The influence of ubiquitin-related modifier protein URM1 on prion formation

Prions are infections proteins that are auto-catalyzing (form by altering a regular protein into the structurally different prion form), and are the cause of many common diseases such as Alzheimer’s, Parkinson’s, Huntington’s, and Bovine Spongiform encephalopathy (or Mad Cow disease). This experiment tested the effect of three different plasmids, pH317, pER62 and pmp46 on prion formation in both wild-type and Urm1 deletion mutants in the yeast Saccharomyces cerevisiae. The proposed hypothesis was overexpression of the prion forming protein would increase the frequency of prion formation, as well as yield less sustainable prion amyloids (or prion aggregations) that are easier to cure. Another purpose of this experiment is to investigate how the presence or absence of the URM1 gene, that can form a prion, affects the overall formation of prions. The data showed both that overexpression of proteins was seen to increase prion formation, and that overexpression yielded prions that were less sustainable across generations. Also shown was that deletion mutants yielded higher numbers of prions than their wild-type counterparts. Efforts to cure prions through use of overexpression and guanidine, which inhibits the chaperone proteins associated with dividing prions during cellular division, proved inconclusive because there was no visible difference between any of the three plasmids. Introduction Initially, prions were studied because of the threat they posed to food supplies for humans because of the disease they cause in mammals. They are now being studied extensively because of their abilities to mediate non-Mendelian inheritance, produce additional prions, and display