Michael M. Pierce
Prions are infectious proteins that are autocatalyzing (formed by altering a regular protein into the structurally different prion form), and are associated with many neurodegenerative 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 over-expression of the Ure2 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 was to investigate how the presence or absence of the URM1 gene affects the overall formation of prions. The data showed that over-expression of proteins was seen to increase prion formation, and that over-expression yielding prions were less sustainable across generations. Also shown was that deletion mutants yielded higher numbers of prions than their wild-type counterparts.Curing through use of over-expression 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.
"The Influence of Ubiquitin-Related Modifier Protein URM1 on Prion Formation,"
Bridges: A Journal of Student Research: Vol. 7
, Article 1.
Available at: https://digitalcommons.coastal.edu/bridges/vol7/iss7/1