Marondedze Claudius, Elia Giuliano, Thomas Ludivine, Wong Aloysius, Gehring Chris
Division of Biological and Chemical Science and Engineering, King Abdullah University of Science and Technology, Thuwal, Saudi Arabia.
Rijk Zwaan, De Lier, Netherlands.
Front Plant Sci. 2021 Apr 8;12:638392. doi: 10.3389/fpls.2021.638392. eCollection 2021.
Arginine deimination, also referred to as citrullination of proteins by L-arginine deiminases, is a post-translational modification affecting histone modifications, epigenetic transcriptional regulation, and proteolysis in animals but has not been reported in higher plants. Here we report, firstly, that proteome contains proteins with a specific citrullination signature and that many of the citrullinated proteins have nucleotide-binding regulatory functions. Secondly, we show that changes in the citrullinome occur in response to cold stress, and thirdly, we identify an protein with peptidyl arginine deiminase activity that was shown to be calcium-dependent for many peptide substrates. Taken together, these findings establish this post-translational modification as a hitherto neglected component of cellular reprogramming during stress responses.
精氨酸脱亚胺作用，也被称为L-精氨酸脱亚胺酶对蛋白质的瓜氨酸化作用，是一种翻译后修饰，影响动物体内的组蛋白修饰、表观遗传转录调控和蛋白水解，但在高等植物中尚未见报道。在此，我们首先报道，蛋白质组中含有具有特定瓜氨酸化特征的蛋白质，且许多瓜氨酸化蛋白具有核苷酸结合调节功能。其次，我们表明瓜氨酸化蛋白质组的变化会响应冷胁迫而发生，第三，我们鉴定出一种具有肽基精氨酸脱亚胺酶活性的蛋白质，该酶对许多肽底物的活性表现出钙依赖性。综上所述，这些发现确立了这种翻译后修饰是应激反应期间细胞重编程中一个迄今被忽视的组成部分。
