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Title: Exploring the role of the molecular chaperone Hsp104 in yeast [PSI+] prion propagation and transmission
Author: Wongwigkarn, Jintana
Awarding Body: University of Kent
Current Institution: University of Kent
Date of Award: 2013
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[PSI+] is the prion form of the Sup35 protein in Saccharomyces cerevisiae. The molecular Hsp 104 chaperone is involved in the propagation of the [PSI+] by dissolving Sup35p prion fibres into the small seeds (propagons) needed to generate a new round propagation. Overexpression of the HSP104 gene results in elimination of the [PSI+] prion, but the mechanism by which [PSI+] loss is triggered remains undetermined. To gain insight into the mechanism of such induced [PSr] elimination, the cellular factors with a known functional connection with Hsp104 and that may necessary for Hsp 104 overexpression-induced prion loss, were investigated. The Hsp90 cochaperones Cpr7p and Stilp that also bind to the C-terminus of Hspl04 are required for [PSI+] elimination by overexpression of both wild type Hsp104 and two different ATPase-defective mutants of Hspl04 but are not essential for [PSI+] prion propagation. This indicated that [PSr] elimination by elevated Hsp104 may occur as a consequence of activities of Hsp104 in addition to its remodelling activity.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID:  DOI: Not available