Submission Date

7-19-2024

Document Type

Paper- Restricted to Campus Access

Department

Biology

Faculty Mentor

Dale Cameron

Second Faculty Mentor

Christina Kelly

Comments

Presented during the 26th Annual Summer Fellows Symposium, July 19, 2024 at Ursinus College.

This work was funded by the National Institutes of Health.

Project Description

Proteins are one of the four macromolecules essential to life. The different forces acting on each amino acid within a protein determines the manner in which it will fold, which in turn determines its structure and function. Prions self-propagate by changing the configuration of a correctly folded protein of the same type, which leads to protein aggregates and typically has a detrimental effect on cellular functions. In mammals, prion or prion-like infections lead to neurodegenerative diseases such as Alzheimer’s, Huntington’s, or Creutzfeldt-Jakob disease. One factor that may increase the rate of protein misfolding is ribosomal stalling during translation, where protein translation slows down or completely ceases. This leaves the nascent protein exposed to the cellular environment without the regulatory system to ensure proper folding. Using Saccharomyces cerevisiae with artificial ribosomal stalling sequences to halt protein formation during the synthesis of Sup35p, the mechanism of spontaneous prion formation may be investigated.

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