Journal
MOLECULAR CELL
Volume 7, Issue 6, Pages 1121-1130Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(01)00259-3
Keywords
-
Categories
Ask authors/readers for more resources
The yeast [PSI+] element represents an aggregated form of release factor Sup35p and is inherited by a prion mechanism. A species barrier prevents crosstransmission of the [PSI+] state between heterotypic Sup35p prions. Kluyveromyces lactis and Yarrowia lipolytica Sup35 proteins, however, show interspecies [PSI+] transmissibility and susceptibility and a high spontaneous propagation rate. Cross-seeding was visualized by coaggregation of differential fluorescence probes fused to heterotypic Sup35 proteins. This coaggregation state, referred to as a quasiprion state, can be stably maintained as a heritable [PSI+] element composed of heterologous Sup35 proteins. K. lactis Sup35p was capable of forming [PSI+] elements not only in S. cerevisiae but in K. lactis. These two Sup35 proteins contain unique multiple imperfect oligopeptide repeats responsible for crosstransmission and high spontaneous propagation of novel [PSI+] elements.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available