Comprehensive proteome analyses of lysine acetylation in tea leaves by sensing nitrogen nutrition.
Comprehensive proteome analyses of lysine acetylation in tea leaves by sensing nitrogen nutrition.
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DOI：
10.1186/s12864-018-5250-4
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发表时间：
2018-11-26
期刊：
影响因子：
4.4
通讯作者：
Ding Z
中科院分区：
文献类型：
--
作者：
Jiang J;Gai Z;Wang Y;Fan K;Sun L;Wang H;Ding Z
赖氨酸残基的Nε-乙酰化是一种常见的翻译后修饰，在生理代谢中起着重要的调节作用。然而，氮饥饿/再供应条件下茶树叶片蛋白质乙酰组的整体概况信息有限。赖氨酸乙酰化蛋白在茶树氮素吸收和同化中的功能尚不清楚。在这里，我们进行了氮（N）饥饿/再供应下的茶叶赖氨酸乙酰组的全球审查，使用肽预分级，免疫亲和富集，并与高灵敏度LC-MS/MS结合亲和纯化分析耦合。共在1286个蛋白质上鉴定出2229个赖氨酸乙酰化位点，其中16个保守基序分别为E*KacK、Kac*K、Kac*R、Kac*HK、Kac*N、Kac*S、Kac*T、Kac*D。大约36.76%的乙酰化赖氨酸位于有序二级结构区域。大部分赖氨酸乙酰化蛋白定位于叶绿体（39%）和细胞质（29%）。乙酰化蛋白中最大的一类是ATP合成酶、核糖体蛋白和苹果酸脱氢酶（NADP）等，它们在生物过程中与代谢有关（38%）。这些乙酰化的蛋白质主要富集在三个主要的光合作用蛋白质复合物：光系统I，光系统II和细胞色素b6/f复合物。与糖酵解和次生代谢产物合成相关的乙酰化蛋白在氮再供应条件下增加或减少。蛋白质相互作用（PPI）分析表明，乙酰化蛋白的相互作用主要涉及光合作用和核糖体。结果表明，赖氨酸乙酰化蛋白可能在茶叶代谢过程中起调节作用。这些关键的调节作用主要涉及代谢过程的各个方面，尤其是光合作用、糖酵解和次生代谢。发现许多与光合作用和糖酵解相关的蛋白质发生了乙酰化，包括LHCA 1、LHCA 3、LHCB 6、psaE、psaD、psaN、GAPDH、PEPC、ENL和petC。与黄酮类化合物相关的PAL、DFR、柚皮素3-双加氧酶和CHI等蛋白质也发生了乙酰化。这些数据为进一步研究茶树赖氨酸乙酰化的生理生化和遗传学作用提供了重要资料。数据可通过ProteomeXchange获得，标识符为PXD 008931。本文的在线版本（10.1186/s12864-018-5250-4）包含补充材料，可供授权用户使用。
Nε-Acetylation of lysine residues, a frequently occurring post-translational modification, plays important functions in regulating physiology and metabolism. However, the information of global overview of protein acetylome under nitrogen-starvation/resupply in tea (Camellia sinensis) leaves was limited. And the full function of lysine acetylated proteins of tea plants in nitrogen absorption and assimilation remains unclear. Here, we performed the global review of lysine acetylome in tea leaves under nitrogen (N)-starvation/resupply, using peptide prefractionation, immunoaffinity enrichment, and coupling with high sensitive LC-MS/MS combined with affinity purification analysis. Altogether, 2229 lysine acetylation sites on 1286 proteins were identified, of which 16 conserved motifs in E*KacK, Kac*K, Kac*R, Kac*HK, Kac*N, Kac*S, Kac*T, Kac*D, were extracted from 2180 acetylated peptides. Approximately, 36.76% of the acetylated lysines were located in the regions of ordered secondary structures. The most of the identified lysine acetylation proteins were located in the chloroplast (39%) and cytoplasm (29%). The largest group of acetylated proteins consisted of many enzymes, such as ATP synthase, ribosomal proteins and malate dehydrogenase [NADP], which were related to metabolism (38%) in the biological process. These acetylated proteins were mainly enriched in three primary protein complexes of photosynthesis: photosystem I, photosystem II and the cytochrome b6/f complex. And some acetylated proteins related to glycolysis and secondary metabolite biosynthesis were increased/decreased under N-resupply. Moreover, the PPI (protein-protein interaction) analysis revealed that the diverse interactions of identified acetylated proteins mainly involved in photosynthesis and ribosome. The results suggested that lysine acetylated proteins might play regulating roles in metabolic process in tea leaves. The critical regulatory roles mainly involved in diverse aspects of metabolic processes, especially in photosynthesis, glycolysis and secondary metabolism. A lot of proteins related to the photosynthesis and glycolysis were found to be acetylated, including LHCA1, LHCA3, LHCB6, psaE, psaD, psaN, GAPDH, PEPC, ENL and petC. And some proteins related to flavonoids were also found to be acetylated, including PAL, DFR, naringenin 3-dioxygenase and CHI. The provided data may serve as important resources for exploring the physiological, biochemical, and genetic role of lysine acetylation in tea plants. Data are available via ProteomeXchange with identifier PXD008931. The online version of this article (10.1186/s12864-018-5250-4) contains supplementary material, which is available to authorized users.