Protein Folding Activity of the Ribosome is involved in Yeast Prion Propagation
| Type | Article | ||||||||||||
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| Date | 2016-09 | ||||||||||||
| Language | English | ||||||||||||
| Author(s) | Blondel Marc1, 2, 3, Soubigou Flavie1, 2, 3, Evrard Justine1, 2, 3, Phu Hai Nguyen 1, 2, 3, 8, Hasin Naushaba4, 9, Chedin Stephane5, Gillet Reynald6, Contesse Marie-Astrid1, 2, 3, Friocourt Gaelle1, 2, 3, Stahl Guillaume7, Jones Gary W.4, 10, Voisset Cecile1, 2, 3 | ||||||||||||
| Affiliation(s) | 1 : Univ Bretagne Occidentale, INSERM, UMR 1078, Fac Med & Sci Sante, Brest, France. 2 : Etab Francais Sang EFS Bretagne, Brest, France. 3 : CHRU Brest, Hop Morvan, Lab Genet Mol, Brest, France. 4 : Maynooth Univ, Dept Biol, Yeast Genet Lab, Maynooth, Kildare, Ireland. 5 : Univ Paris 11, CEA Saclay, CNRS,SBIGeM, Inst Integrat Biol Cell I2BC,UMR 9198,CEA, Gif Sur Yvette, France. 6 : Univ Rennes 1, CNRS, UMR IGDR 6290, Translat & Folding Team, Rennes, France. 7 : Univ Toulouse, CNRS, Lab Biol Mol Eucaryotes, Toulouse, France. 8 : NIAID, Host Parasite Interact Sect, Intracellular Parasites Lab, NIH,Rocky Mt Labs, Hamilton, NJ USA. 9 : NICHHD, Sect Format RNA, NIH, Bethesda, MD 20814 USA. 10 : Leeds Beckett Univ, Fac Hlth & Social Sci, Sch Clin & Appl Sci, Leeds LS1 3HE, W Yorkshire, England. |
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| Source | Scientific Reports (2045-2322) (Nature Publishing Group), 2016-09 , Vol. 6 , N. 32117 , P. 1-14 | ||||||||||||
| DOI | 10.1038/srep32117 | ||||||||||||
| WOS© Times Cited | 15 | ||||||||||||
| 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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