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泛素化酶在植物与非生物环境相互作用中的作用。

Role of ubiquitination enzymes in abiotic environmental interactions with plants.

机构信息

National Institute of Plant Genome Research, Aruna Asaf Ali Marg, New Delhi, 110067, India.

National Institute of Plant Genome Research, Aruna Asaf Ali Marg, New Delhi, 110067, India.

出版信息

Int J Biol Macromol. 2021 Jun 30;181:494-507. doi: 10.1016/j.ijbiomac.2021.03.185. Epub 2021 Mar 30.

DOI:10.1016/j.ijbiomac.2021.03.185
PMID:33798570
Abstract

Ubiquitination, a post-translational modification, plays a crucial role in various aspects of plant development and stress responses. Protein degradation by ubiquitination is well established and ubiquitin is the main underlying component directing the turnover of proteins. Recent reports have also revealed the non-proteolytic roles of ubiquitination in plants. In the past decade, ubiquitination has emerged to be one of the most important players in modulating plant's responses to abiotic stresses, which led to identification of specific E3 ligases and their targets involved in the process. Most of the E3 ligases play regulatory roles by modifying the stability and accumulation of stress responsive regulatory proteins, such as transcription factors, thus, modifying the downstream responses, or by degrading the proteins involved in the downstream cascade itself. In this review, we summarize and highlight the recent advances in the field of ubiquitination-mediated regulation of plant's responses to various abiotic stresses including limited nutrient availability and metal toxicity. The non-proteolytic role of ubiquitination in epigenetic regulation of abiotic stress induced response has also been discussed.

摘要

泛素化是一种翻译后修饰,在植物发育和应激反应的各个方面都起着至关重要的作用。通过泛素化进行的蛋白质降解已得到充分证实,而泛素是指导蛋白质周转的主要潜在成分。最近的报告还揭示了泛素化在植物中的非蛋白水解作用。在过去的十年中,泛素化已成为调节植物对非生物胁迫反应的最重要因素之一,这导致了特定 E3 连接酶及其参与该过程的靶标的鉴定。大多数 E3 连接酶通过修饰应激反应调节蛋白(如转录因子)的稳定性和积累来发挥调节作用,从而改变下游反应,或者通过降解下游级联反应本身涉及的蛋白质来发挥调节作用。在这篇综述中,我们总结和强调了泛素化介导的植物对各种非生物胁迫反应(包括有限的养分供应和金属毒性)的调节的最新进展。泛素化在非生物胁迫诱导反应的表观遗传调控中的非蛋白水解作用也已被讨论。

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