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Proteins are one of the four main macromolecules essential to life. They are responsible for a diverse array of processes, including cellular signaling, cell structure, and catalytic activity. These functions are directly related to a protein’s structure. Consequently, the misfolding of a protein, which can be due to a variety of factors, can lead to an alteration in the function of that protein. Misfolded proteins can also associate together to form aggregates, which can become toxic to cells. In prions and prion-like proteins, the misfolding of one protein can propagate to another protein, increasing aggregation, which can lead to cellular death and result in neurodegenerative diseases in mammals. One factor that is linked to increased misfolding is stalling of the ribosome, the cellular machinery responsible for the construction of proteins, during synthesis. In the model organism S. cerevisiae, stalling is a natural process that may allow for misfolding to occur in a way that benefits yeast in times of stress. By using antibiotics to halt the production of two proteins with known misfolded structures, the mechanism and rate at which these proteins convert to their alternate fold can be investigated.
Kane, Hayley, "Cycloheximide and Hygromycin B-Induced Ribosome Stalling Leads to Decreased Prion Formation Rate for polyQ, but not Sup35, in Saccharomyces cerevisiae" (2023). Biology Summer Fellows. 102.
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