A yeast toxic mutant of HET-s amyloid disrupts membrane integrity

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Amyloid aggregates of the HET-s prion protein are infectious.

The [Het-s] infectious element of the filamentous fungus Podospora anserina is a prion. We have recently reported that recombinant HET-s protein aggregates in vitro into amyloid fibers. In vivo, the protein aggregates specifically in the [Het-s] prion strains. Here, we show that biolistic introduction of aggregated recombinant HET-s protein into fungal cells induces emergence of the [Het-s] pri...

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The [Het-s] Prion, an Amyloid Fold as a Cell Death Activation Trigger

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The HET-s protein from the filamentous fungus Podospora anserina is a prion involved in a cell death reaction termed heterokaryon incompatibility. This reaction is observed at the point of contact between two genetically distinct strains when one harbors a HET-s prion (in the form of amyloid aggregates) and the other expresses a soluble HET-S protein (96% identical to HET-s). How the HET-s prio...

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HET-s is a prion protein of the fungus Podospora anserina which, in the prion state, is active in a self/nonself recognition process called heterokaryon incompatibility. Its prionogenic properties reside in the C-terminal "prion domain." The HET-s prion domain polymerizes in vitro into amyloid fibrils whose properties depend on the pH of assembly; above pH 3, infectious singlet fibrils are prod...

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ژورنال

عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Biomembranes

سال: 2012

ISSN: 0005-2736

DOI: 10.1016/j.bbamem.2012.04.013