Conformational Shifts of the 26S Proteasome After Pore Loop Mutation
The 26S proteasome is the last stop of the main protein degradation pathway in our cells, and it allows us to keep our bodies healthy by degrading old or non-functional proteins. The motor of the proteasome is responsible for engaging, unraveling and pulling the targeted protein into the core, where it is degraded. The pore loops, six in total, are located on the motor and are the parts of the proteasome that physically interact with the targeted protein. These six pore loops pull the protein to the core like hands pulling a rope downward, switching position like hands would from top to bottom of the protein “rope” by using ATP. When a protein substrate tail is initially engaged by these pore loops, the arrangement of the entire proteasome complex shifts to begin degradation of the targeted protein. My research will explore the effect of pore loop mutations on the shift in conformational switch, from non-engaged to engaged, of the 26S proteasome using fluorescence as a marker for which state the proteasome is in.
Message to Sponsor
- Major: Molecular and Cell Biology
- Sponsor: Rose Hill Foundation
- Mentor: Erika M. Lopez Alfonzo