Featured article:
Identification of SUMO conjugation sites in the budding yeast proteome
Miguel Esteras, I-Chun Liu, Ambrosius P. Snijders, Adam Jarmuz & Luis Aragon
Post-translational modification by the small ubiquitin-like modifier (SUMO) is an important mechanism regulating protein function. Identification of SUMO conjugation sites on substrates is a challenging task. Here we employed a proteomic method to map SUMO acceptor lysines in budding yeast proteins. We report the identification of 257 lysine residues where SUMO is potentially attached. Amongst the hits, we identified already known SUMO substrates and sites, confirming the success of the approach. In addition, we tested several of the novel substrates using SUMO immunoprecipitation analysis and confirmed that the SUMO acceptor lysines identified in these proteins are indeed bona fide SUMOylation sites. We believe that the collection of SUMO sites presented here is an important resource for future functional studies of SUMOylation…
About us
News
Meet the editorial board
Most viewed last month
- Recent Insights into the HIV/AIDS Pandemic
- Autophagy: machinery and regulation
- Formyl-methionine as a degradation signal at the N-termini of bacterial proteins
- Identification of SUMO conjugation sites in the budding yeast proteome
- Electron microscopy for ultrastructural analysis and protein localization in Saccharomyces cerevisiae
- Understanding structure, function, and mutations in the mitochondrial ATP synthase
- Coordinate responses to alkaline pH stress in budding yeast
- Thiol trapping and metabolic redistribution of sulfur metabolites enable cells to overcome cysteine overload
- Metabolites in aging and autophagy
- Loss of wobble uridine modification in tRNA anticodons interferes with TOR pathway signaling
Publish with MIC
Social media
Newsfeeds
