NR AJHR
AU Paushkin,S.V.; Kushnirov,V.V.; Smirnov,V.N.; Ter-Avanesyan,M.D.
TI In vitro propagation of the prion-like state of yeast Sup35 protein
QU Science 1997 Jul 18; 277(5324): 381-3
KI Science. 1997 Jul 18;277(5324):314. PMID: 9518359
PT journal article
AB The yeast cytoplasmically inherited genetic determinant [PSI+] is presumed to be a manifestation of the prion-like properties of the Sup35 protein (Sup35p). Here, cell-free conversion of Sup35p from [psi-] cells (Sup35ppsi-) to the prion-like [PSI+]-specific form (Sup35pPSI+) was observed. The conversion reaction could be repeated for several consecutive cycles, thus modeling in vitro continuous [PSI+] propagation. Size fractionation of lysates of [PSI+] cells demonstrated that the converting activity was associated solely with Sup35pPSI+ aggregates, which agrees with the nucleation model for [PSI+] propagation. Sup35pPSI+ was purified and showed high conversion activity, thus confirming the prion hypothesis for Sup35p.
IN Die Autoren konnten die psi(-)-Form des Hefeproteins Sup35 in vitro in die polymere psi(+)-Form umwandeln.
ZR 22
MH Endopeptidases/metabolism; Fungal Proteins/*chemistry/genetics/isolation & purification; Models, Chemical; Phenotype; PrPc Proteins/chemistry; PrPsc Proteins/chemistry; Prions/*chemistry; *Protein Conformation; Protein Folding; Saccharomyces cerevisiae/*chemistry/genetics; Solubility; Support, Non-U.S. Gov't; Transformation, Genetic; Translation, Genetic
AD Institute of Experimental Cardiology, Cardiology Research Center, 3rd Cherepkovskaya Street 15A, Moscow 121552, Russia.
SP englisch
PO USA