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• W2139069968 endingPage "528" @default.
• W2139069968 startingPage "507" @default.
• W2139069968 abstract "Summary Yeast prions are superb models for understanding the mechanisms of self‐perpetuating protein aggregates formation. [ PSI + ] stands among the most documented yeast prions and results from self‐assembly of the translation termination factor S up35p into protein fibrils. A plethora of cellular factors were shown to affect [ PSI + ] formation and propagation. Clearance of S up35p prion particles is however poorly understood and documented. Here, we investigated the role of the proteasome in the degradation of S up35p and in [ PSI + ] prion propagation. We found that cells lacking the RPN4 gene, which have reduced intracellular proteasome pools, accumulated S up35p and have defects in [ PSI + ] formation and propagation. S up35p is degraded in vitro by the 26 S and 20 S proteasomes in a ubiquitin‐independent manner, generating an array of amyloidogenic peptides derived from its prion‐domain. We also demonstrate the formation of a proteasome‐resistant fragment spanning residues 83–685 which is devoid of the prion‐domain that is essential for [ PSI + ] propagation. Most important was the finding that the 26 S and 20 S proteasomes degrade S up35p fibrils in vitro and abolish their infectivity. Our results point to an overlooked role of the proteasome in clearing toxic protein aggregates, and have important implications for a better understanding of the life cycle of infectious protein assemblies." @default.
• W2139069968 created "2016-06-24" @default.
• W2139069968 creator A5084373973 @default.
• W2139069968 creator A5085926900 @default.
• W2139069968 creator A5088401311 @default.
• W2139069968 date "2014-03-17" @default.
• W2139069968 modified "2023-10-03" @default.
• W2139069968 title "A role for the proteasome in the turnover of Sup35p and in [<i>PSI</i>⁺] prion propagation" @default.
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