NR AJGH
AU Patino,M.M.; Liu,J.J.; Glover,J.R.; Lindquist,S.L.
TI Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
QU Science 1996 Aug 2; 273(5275): 622-6
KI Science. 1996 Aug 2;273(5275):580. PMID: 8701310
PT journal article
AB A cytoplasmically inherited genetic element in yeast, [PSI+], was confirmed to be a prionlike aggregate of the cellular protein Sup35 by differential centrifugation analysis and microscopic localization of a Sup35-green fluorescent protein fusion. Aggregation depended on the intracellular concentration and functional state of the chaperone protein Hsp104 in the same manner as did [PSI+] inheritance. The amino-terminal and carboxy-terminal domains of Sup35 contributed to the unusual behavior of [PSI+]. [PSI+] altered the conformational state of newly synthesized prion proteins, inducing them to aggregate as well, thus fulfilling a major tenet of the prion hypothesis.
ZR 26
MH Amino Acid Sequence; Base Sequence; Fungal Proteins/analysis/*chemistry/genetics/physiology; Heat-Shock Proteins/physiology; Luminescent Proteins/analysis; Molecular Sequence Data; Phenotype; Prions/*chemistry/genetics; *Protein Conformation; Recombinant Fusion Proteins/analysis/chemistry; Saccharomyces cerevisiae/*chemistry/*genetics; Solubility; Support, Non-U.S. Gov't; Support, U.S. Gov't, P.H.S.
AD Howard Hughes Medical Institute and the Department of Molecular Genetics and Cell Biology, University of Chicago, 5841 South Maryland Avenue, Chicago, IL 60637, USA
SP englisch
PO USA