Proteome profiling of exponentially growing and heat-shock treated UBC4 and UBC5 deletion strains of S. cerevisiae

ABSTRACT: The Ubiquitin Proteasome System (UPS) governs numerous cellular processes by modulating protein stability and activity via the conjugation of the small molecule ubiquitin, either as a single chain or as linkages with distinct functions. Dysregulation of the UPS has been associated with many diseases, including neurodegenerative and neurodevelopmental diseases, as well as cancer. Ubiquitin conjugating enzymes (E2s) are important players of the UPS which work together with ubiquitin ligases (E3s) to promote substrate ubiquitylation. In this study, we conduct a comparative proteome-wide abundance profiling of S. cerevisiae cells during exponential growth phase with and without heat shock treatment. We focus on cells with deletions of the two highly homologous E2s, UBC4 or UBC5, and use isobaric tag-based quantitative mass spectrometry to elucidate variations and similarities in their proteome profiles. Our analysis revealed that Ubc4 has a much stronger effect on the proteome compared to Ubc5, particularly in exponentially growing cells. In contrast, the effect of Ubc5 on the proteome only becomes evident after heat shock, and even then, it remains minor compared to Ubc4. Furthermore, we identified proteins increasing in absence of each enzyme, which may represent their candidate substrates, potentially contributing to a better understanding of their cellular role.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Joao Paulo  

LAB HEAD: Joao A. Paulo

PROVIDER: PXD056103 | Pride | 2024-10-18

REPOSITORIES: Pride