Document Type

Paper- Restricted to Campus Access

Publication Date

4-30-2020

Faculty Mentor

Dale Cameron

Abstract

In order to be useful, our genetic information needs to be translated into functional proteins. Proteins carry out many important functions within our cells. Once built, proteins must fold in specific and correct ways to function properly. When proteins misfold they can be very detrimental to the organism, since misfolded proteins can lose their intended function or potentially even acquire new, harmful functions. One classification of misfolded proteins is called prions. Prions are able to interact with correctly folded copies of the same type of proteins and transform them into the misfolded prion structure. These misfolded proteins can then clump together to form aggregates that are associated with mammalian neurological diseases like Creutzfeldt–Jakob disease and Kuru in humans, Scrapie in sheep, and Mad Cow disease in cows. However, while in mammals, prions cause diseases, it has been shown that in yeast, prions may provide a fitness advantage in some environments. For example, the [PSI+] prion alters the way in which proteins are synthesized by cells, which can impact the functions and abundance of many different proteins and therefore has the potential to profoundly affect cell physiology. Previous work from our lab has shown that cells with the [PSI+] prion have reduced levels of glucose transporters.

Comments

Presented as part of the Ursinus College Celebration of Student Achievement (CoSA) held April 23 – April 30, 2020.

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