stress response related proteins were also discovered to be acetylated, like arginine kinases, heat shock protein 70, and hemocyanins. In the two hemocyanins, nine acetylation sites were identified, among which one acetylation site was unique in A. longirostris when compared with other shallow water shrimps. Further studies are warranted to verify its function.
The lysine acetylome of A. longirostris is investigated for the first time and brings new insights into the regulation function of the lysine acetylation. The results supply abundant resources for exploring the functions of acetylation in A. longirostris and other shrimps.
深海热液喷口是具有恶劣条件的独特化能自养生态系统。Alvinocaris longirostris 是栖息在这些极端环境中的主要甲壳类物种之一。阐明其对喷口适应的机制意义重大。赖氨酸乙酰化已被证明在许多细胞过程的调节中起着关键作用。然而，它在 A. longirostris 甚至海洋无脊椎动物中的功能仍然难以捉摸。据我们所知，我们的研究首次全面研究了 A. longirostris 中的赖氨酸乙酰组。
总共通过亲和富集和高灵敏度质谱仪的组合鉴定了 206 种蛋白质中的 501 个独特的乙酰化位点。结果表明，Arg、His 和 Lys 最常出现在乙酰化位点下游的+1 位置，它们都是碱性氨基酸和带正电荷的。功能分析表明，蛋白质乙酰化参与了多种细胞过程，如氨基酸的生物合成、柠檬酸循环、脂肪酸降解和氧化磷酸化。发现乙酰化蛋白富集在线粒体和过氧化物酶体中，许多与应激反应相关的蛋白质也被发现乙酰化，如精氨酸激酶、热休克蛋白 70 和血蓝蛋白。在两种血蓝蛋白中，鉴定出九个乙酰化位点，其中一个乙酰化位点在 A. longirostris 与其他浅水区虾类相比是独特的。需要进一步的研究来验证其功能。
首次研究了 A. longirostris 的赖氨酸乙酰组，为赖氨酸乙酰化的调节功能提供了新的见解。研究结果为探索乙酰化在 A. longirostris 和其他虾类中的功能提供了丰富的资源。
