Submission Date
4-24-2015
Document Type
Paper- Restricted to Campus Access
Department
Biology
Adviser
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.
Recommended Citation
Selechnik, Daniel, "Innovation of a Novel Prion Reporter System in Saccharomyces cerevisiae" (2015). Biology Honors Papers. 6.
https://digitalcommons.ursinus.edu/biology_hon/6
