Proteomic characterization of the effect of proteasome activity on stationary phase model of aging in S. cerevisiae yeast.

Protein turnover regulation is essential for maintaining cellular homeostasis. The accumulation of unneeded or abnormal proteins is harmful and may affect multiple cellular functions. Studies found a positive correlation between age and the decreasing rates of proteins’ turnover in eukaryotic cells.

In this research, we investigated if and how we can alter the activity of the main intracellular proteolytic systems; the ubiquitin-proteasome system, and what are the implications of these alternations on baker yeast stationary phase model of aging.

Using Mass-Spectrometry based proteomic, we characterized changes in protein’s abundance resulted from proteasome inhibition with MG132 and activation with Dipyridamole, under lag, logarithmic, and stationary growth phases.

The analysis revealed 511 proteins that had a differential abundance between the different treatment groups.

These findings can contribute to the understanding of the aging phenotype and the pathogenesis of aging-related diseases.