蛋白质泛素化介导的植物低温胁迫反应

Low Temperature Stress Response Mediated by Protein Ubiquitination in Plant

低温胁迫限制植物的生长发育及其地理分布。不同物种在低温胁迫反应过程中发生了重大的转录组重新编程,许多蛋白质被认为是这种适应性反应的重要因子。泛素化是一种翻译后修饰,能够调控蛋白的丰度、活性、亚细胞区隔和转运,并参与低温应答过程。E3是泛素-蛋白酶体系统的主要组成部分,识别目标蛋白,并将泛素从E2上转移到目标蛋白上。由于E3具有底物识别的特异性,从而调控植物多种低温胁迫反应相关的信号通路。以此为基础,总结了参与泛素-蛋白酶体系统的组成成分,并详细阐述了E3在低温胁迫反应中的作用。

Low-temperature stress restricts plant growth,development,and geographical distribution.A large transcriptome reprogramming occurs as a response to low-temperature stress in diverse species,and a number of proteins have been identified as important factors in this adaptive response.Ubiquitination is a post-translational modification that regulates abundance,activities,subcellular compartmentalization and transport,and involved in the low-temperature stress response.The E3 is a major component of the ubiquitinproteasome system that recognizes the target protein and transfer of ubiquitin from the E2 to the target protein.Owing to its substrate recognition specificity,the E3 regulates various signaling pathways involved in the low-temperature stress response in plants.Therefore,components involved in the ubiquitin-proteasome system are summarized in the present study,and the role of E3 in the low-temperature stress response is described in detail.