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Author ORCID Identifier

https://orcid.org/0000-0003-4187-1518

AccessType

Open Access Dissertation

Document Type

dissertation

Degree Name

Doctor of Philosophy (PhD)

Degree Program

Molecular and Cellular Biology

Year Degree Awarded

2022

Month Degree Awarded

September

First Advisor

Peter Chien

Subject Categories

Bacteriology | Biochemistry, Biophysics, and Structural Biology | Cell Biology

Abstract

ATPases associated with diverse cellular activities (AAA+) proteases in bacteria help maintain protein homeostasis by degrading misfolded and regulatory proteins. While a handful of protein targets for these proteases have been identified in Caulobacter crescentus and other organisms, more research is needed to elucidate mechanisms that govern substrate specificity. In the second chapter of this thesis, I will elaborate on how AAA+ substrate specificity is less rigid than previous work has suggested and how limiting ATP or mutations can alter substrate preferences of the ClpXP protease. In the third chapter, I will highlight our efforts to use a quantitative proteomics approach and how this approach has provided us with insights on new phenotypes. The fourth chapter of this thesis is a compilation of our efforts to identify suppressors of Dlon defects. Lastly, the remainder of this thesis will present additional data that was generated in the pursuit of these three projects and other endeavors.

DOI

https://doi.org/10.7275/29942935

Creative Commons License

Creative Commons Attribution 4.0 License
This work is licensed under a Creative Commons Attribution 4.0 License.

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