Key Laboratory of Chinese Ministry of Agriculture for Nuclear-Agricultural Sciences, Institute of Nuclear-Agricultural Sciences, Zhejiang University, Zhejiang, 310058, China.
Proteomics. 2019 Oct;19(20):e1900158. doi: 10.1002/pmic.201900158. Epub 2019 Sep 25.
Increasing evidence shows that the succinylation of lysine residues mainly regulates enzymes involved in the carbon metabolism pathway, in both prokaryotic and eukaryotic cells. Deinococcus radiodurans is one of the most radioresistant organisms on earth and is famous for its robust resistance. A major goal in the current study of protein succinylation is to explore its function in D. radiodurans. High-resolution LC-MS/MS is used for qualitative proteomics to perform a global succinylation analysis of D. radiodurans and 492 succinylation sites in 270 proteins are identified. These proteins are involved in a variety of biological processes and pathways. It is found that the enzymes involved in nucleic acid binding/processing are enriched in D. radiodurans compared with their previously reported levels in other bacteria. The mutagenesis studies confirm that succinylation regulates the enzymatic activities of species-specific proteins PprI and DdrB, which belong to the radiation-desiccation response regulon. Together, these results provide insight into the role of lysine succinylation in the extreme resistance of D. radiodurans.
越来越多的证据表明，赖氨酸残基的琥珀酰化主要调节原核和真核细胞中参与碳代谢途径的酶。耐辐射球菌是地球上最具放射性抗性的生物之一，以其强大的抗性而闻名。目前研究蛋白质琥珀酰化的一个主要目标是探索其在耐辐射球菌中的功能。高分辨率 LC-MS/MS 用于定性蛋白质组学，对耐辐射球菌进行全局琥珀酰化分析，鉴定出 270 种蛋白质中的 492 个琥珀酰化位点。这些蛋白质参与多种生物过程和途径。研究发现，与其他细菌先前报道的水平相比，参与核酸结合/加工的酶在耐辐射球菌中富集。诱变研究证实，琥珀酰化调节属于辐射干燥反应调控子的种特异性蛋白 PprI 和 DdrB 的酶活性。总之，这些结果深入了解了赖氨酸琥珀酰化在耐辐射球菌极端抗性中的作用。
