The intent of this thesis is to determine whether the deubiquitinating enzyme ubiquitin specific protease 30 (USP30) is cleaved by Omi/HtrA2 (hereafter referred to as Omi) protease during mitochondrial stress. USP30 is a mitochondrial protein that is anchored in the outer mitochondrial membrane and has components in the intermembrane space (IMS) as well as in the cytoplasm. USP30's IMS component has a six-amino-acid sequence that is very similar to Omi's consensus cleavage sites. Under normal conditions, Omi resides exclusively within the IMS; therefore, if Omi were to cleave USP30, it would target the part of the protein located in the IMS component. Omi is known to play a crucial role in a variety of diseases including cancers, neurodegenerative, and metabolic disorders. Since Omi is a serine protease, it is assumed to carry its normal function through the direct cleavage and degradation of specific substrates. If USP30 deubiquitinase is a bona fide substrate of Omi, this will provide new and important information on the mechanism by which Omi regulates the polyubiquitination process during mitochondrial stress.
| Identifer | oai:union.ndltd.org:ucf.edu/oai:stars.library.ucf.edu:honorstheses-1527 |
| Date | 01 January 2019 |
| Creators | Jin, Sunmi |
| Publisher | STARS |
| Source Sets | University of Central Florida |
| Language | English |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Honors Undergraduate Theses |
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