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Protein aggregates, which can result in cellular toxicity, are found in the brains of people afflicted with neurodegenerative diseases. One of the proteins found to aggregate is Tau, a protein that stabilizes microtubules in neuronal cells. Based on its amino acid sequence, Tau is likely to be N-terminally acetylated by the complex NatA, which is responsible for the acetylation of a majority of proteins with this post-translational modification. Mutations in the NatA complex result in a variety of pleiotropic detrimental phenotypes, showing that acetylation is a crucial modification for many proteins. Without the presence of NatA – and therefore without acetylation – Tau may be more prone to aggregation and toxicity. By expressing Tau in yeast strains with and without the presence of NatA, the possible effects of acetylation or lack thereof can be determined by examining protein expression and aggregation within the cells by SDS-PAGE and SDD-AGE. Initial results indicate that Tau aggregates within these yeast cells although the nature and effect of the aggregates is still being determined. This project has allowed for the creation of a system by which Tau aggregates can be examined in vivo.

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