Submission Date

5-4-2026

Document Type

Paper- Restricted to Campus Access

Department

Biology

Adviser

Dale Cameron

Committee Member

Erica Gorenberg

Committee Member

Molly O'Rourke-Friel

Department Chair

Denise Finney

Project Description

The misfolding of proteins can result in a change in or loss of function. Organisms have evolved mechanisms to prevent or reduce misfolding, producing chaperone complexes to ensure correct protein folding. The Ribosome-Associated Complex (RAC) and the Nascent Polypeptide-Associated Complex (NAC) are eukaryotic chaperone complexes that interact with nascent polypeptides. The RAC is known to antagonize protein misfolding in Saccharomyces cerevisiae, and work from our lab has previously shown that the human RAC orthologs can partially rescue growth defects associated with the loss of endogenous RAC in yeast. NAC regulates nascent polypeptide processing, but the functional relationship between RAC and NAC is not understood. Thus, this study seeks to determine the roles of RAC and NAC in ER stress tolerance in S. cerevisiae. We constructed strains of S. cerevisiae to express varying combinations of yeast and human RAC and NAC orthologs, subjected them to ER stress, and measured cell fitness. Preliminary results show that under stress, fitness is greatest in cells expressing yeast RAC in the absence of NAC, while expression of yeast or human NAC in the absence of RAC significantly reduced fitness. Our data therefore suggests that the absence of NAC promotes ER stress tolerance.

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