Type of Thesis
Molecular, Cellular, & Developmental Biology
Dr. Soyeon Park
Dr. Sabrina Spencer
Dr. Christy Fillman
Dr. Nancy Guild
The 26S proteasome is a molecular machine for regulated protein degradation in eukaryotes. In order to build a functional proteasome, proper assembly between the 19-subunit regulatory particle (RP) and 28-subunit core particle (CP) is very crucial. RP assembly relies on four evolutionarily conserved chaperones: Nas6, Rpn14, Hsm3, and Nas2 (1-4). These chaperones bind to RP and prevent their premature interaction with CP. However, it is unknown what controls the switch between chaperone-RP state and CP-RP (proteasome holoenzyme) state. In this project, I focus on the Nas6 chaperone to understand how Nas6 and CP compete for RP to achieve successful assembly of the proteasome in Saccharomyces cerevisiae. I also examine potential factors that can further shift the competition between Nas6 and CP to probe how cells coordinate proteasome assembly with metabolic states in cell.
Li, Frances, "Rpt6 Tail influences the Competition between Nas6 and Core Particle in Proteasome Assembly" (2015). Undergraduate Honors Theses. 822.