“Ancient Role of Prolyl Hydroxylation in Protist Oxygen Sensing is Modulated by Glycosylation and Targets a Ubiquitin Ligase,” will be presented by Dr. Chris West, University of Oklahoma Health Sciences Center. Posttranslational modifications introduce incredible diversity to the function and regulation of proteins. Discovery of a novel form of cytoplasmic glycosylation in the social amoeba Dictyostelium has led to characterization of a mechanism of oxygen sensing that shares a common enzymatic basis with that of humans, with a novel twist that instead of regulating the substrate of a polyubiquitin ligase, the ubiquitin ligase itself appears to be regulated. Current evidence suggests that prolyl hydroxylation and glycosylation influences Skp1 folding and E3(SCF)ubiquitin ligase assembly, and that peripheral glycosylation terminates rather than enables the modulating cellular function of the glycosylation pathway. Other evidence shows that key elements of this novel modification pathway have a conserved oxygen sensing functions in other protists including the agent for human toxoplasmosis, Toxoplasma gondii.
The seminar begins at 4:00 p.m., preceded by a reception at 3:30 p.m. The seminar is free and open to the public. The Beadle Center is located at 1901 Vine Street. The complete schedule of seminars may be found at http://biotech.unl.edu/
More details at: http://go.unl.edu/df7