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search.filters.applied.f.advisor: Chernoff, Yury O. × Author: Tennant, Esther Paula × End date: 2019 × Start date: 2000 × search.filters.applied.f.isOrgUnitOfPublicationTitle: College of Sciences × search.filters.applied.f.isOrgUnitOfPublicationTitle: School of Biological Sciences × search.filters.applied.f.resourcesubtype: Thesis ×

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Interactions of the chaperones and components of UB system in the formation and propagation of the yeast prion [PSI+]

2005-06-28 , Tennant, Esther Paula

Three of the best-characterized prions of Saccharomyces cerevisiae are [PSI+], [URE3], and [PIN+]. This study focuses on the prions [PSI+] and [PIN+]. [PSI+] is the prion isoforms of the protein Sup35 that functions as a eRF3 translational termination factor. The presence of [PSI+] is detected by the partial loss of function of Sup35. The prion [PIN+] is the isoform of the protein Rnq1, and this proteins function is unknown. The presence of the prion [PIN+] is necessary for the de novo formation of the prion [PSI+] (Derkatch et al., 1997). The chaperone, Hsp104, belongs to an evolutionary conserved Hsp100 family of proteins that participate in a various number of cellular processes (Schirmer et al., 1996). Hsp104, in particular, is responsible for the cells adaptation to heat shock, it controls spore viability and the long-term viability of starving vegetative cells. (Sanchez and Linquist, 1990; Sanchez et al.,1992) It is an ATPase that has been shown to promote solubilization of aggregated protein (Parsel et al., 1991). A unique relationship exists between Hsp104 levels within the cell and the maintenance of the prion [PSI+]. The over production of Hsp104 eliminates [PSI+] (Chernoff 1995). This seems logical considering Hsp104 is a disaggregase, and it is reasonable to assume that the over production provides sufficient resources to break the aggregates into portions that are accessible to either other chaperones which would facilitate the proper folding or perhaps the system responsible for the elimination of unusable proteins, such as the ubiquitin-proteasome system. This study examines the role of the ubiquitin-proteasome system in curing of [PSI+] by Hsp104. The role of alternate pathways, in which the prion isoform is refolded into it correct, functional conformation by the action of the chaperones Ssb1 and Ssb2 is examined. These results suggest that the combination of both the degradation pathway and the refolding of proteins are involved in curing of [PSI+] by Hsp104 over production.

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