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The molecular chaperone Hsp104 is a crucial factor in the acquisition of thermotolerance in yeast. Under stress conditions, the disaggregase activity of Hsp104 facilitates the reactivation of misfolded proteins. Hsp104 is also involved in the propagation of fungal prions. For instance, the well-characterized [ PSI +  ] prion of  Saccharomyces cerevisiae  does not propagate in  Δhsp104  cells or in cells overexpressing Hsp104. In this study, we characterized the functional homolog of Hsp104 from  Schizosaccharomyces pombe  (Sp_Hsp104). As its  S. cerevisiae  counterpart,  Sp_hsp104 +   is heat-inducible and required for thermotolerance in  S. pombe . Sp_Hsp104 displays low disaggregase activity and cannot propagate the [ PSI +  ] prion in  S. cerevisiae . When overexpressed in  S. cerevisiae , Sp_Hsp104 confers thermotolerance to  Δhsp104  cells and reactivates heat-aggregated proteins. However, overexpression of Sp_Hsp104 does not propagate nor eliminate [ PSI +  ]. Strikingly, [ PSI +  ] was cured by overexpression of a chimeric chaperone bearing the C-terminal domain (CTD) of the  S. cerevisiae  Hsp104 protein. Our study demonstrates that the ability to untangle aggregated proteins is conserved between the  S. pombe  and  S. cerevisiae  Hsp104 homologs, and points to a role of the CTD in the propagation of the  S. cerevisiae  [ PSI +  ] prion.

The Schizosaccharomyces pombe Hsp104 Disaggregase Is Unable to Propagate the [PSI+] Prion