NR APQK
AU Bradley,M.E.; Liebman,S.W.
TI Destabilizing interactions among [PSI(+)] and [PIN(+)] yeast prion variants
QU Genetics 2003 Dec; 165(4): 1675-85
PT journal article
AB The yeast Sup35 and Rnq1 proteins can exist in either the noninfectious soluble forms, [psi-] or [pin-], respectively, or the multiple infectious amyloid-like forms called [PSI+] or [PIN+] prion variants (or prion strains). It was previously shown that [PSI+] and [PIN+] prions enhance one another's de novo appearance. Here we show that specific prion variants of [PSI+] and [PIN+] disrupt each other's stable inheritance. Acquiring [PSI+] often impedes the inheritance of particular [PIN+] variants. Conversely, the presence of some [PIN+] variants impairs the inheritance of weak [PSI+] but not strong [PSI+] variants. These same [PIN+] variants generate a single-dot fluorescence pattern when a fusion of Rnq1 and green fluorescent protein is expressed. Another [PIN+] variant, which forms a distinctly different multiple-dot fluorescence pattern, does not impair [PSI+] inheritance. Thus, destabilization of prions by heterologous prions depends upon the variants involved. These findings may have implications for understanding interactions among other amyloid-forming proteins, including those associated with certain human diseases.
MH Comparative Study; Gene Expression Regulation, Fungal; Heat-Shock Proteins; Luminescent Proteins/metabolism; Phenotype; Prions/genetics/*metabolism; Saccharomyces cerevisiae/cytology/genetics/*metabolism; Saccharomyces cerevisiae Proteins/genetics/*metabolism; Support, U.S. Gov't, P.H.S.; Variation (Genetics)
AD Department of Biological Sciences, Laboratory for Molecular Biology, University of Illinois, Chicago, Illinois 60607, USA
SP englisch
PO USA