Submission Date


Document Type

Paper- Restricted to Campus Access


Biochemistry & Molecular Biology


Dale Cameron

Committee Member

Andrew Jones

Committee Member

Eric Williamsen

Department Chair

Eric Williamsen

Project Description

Prions are a class of misfolded proteins that are infectious due to their ability to self-propagate and form protein aggregates, which are associated with diseases like Mad-Cow Disease and Creutzfeldt-Jakob. Fortunately, our cells have a natural defense mechanism, called chaperones, that can suppress the formation of these prions by helping to fold nascent polypeptide chains into their correct structure. In previous research studies performed in the Cameron Lab using yeast as a model organism, the Ribosome-Associated Complex (RAC) chaperone has been linked to the suppression of prion formation in cells. Researchers have identified human homologs of the RAC components that are very similar in structure and function to those in yeast. The purpose of this study is to determine if yeast cells lacking their own RAC components can functionally use the human homologs to suppress prion formation and toxicity of disease-associated proteins.


This work was supported by Ursinus College and by the National Institute of General Medical Sciences of the National Institutes of Health under Award Number R15GM119081 (to DMC).