NR AGLW
AU King,C.Y.; Tittmann,P.; Gross,H.; Gebert,R.; Aebi,M.; Wüthrich,K.
TI Prion-inducing domain 2-114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
QU Proceedings of the National Academy of Sciences of the United States of America 1997 Jun 24; 94(13): 6618-22
PT journal article
AB The yeast non-Mendelian genetic factor [PSI], which enhances the efficiency of tRNA-mediated nonsense suppression in Saccharomyces cerevisiae, is thought to be an abnormal cellular isoform of the Sup35 protein. Genetic studies have established that the N-terminal part of the Sup35 protein is sufficient for the genesis as well as the maintenance of [PSI]. Here we demonstrate that the N-terminal polypeptide fragment consisting of residues 2-114 of Sup35p, Sup35pN, spontaneously aggregates to form thin filaments in vitro. The filaments show a beta-sheet-type circular dichroism spectrum, exhibit increased protease resistance, and show amyloid-like optical properties. It is further shown that filament growth in freshly prepared Sup35pN solutions can be induced by seeding with a dilute suspension of preformed filaments. These results suggest that the abnormal cellular isoform of Sup35p is an amyloid-like aggregate and further indicate that seeding might be responsible for the maintenance of the [PSI] element in vivo.
ZR 31 Zitate
MH Amyloid/*ultrastructure; Fungal Proteins/chemistry/drug effects/*ultrastructure; Peptide Fragments/chemistry; Prions/*pharmacology; Saccharomyces cerevisiae/*metabolism/ultrastructure; Support, Non-U.S. Gov't
AD Institut für Molekularbiologie und Biophysik, Eidgenössische Technische Hochschule, CH-8093 Zürich, Switzerland.
SP englisch
PO USA
OR Prion-Krankheiten 5