ArticleProceedings of the National Academy of Sciences of the United States of America2005
Curing of yeast [PSI+] prion by guanidine inactivation of Hsp104 does not require cell division.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 26 citations in OpenAlex.
- Hsp70 Binding to the N-terminal Domain of Hsp104 Regulates [Molecular and cellular biology · 2023Article
- Recent Insights on Alzheimer's Disease Originating from Yeast Models.International journal of molecular sciences · 2018Review
- Study of Amyloids Using Yeast.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Patterns of [PSI (+) ] aggregation allow insights into cellular organization of yeast prion aggregates.Prion · 2012Review
- Insight into molecular basis of curing of [PSI+] prion by overexpression of 104-kDa heat shock protein (Hsp104).The Journal of biological chemistry · 2012Article
- Study of amyloids using yeast.Methods in molecular biology (Clifton, N.J.) · 2012Article
- Article
- Pathogenic polyglutamine tracts are potent inducers of spontaneous Sup35 and Rnq1 amyloidogenesis.PloS one · 2010Article
- Application of GFP-labeling to study prions in yeast.Protein and peptide letters · 2009Review
- Cell division is essential for elimination of the yeast [PSI+] prion by guanidine hydrochloride.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- Hsp104-dependent remodeling of prion complexes mediates protein-only inheritance.PLoS biology · 2007Article
- Application of photobleaching for measuring diffusion of prion proteins in cytosol of yeast cells.Methods (San Diego, Calif.) · 2006Article
- Review
- Prion stability.PrionReview
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Propagation of the yeast prion [PSI+], a self-replicating aggregated form of Sup35p, requires Hsp104. One model to explain this phenomenon proposes that, in the absence of Hsp104, Sup35p aggregates enlarge but fail to replicate thus becoming diluted out as the yeast divide. To test this model, we used live imaging of Sup35p-GFP to follow the changes that occur in [PSI+] cells after the addition of guanidine to inactivate Hsp104. After guanidine addition there was initially an increase in aggregation of Sup35p-GFP; but then, before the yeast divided, the aggregates began to dissolve, and after approximately 6 h the Sup35-GFP looked identical to the Sup35-GFP in [psi+] cells. Although plating studies showed that the yeast were still [PSI+], this reduction in aggregation suggested that curing of [PSI+] by inactivation of Hsp104 might be independent of cell division. This was tested by measuring the rate of curing of [PSI+] cells in both dividing and nondividing cells. Cell division was inhibited by adding either alpha factor or farnesol. Remarkably, with both of these methods, we found that the rate of curing was not significantly affected by cell division. Thus, cell division is not a determining factor for curing [PSI+] by inactivating Hsp104 with guanidine. Rather, curing apparently occurs because Sup35-GFP polymers slowly depolymerize in the absence of Hsp104 activity. Hsp104 then counteracts this curing possibly by catalyzing formation of new polymers.
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