Submission Date


Document Type

Paper- Restricted to Campus Access




Dr. Dale Cameron

Committee Member

Dr. Beth Bailey

Committee Member

Dr. Ronald Hess

Committee Member

Dr. Dale Cameron

Department Chair

Dr. Kathryn Goddard

Project Description

Prions are misfolded proteins that become infectious and propagate themselves by causing the misfolding of other copies of the same type of protein. The [PSI+] prion results from misfolded conformations of the translation termination factor Sup35, and in these conformations, it cannot properly terminate translation at stop codons. Read-through of stop codons occurs due to decreased availability of normally folded Sup35, causing longer polypeptides to form. There are currently reporter systems that qualitatively assess the prion condition of cells by causing prion-containing and prion-free cells to form colonies of different colors. This study sought to engineer a quantitative reporter system in which the amount of Green Fluorescent Protein (GFP) produced is directly proportional to stop codon read-through. I hypothesized that by measuring GFP fluorescence intensity, the amount of [PSI+] prion that is formed could be quantitatively assessed.