Hrr25 is a highly conserved serine/threonine protein kinase with diverse functions and it localizes to a number of intracellular sites. Hrr25 possesses an N-terminal kinase domain, a middle region, and a C-terminal proline/glutamine rich domain. In this thesis, we systematically characterized the roles of these three domains of Hrr25 on cell growth, cell morphology, and its cellular localizations. Additionally, we identified a novel target of Hrr25, Pin4. We show that Hrr25-dependent phosphorylation of Pin4 is required for cell wall integrity maintenance. We found that that Hrr25 and Pin4 physically interact in vivo and that the C-terminal domain of Hrr25 is required for this interaction and for maintaining cell wall integrity. Together, we identified a new target and a novel function for Hrr25 and provided insights into the structure-function relationship of Hrr25 domains.
Identifer | oai:union.ndltd.org:uno.edu/oai:scholarworks.uno.edu:td-3851 |
Date | 05 August 2019 |
Creators | Bhattarai, Amita |
Publisher | ScholarWorks@UNO |
Source Sets | University of New Orleans |
Detected Language | English |
Type | text |
Format | application/pdf |
Source | University of New Orleans Theses and Dissertations |
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