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• W2077904734 endingPage "e87521" @default.
• W2077904734 startingPage "e87521" @default.
• W2077904734 abstract "Molecular chaperones play a significant role in preventing protein misfolding and aggregation. Indeed, some protein conformational disorders have been linked to changes in the chaperone network. Curiously, in yeast, chaperones also play a role in promoting prion maintenance and propagation. While many amyloidogenic proteins are associated with disease in mammals, yeast prion proteins, and their ability to undergo conformational conversion into a prion state, are proposed to play a functional role in yeast biology. The chaperone Hsp104, a AAA+ ATPase, is essential for yeast prion propagation. Hsp104 fragments large prion aggregates to generate a population of smaller oligomers that can more readily convert soluble monomer and be transmitted to daughter cells. Here, we show that the middle (M) domain of Hsp104, and its mobility, plays an integral part in prion propagation. We generated and characterized mutations in the M-domain of Hsp104 that are predicted to stabilize either a repressed or de-repressed conformation of the M-domain (by analogy to ClpB in bacteria). We show that the predicted stabilization of the repressed conformation inhibits general chaperone activity. Mutation to the de-repressed conformation, however, has differential effects on ATP hydrolysis and disaggregation, suggesting that the M-domain is involved in coupling these two activities. Interestingly, we show that changes in the M-domain differentially affect the propagation of different variants of the [PSI+] and [RNQ+] prions, which indicates that some prion variants are more sensitive to changes in the M-domain mobility than others. Thus, we provide evidence that regulation of the M-domain of Hsp104 is critical for efficient prion propagation. This shows the importance of elucidating the function of the M-domain in order to understand the role of Hsp104 in the propagation of different prions and prion variants." @default.
• W2077904734 created "2016-06-24" @default.
• W2077904734 creator A5048110608 @default.
• W2077904734 creator A5078388064 @default.
• W2077904734 creator A5081342912 @default.
• W2077904734 date "2014-01-23" @default.
• W2077904734 modified "2023-09-27" @default.
• W2077904734 title "Regulation of the Hsp104 Middle Domain Activity Is Critical for Yeast Prion Propagation" @default.
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• W2077904734 doi "https://doi.org/10.1371/journal.pone.0087521" @default.
• W2077904734 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3900729" @default.
• W2077904734 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/24466354" @default.
• W2077904734 hasPublicationYear "2014" @default.
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