NR ARFI
AU Bagriantsev,S.N.; Liebman,S.W.
TI Specificity of prion assembly in vivo. [PSI+] and [PIN+] form separate structures in yeast.
QU The Journal of Biological Chemistry 2004 Dec 3; 279(49): 51042-8
IA http://www.jbc.org/cgi/content/full/279/49/51042
PT journal article
AB The yeast prions [PSI+] and [PIN+] are self-propagating amyloid aggregates of the Gln/Asn-rich proteins Sup35p and Rnq1p, respectively. Like the mammalian PrP prion "strains," [PSI+] and [PIN+] exist in different conformations called variants. Here, [PSI+] and [PIN+] variants were used to model in vivo interactions between co-existing heterologous amyloid aggregates. Two levels of structural organization, like those previously described for [PSI+], were demonstrated for [PIN+]. In cells with both [PSI+] and [PIN+] the two prions formed separate structures at both levels. Also, the destabilization of [PSI+] by certain [PIN+] variants was shown not to involve alterations in the [PSI+] prion size. Finally, when two variants of the same prion that have aggregates with distinct biochemical characteristics were combined in a single cell, only one aggregate type was propagated. These studies demonstrate the intracellular organization of yeast prions and provide insight into the principles of in vivo amyloid assembly.
MH Amyloid/chemistry; Detergents/pharmacology; Electrophoresis, Polyacrylamide Gel; Genes, Recessive; Guanidine/chemistry; Prions/*chemistry; Protein Conformation; Research Support, U.S. Gov't, P.H.S.; Saccharomyces cerevisiae Proteins/chemistry; Sodium Dodecyl Sulfate/chemistry; Temperature
AD Laboratory for Molecular Biology, University of Illinois, Chicago, Illinois 60607, USA
SP englisch
PO USA