Reference: Blondel M, et al. (2016) Protein Folding Activity of the Ribosome is involved in Yeast Prion Propagation. Sci Rep 6:32117

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Abstract


6AP and GA are potent inhibitors of yeast and mammalian prions and also specific inhibitors of PFAR, the protein-folding activity borne by domain V of the large rRNA of the large subunit of the ribosome. We therefore explored the link between PFAR and yeast prion [PSI(+)] using both PFAR-enriched mutants and site-directed methylation. We demonstrate that PFAR is involved in propagation and de novo formation of [PSI(+)]. PFAR and the yeast heat-shock protein Hsp104 partially compensate each other for [PSI(+)] propagation. Our data also provide insight into new functions for the ribosome in basal thermotolerance and heat-shocked protein refolding. PFAR is thus an evolutionarily conserved cell component implicated in the prion life cycle, and we propose that it could be a potential therapeutic target for human protein misfolding diseases.

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Journal Article
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Blondel M, Soubigou F, Evrard J, Nguyen PH, Hasin N, Chédin S, Gillet R, Contesse MA, Friocourt G, Stahl G, ... Show all
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