Submission Date

4-26-2024

Document Type

Paper- Restricted to Campus Access

Department

Biochemistry & Molecular Biology

Adviser

Dale Cameron

Committee Member

Anthony Lobo

Committee Member

Denise Finney

Department Chair

Eric Williamsen

Department Chair

Anthony Lobo

Project Description

Proteins are essential, functionally diverse macromolecules found in all living cells. Their structure is integral to their function, and they can fold in a variety of different conformations, which results in a change or loss of function. A specific class of misfolded proteins, known as prions, can transmit their structure onto natively folded proteins of the same type. While they are not known to cause disease in Saccharomyces cerevisiae (yeast), prions and similar aggregation patterns have been linked to neurodegenerative diseases in other organisms. Prion disease-causing proteins, like mammalian PrPSC causing transmissible spongiform encephalopathies (TSEs), and proteins underlying prion-like disease states, like α-synuclein (Parkinson’s disease), amyloid-β (Alzheimer’s disease), and Huntingtin (Huntington’s disease) are some of the most well-known cases. Cells have developed machinery to promote correct protein folding, consisting primary of molecular chaperones. These proteins are varied throughout the cell in location and function. Some exist on the nascent polypeptide exit tunnel of ribosomes to ensure proteins fold correctly during synthesis. Two of these complexes are known as the ribosome-associated complex (RAC) and nascent chain-associated complex (NAC), have been shown in previous studies from the Cameron lab to individually play important roles in reducing prion formation and promoting survival in yeast experiencing stress. This study seeks to better understand the functional relationship between the RAC and NAC components in yeast by comparing prion formation and stressed cell survival between pairwise deletion strains lacking combinations of RAC and NAC subunits.

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