—
Phosphorylation, glycosylation, acetylation, ubiquitination, SUMOylation and many others are included in protein post-translational modifications (PTMs). As a counterpart of ubiquitination, protein SUMOylation has become more popular in research hotspots recently. As one of PTMs, in which a member of the small ubiquitin-like modifier (SUMO) family of proteins is conjugated to lysine (Lys) residues in target proteins, SUMOylation modification is reversible and dynamic process. During the process, the modified proteins can be deSUMOylated.SUMOylation plays significant roles in various biological functions, for example, in cell growth, migration, cellular responses to stress and tumorigenesis. The balance between SUMOylation and deSUMOylation has been related to the onset and progression of many diseases, including cardiac disease, neurodegenerative disease and cancers. With the advance of knowledge on its biological functions, SUMOylation has been reported to regulate protein subcellular localization, protein–DNA binding, protein–protein interactions, transcriptional regulation, DNA repair and genome organization.
Moreover, with the continuous development of bioinformatics and mass spectrometry, several accurate and high-throughput methods have been implemented to explore small ubiquitin-like modifier-modified substrates and sites, which is helpful for deciphering protein SUMOylation-mediated molecular mechanisms of disease.
Creative Proteomics has established a highly sensitive platform (Ion Chromatography, High Performance Liquid Chromatography (HPLC) and Matrix Assisted Laser Desorption Ionization Mass Spectrometry (MALDI-MS)) that can analyze sumoylation in multiple samples and in both eukaryotic and prokaryotic organisms. In addition, the company has optimized its protocol to enable more fast and sensitive site mapping service for sumoylation analysis.
Recent studies about sumoylation
In order to study the mechanism of the interaction between protein ubiquitination and SUMO modification in meiosis, researchers first screened the function of SUMO targeting ubiquitin ligase during yeast meiosis and found that the loss of a protein in the complex Slx5p-Slx8p will affect the normal progress of meiosis. Further studies have found that knocking out SLX8 affects the degradation of meiotic homologous interchromosomal intercombination complex protein components, while failure to effectively degrade the synaptic complex protein affects the proper separation of homologous chromosomes. Slx8p's ubiquitin ligase activity and the SUMO recognition domain are critical to its function in meiosis, indicating that the interaction of Slx8p-mediated protein ubiquitination and SUMOylation modification in the correct separation of meiotic homologous chromosomes play an important role. To further verify this conclusion, the researchers expressed the fusion ubiquitin-SUMO protein in the SLX8 knockout strain, artificially linked ubiquitination and SUMO modification, and found that the ubiquitin-SUMO fusion protein can partially rescue the SLX8 knockout caused by Abnormal meiosis. In order to further clarify the key role of Slx5p-Slx8p in the meiosis process, the researchers reconstructed the Slx5p-Slx8p ubiquitination system in vitro and found that Slx5p-Slx8p can be SUMO-modified in the complex association protein Zip1p and Ecm11p Directly catalyze the modification of ubiquitination. Using the AID system to induce Ecm11p protein degradation during the meiosis of the SLX8 knockout strain can partially rescue its meiotic abnormalities. Therefore, SUMO targeting ubiquitin ligase Slx5p-Slx8p can catalyze the ubiquitination and mediate its degradation on the SUMO-modified synaptic complex protein Ecm11p, thereby regulating the correct separation of homologous chromosomes.
The above work illustrates for the first time that SUMO targeting ubiquitin ligase Slx5p-Slx8p mediates the interaction between protein ubiquitination and SUMO modification during meiosis, promotes the degradation of SUMO-modified associative complex protein and regulates the correct separation of homologous chromosomes. It provides new ideas for people to further understand the complex regulation of protein post-translational modification.
Contact Info:
Name: Melisa Geoge
Email: Send Email
Organization: Creative Proteomics
Address: 45-1 Ramsey Road
Phone: 6316197922
Website: https://www.creative-proteomics.com/pronalyse/
Release ID: 88957845
Google
RSS