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Protein Folding Activity of the Ribosome is involved in Yeast Prion Propagation ArchiMer
Blondel, Marc; Soubigou, Flavie; Evrard, Justine; Phu Hai Nguyen,; Hasin, Naushaba; Chedin, Stephane; Gillet, Reynald; Contesse, Marie-astrid; Friocourt, Gaelle; Stahl, Guillaume; Jones, Gary W.; Voisset, Cecile.
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...
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Ano: 2016 URL: https://archimer.ifremer.fr/doc/00358/46931/46834.pdf
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