Submission Date


Document Type

Paper- Restricted to Campus Access


Biochemistry & Molecular Biology


Dale Cameron

Committee Member

Samantha Wilner

Committee Member

Maureen Cumpstone

Department Chair

Eric Williamsen

Project Description

Prions are infectious, self-propagating protein aggregates that cause diverse neurodegenerative diseases in mammals including Transmissible Spongiform Encephalopathies (TSEs). In yeast, prions are not disease-causing agents and instead may have beneficial functions, including adaptation to stress, by altering gene expression and protein production in cells. To ensure the proper folding of proteins, cells have developed various quality control systems. One of the cell’s quality control mechanisms is the use of ribosome-associated chaperone complexes, allowing co-translational quality control as the amino acid chain is synthesized by the ribosome. The Ribosome-Associated Complex (RAC) and Nascent Polypeptide-Associated Complex (NAC) constitute the ribosome-associated chaperone complexes and are conserved in eukaryotic organisms from yeast to humans. Despite the increased interest in the study of individual complexes, limited information on the interaction between the two complexes is available. Therefore, in this research, we have investigated the role of the RAC and NAC subunits in response to multiple types of environmental stress conditions. Our experiment suggests that the subunits of RAC and NAC may contribute differently to each type of environmental stress and that certain subunits may perform additional functions beyond chaperoning. In addition, our preliminary work shows a trend of better stress tolerance in cells with the [PSI+] prion compared to [psi-] cells that lack the prion, consistent with the hypothesis that novel proteins produced in [PSI+] cells may help to promote stress survival.