Can Saccharomyces cerevisiae Lacking Their Own Ribosome-associated Complex Chaperones Use the Human Orthologs to Suppress Prion Formation and the Toxicity of Disease-associated Proteins?

Proteins are complex macromolecules that carry out a variety of different functions like structural composition and regulation of cellular processes that are essential to all forms of life. In order to carry out their specific functions, proteins must fold properly during their synthesis. Prions are a class of misfolded proteins that are infectious due to their ability to self-propagate forming protein aggregates. These aggregates are associated with infectious diseases like Mad-Cow Disease and Creutzfeldt-Jakob disease. Fortunately, our cells have a natural defense mechanism, called chaperones, that can suppress the formation of these prions. Chaperones are types of proteins that facilitate the proper folding of other proteins to ensure the correct conformation of each protein is achieved. There are several different families of chaperones, but in previous research studies performed in the Cameron Lab using Saccharomyces cerevisiae as a model organism, the Ribosome- Associated Complex (RAC) has been linked to the suppression of prion formation in cells. Researchers have identified human homologs of the RAC components that are very similar in structure and function to those in yeast. The purpose of this study is to determine if yeast cells lacking their own RAC components can functionally use the human homologs to rescue their growth and suppress prion formation and toxicity of a disease-associated protein