Germplasm Bank of Wild Species, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming 650201, China.
Yunnan Key Laboratory for Wild Plant Resources, Department of Economic Plants and Biotechnology, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming 650201, China.
Cells. 2022 Jun 17;11(12):1947. doi: 10.3390/cells11121947.
Protein post-translational modification (PTM) is an efficient biological mechanism to regulate protein structure and function, but its role in plant responses to heavy metal stress is poorly understood. The present study performed quantitative succinyl-proteome profiling using liquid chromatography−mass spectrometry analysis to explore the potential roles of lysine succinylation modification in turnip seedlings in response to cadmium (Cd) stress (20 μM) under hydroponic conditions over a short time period (0−8 h). A total of 547 succinylated sites on 256 proteins were identified in the shoots of turnip seedlings. These succinylated proteins participated in various biological processes (e.g., photosynthesis, tricarboxylic acid cycle, amino acid metabolism, and response to stimulation) that occurred in diverse cellular compartments according to the functional classification, subcellular localization, and protein interaction network analysis. Quantitative analysis showed that the intensities of nine succinylation sites on eight proteins were significantly altered (p < 0.05) in turnip shoots after 8 h of Cd stress. These differentially succinylated sites were highly conserved in Brassicaceae species and mostly located in the conserved domains of the proteins. Among them, a downregulated succinylation site (K150) in the glycolate oxidase protein (Gene0282600.1), an upregulated succinylation site (K396) in the catalase 3 protein (Gene0163880.1), and a downregulated succinylation site (K197) in the glutathione S-transferase protein (Gene0315380.1) may have contributed to the altered activity of the corresponding enzymes, which suggests that lysine succinylation affects the Cd detoxification process in turnip by regulating the H2O2 accumulation and glutathione metabolism. These results provide novel insights into understanding Cd response mechanisms in plants and important protein modification information for the molecular-assisted breeding of Brassica varieties with distinct Cd tolerance and accumulation capacities.
蛋白质翻译后修饰(PTM)是一种有效的生物机制,可以调节蛋白质的结构和功能,但其在植物应对重金属胁迫中的作用还知之甚少。本研究采用液相色谱-质谱分析进行定量琥珀酰化蛋白质组学分析,以探索赖氨酸琥珀酰化修饰在白菜幼苗应对水培条件下短期(0-8 h)镉(Cd)胁迫(20 μM)中的潜在作用。在白菜幼苗的地上部分共鉴定到 256 种蛋白质上的 547 个琥珀酰化位点。根据功能分类、亚细胞定位和蛋白质相互作用网络分析,这些琥珀酰化蛋白参与了光合作用、三羧酸循环、氨基酸代谢和对刺激的反应等各种生物过程,这些过程发生在不同的细胞区室中。定量分析表明,Cd 胁迫 8 h 后,白菜地上部分有 8 个蛋白上的 9 个琥珀酰化位点的强度发生了显著变化(p < 0.05)。这些差异琥珀酰化位点在芸薹属物种中高度保守,且大部分位于蛋白的保守结构域内。其中,糖酸氧化酶蛋白(Gene0282600.1)中的下调琥珀酰化位点(K150)、过氧化氢酶 3 蛋白(Gene0163880.1)中的上调琥珀酰化位点(K396)和谷胱甘肽 S-转移酶蛋白(Gene0315380.1)中的下调琥珀酰化位点(K197)可能导致相应酶活性的改变,表明赖氨酸琥珀酰化通过调节 H2O2 积累和谷胱甘肽代谢影响白菜的 Cd 解毒过程。这些结果为理解植物对 Cd 的响应机制提供了新的见解,并为具有不同 Cd 耐性和积累能力的芸薹属品种的分子辅助育种提供了重要的蛋白质修饰信息。