NR ADXY
AU Fernandez-Bellot,E.; Guillemet,E.; Ness,F.; Baudin-Baillieu,A.; Ripaud,L.; Tuite,M.; Cullin,C.
TI The [URE3] phenotype: evidence for a soluble prion in yeast.
QU EMBO Reports 2002 Jan; 3(1): 76-81
IA http://www.nature.com/embor/journal/v3/n1/pdf/embor248.pdf
PT journal article
AB The aggregation of the two yeast proteins Sup35p and Ure2p is widely accepted as a model for explaining the prion propagation of the phenotypes [PSI+] and [URE3], respectively. Here, we demonstrate that the propagation of [URE3] cannot simply be the consequence of generating large aggregates of Ure2p, because such aggregation can be found in some conditions that are not related to the prion state of Ure2p. A comparison of [PSI+] and [URE3] aggregation demonstrates differences between these two prion mechanisms. Our findings lead us to propose a new unifying model for yeast prion propagation.
MH Amino Acid Sequence; Molecular Sequence Data; Phenotype; Prions/*chemistry/genetics; Protein Isoforms/chemistry/genetics; Protein Structure, Tertiary; Recombinant Fusion Proteins/chemistry/genetics; Saccharomyces cerevisiae/*chemistry/genetics; Saccharomyces cerevisiae Proteins/*chemistry/genetics; Solubility; Support, Non-U.S. Gov't
AD Centre de Genetique Moleculaire, 91190 Gif-sur-Yvette, France.
SP englisch
PO England