FN Archimer Export Format
PT J
TI Protein Folding Activity of the Ribosome is involved in Yeast Prion Propagation
BT 
AF BLONDEL, Marc
   SOUBIGOU, Flavie
   EVRARD, Justine
   HASIN, Naushaba
   CHEDIN, Stephane
   GILLET, Reynald
   CONTESSE, Marie-Astrid
   FRIOCOURT, Gaelle
   STAHL, Guillaume
   JONES, Gary W.
   VOISSET, Cecile
AS 1:1,2,3;2:1,2,3;3:1,2,3;4:1,2,3,8;5:4,9;6:5;7:6;8:1,2,3;9:1,2,3;10:7;11:4,10;12:1,2,3;
FF 1:;2:;3:;4:;5:;6:;7:;8:;9:;10:;11:;12:;
C1 Univ Bretagne Occidentale, INSERM, UMR 1078, Fac Med & Sci Sante, Brest, France.
   Etab Francais Sang EFS Bretagne, Brest, France.
   CHRU Brest, Hop Morvan, Lab Genet Mol, Brest, France.
   Maynooth Univ, Dept Biol, Yeast Genet Lab, Maynooth, Kildare, Ireland.
   Univ Paris 11, CEA Saclay, CNRS,SBIGeM, Inst Integrat Biol Cell I2BC,UMR 9198,CEA, Gif Sur Yvette, France.
   Univ Rennes 1, CNRS, UMR IGDR 6290, Translat & Folding Team, Rennes, France.
   Univ Toulouse, CNRS, Lab Biol Mol Eucaryotes, Toulouse, France.
   NIAID, Host Parasite Interact Sect, Intracellular Parasites Lab, NIH,Rocky Mt Labs, Hamilton, NJ USA.
   NICHHD, Sect Format RNA, NIH, Bethesda, MD 20814 USA.
   Leeds Beckett Univ, Fac Hlth & Social Sci, Sch Clin & Appl Sci, Leeds LS1 3HE, W Yorkshire, England.
C2 UBO, FRANCE
   EFS, FRANCE
   CHRU BREST, FRANCE
   UNIV MAYNOOTH, IRELAND
   UNIV PARIS 11, FRANCE
   UNIV RENNES, FRANCE
   UNIV TOULOUSE, FRANCE
   NIAID, USA
   NICHHD, USA
   UNIV LEEDS, UK
IN DOAJ
IF 4.259
TC 15
UR https://archimer.ifremer.fr/doc/00358/46931/46834.pdf
   https://archimer.ifremer.fr/doc/00358/46931/46835.pdf
LA English
DT Article
AB 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.
PY 2016
PD SEP
SO Scientific Reports
SN 2045-2322
PU Nature Publishing Group
VL 6
IS 32117
UT 000383327500001
BP 1
EP 14
DI 10.1038/srep32117
ID 46931
ER

EF