Undergraduate Honors Theses

Thesis Defended

Spring 2015

Document Type

Thesis

Type of Thesis

Departmental Honors

Department

Molecular, Cellular, & Developmental Biology

First Advisor

Dr. Soyeon Park

Second Advisor

Dr. Sabrina Spencer

Third Advisor

Dr. Christy Fillman

Fourth Advisor

Dr. Nancy Guild

Abstract

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.

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