Role of Hsp104 in the Propagation and Inheritance of the [Het-s] Prion
Podospora anserina
Fungal prion
CLPB
DOI:
10.1091/mbc.e07-07-0657
Publication Date:
2007-09-20T01:19:02Z
AUTHORS (5)
ABSTRACT
The chaperones of the ClpB/HSP100 family play a central role in thermotolerance bacteria, plants, and fungi by ensuring solubilization heat-induced protein aggregates. In addition yeast, Hsp104 was found to be required for prion propagation. Herein, we analyze Podospora anserina (PaHsp104) formation propagation [Het-s] prion. We show that DeltaPaHsp104 strains propagate [Het-s], making first native fungal propagated absence Hsp104. Nevertheless, [Het-s]-propagon numbers, rate, spontaneous emergence are reduced background. addition, inactivation PaHsp104 leads severe meiotic instability abolishes its drive activity. Finally, DeltaPaHSP104 less susceptible than wild type infection exogenous recombinant HET-s(218-289) amyloids. Like [URE3] [PIN(+)] yeast but unlike [PSI(+)], is not cured constitutive overexpression. observed effects consistent with described aggregate shearing yeast. However, Hsp104-dependency appears stringent P. yeast; presumably because occurs syncitium.
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