Studies on adaptation ability to environmental stresses during structural transition of plant proteasome

蛋白酶体是一个庞大的蛋白质复合体，可以降解受损的和选择性泛素化的蛋白质，并与各种环境应激反应有关。虽然在哺乳动物中对蛋白酶体的生化特性进行了很好的研究，但植物蛋白酶体的细节仍不清楚。在这里，我们使用蛋白质组学的方法来揭示植物蛋白酶体的详细亚单位组成。我们的2D电泳法和LC-MS/MS分析结合亲和纯化证明，由于植物特有的基因复制和可能的翻译后修饰，蛋白酶体的亚基组成具有高度的异质性。此外，我们的研究表明，蛋白酶体的活性受到病原体信号转译后修饰的影响。我们的研究揭示了植物蛋白酶体组成和调控机制的新见解，这可能有助于提高作物对病原菌的抗性和农业上的作物产量。

The proteasome is a huge protein complex that degrades damaged and selective ubiquitinated proteins, and is related to various environmental stress responses. Although the biochemical characteristic of the proteasome is well-studied in mammals, the details of the plant proteasome remains unclear. Here, we used a proteomics approach to reveal the detailed subunit composition of the plant proteasome. Our 2D electrophoresis and LC-MS/MS analyses combined with affinity purification demonstrated the highly heterogeneous subunit composition of the proteasome due to plant-specific gene duplication and putative post-translational modification in plant cells. Moreover, our studies demonstrated that proteasome activity is affected by post-translational modification in response to pathogen signaling. Our study revealed new insights into the plant proteasome composition and regulatory mechanism, which may contribute to increased pathogen resistance and improved crop yield in agriculture.