Institute of Biochemistry and Biophysics, Polish Academy of Science, Warszawa, Poland.
Friedrich Miescher Institute for Biomedical Research, Department of Mechanisms of Cancer, Maulbeerstrasse 66, CH-4058, Basel, Switzerland.
Sci Rep. 2018 Jan 18;8(1):1139. doi: 10.1038/s41598-018-19424-9.
Post-translational modification by small ubiquitin-related modifier (SUMO) is a key regulator of cell physiology, modulating protein-protein and protein-DNA interactions. Recently, SUMO modifications were postulated to be involved in response to various stress stimuli. We aimed to identify the near complete set of proteins modified by SUMO and the dynamics of the modification in stress conditions in the higher eukaryote, Caenorhabditis elegans. We identified 874 proteins modified by SUMO in the worm. We have analyzed the SUMO modification in stress conditions including heat shock, DNA damage, arsenite induced cellular stress, ER and osmotic stress. In all these conditions the global levels of SUMOylation was significantly increased. These results show the evolutionary conservation of SUMO modifications in reaction to stress. Our analysis showed that SUMO targets are highly conserved throughout species. By comparing the SUMO targets among species, we approximated the total number of proteins modified in a given proteome to be at least 15-20%. We developed a web server designed for convenient prediction of potential SUMO modification based on experimental evidences in other species.
由小泛素相关修饰物（SUMO）介导的翻译后修饰是细胞生理学的关键调节因子，可调节蛋白质-蛋白质和蛋白质-DNA相互作用。最近，有人推测SUMO修饰参与了对各种应激刺激的反应。我们旨在确定在高等真核生物秀丽隐杆线虫中被SUMO修饰的近乎完整的蛋白质组以及应激条件下修饰的动态变化。我们在该线虫中鉴定出874种被SUMO修饰的蛋白质。我们分析了包括热休克、DNA损伤、亚砷酸盐诱导的细胞应激、内质网应激和渗透压应激在内的应激条件下的SUMO修饰情况。在所有这些条件下，SUMO化的整体水平均显著增加。这些结果表明SUMO修饰在应激反应中的进化保守性。我们的分析表明，SUMO靶标在整个物种中高度保守。通过比较不同物种间的SUMO靶标，我们估计给定蛋白质组中被修饰蛋白质的总数至少为15% - 20%。我们基于其他物种的实验证据开发了一个网络服务器，用于方便地预测潜在的SUMO修饰。
