Undergraduate Honors Thesis


Rpt6 Tail influences the Competition between Nas6 and Core Particle in Proteasome Assembly Public Deposited

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  • 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.
Date Awarded
  • 2015-01-01
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Last Modified
  • 2019-12-02
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