期刊
SCIENTIFIC REPORTS
卷 8, 期 -, 页码 -出版社
NATURE RESEARCH
DOI: 10.1038/s41598-018-19424-9
关键词
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资金
- Novartis Research Foundation
- National Science Centre (Narodowe Centrum Nauki) [DEC 1/Z/2011/01/M/NZ2/02997]
- NIH Office of Research Infrastructure Programs [P40 OD010440]
- OFFICE OF THE DIRECTOR, NATIONAL INSTITUTES OF HEALTH [P40OD010440] Funding Source: NIH RePORTER
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.
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