Hsp110 Chaperones and Their Role in Prion Formation in Yeast
Author Information
Author(s): Sadlish Heather, Rampelt Heike, Shorter James, Wegrzyn Renee D., Andréasson Claes, Lindquist Susan, Bukau Bernd
Primary Institution: Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)
Hypothesis
What is the role of the Hsp110 protein Sse1 in the formation and propagation of the [PSI+] prion in Saccharomyces cerevisiae?
Conclusion
Sse1 is essential for efficient prion propagation and has both NEF-dependent and NEF-independent activities that influence prion formation.
Supporting Evidence
- Sse1 is required for efficient de novo [PSI+] formation and stable propagation of the [PSI+] phenotype.
- Overexpression of Sse1 can counteract the curing of [PSI+] by Hsp104.
- Sse1 stimulates in vitro nucleation of the Sup35 prion domain.
- Cells lacking Sse1 exhibit a weakened prion phenotype.
- Sse1's NEF activity is critical for prion propagation.
- Sse1 can induce [PSI+] formation even in the absence of [PIN+].
- Sse1 inhibits Hsp104-mediated curing of [PSI+].
- Sse1 promotes the assembly of Sup35NM fibers in vitro.
Takeaway
Sse1 helps yeast proteins fold correctly and keeps prions, which are misfolded proteins, from breaking down too quickly.
Methodology
The study involved assays for [PSI+] formation and curing, protein aggregation analyses, and various genetic manipulations in yeast strains.
Limitations
The study primarily focuses on the role of Sse1 and may not account for all factors influencing prion dynamics.
Digital Object Identifier (DOI)
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