Ubiquitination-mediated protein degradation and modification:an emerging theme in plant-microbe interactions

translational 以后修正对蛋白质稳定性并且到蛋白质活动的调整中央。蛋白质修正的各种各样的类型例如 phosphorylation， methylation， acetylation， myristoylation， glycosylation，和 ubiquitination，被报导了。在他们之中， ubiquitination 把自己与其它区分开来因为大多数 ubiquitinated 蛋白质为降级被指向到 26S proteasome。ubiquitin/26S proteasome 系统在房间组成主要蛋白质降级小径。在最近的年里，在众多的真核细胞的细胞的函数的控制的 ubiquitination 机械的重要性逐渐地被欣赏了。增加 E3 ubiquitin ligases 和他们的底层的数字，包括许多必要细胞的管理者被识别了。过去的几年里的研究表明了 ubiquitination 系统为大量植物是重要的发展过程和回答到不能生活、关於生命的压力。这评论从在植物微生物相互作用起重要作用的植物和病原体在联系 ubiquitination 的蛋白质的功能的分析讨论最近的进展。

Post-translational modification is central to protein stability and to the modulation of protein activity. Various types of protein modification, such as phosphorylation, methylation, acetylation, myristoylation, glycosylation, and ubiquitination, have been reported. Among them, ubiquitination distinguishes itself from others in that most of the ubiquitinated proteins are targeted to the 26S proteasome for degradation. The ubiquitin/26S proteasome system constitutes the major protein degradation pathway in the cell. In recent years, the importance of the ubiquitination machinery in the control of numerous eukaryotic cellular functions has been increasingly appreciated. Increasing number of E3 ubiquitin ligases and their substrates, including a variety of essential cellular regulators have been identified. Studies in the past several years have revealed that the ubiquitination system is important for a broad range of plant developmental processes and responses to abiotic and biotic stresses. This review discusses recent advances in the functional analysis of ubiquitination-associated proteins from plants and pathogens that play important roles in plant-microbe interactions.