The glycation of ubiquitin with ribose 5-phosphate (R5P) and glucose was studied to determine the effect of post-translationally modified ubiquitin on intracellular proteolysis. Our investigations focused on identifying the location of glycation sites on the ubiquitin protein and on developing a method for assessing the effect that glycation has on ubiquitin activity. A novel method which employs yeast cytochrome c as a ubiquitination target substrate and LC-MS for subsequent analysis is under development for use in assessing the functionality of modified ubiquitin. Preliminary results suggest that this is a robust method for the detection of ubiquitination. Further refinement of this method is necessary before the effects of glycation on ubiquitination can be analyzed.


Mark Esposito

Roger Sandwick
Associate Professor of Chemistry and Biochemistry

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