ArticlePloS one2012
Differences in the curing of [PSI+] prion by various methods of Hsp104 inactivation.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 26 citations in OpenAlex.
- Overexpression of Hsp104 by Causing Dissolution of the Prion Seeds Cures the Yeast [International journal of molecular sciences · 2023Article
- Hsp70 Binding to the N-terminal Domain of Hsp104 Regulates [Molecular and cellular biology · 2023Article
- [PRIONPathogens (Basel, Switzerland) · 2022Article
- Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures.Viruses · 2022Review
- Differential Interactions of Molecular Chaperones and Yeast Prions.Journal of fungi (Basel, Switzerland) · 2022Review
- Mechanisms for Curing Yeast Prions.International journal of molecular sciences · 2020Review
- Review
- A unifying model for the propagation of prion proteins in yeast brings insight into the [PSI+] prion.PLoS computational biology · 2020Article
- Variant-specific and reciprocal Hsp40 functions in Hsp104-mediated prion elimination.Molecular microbiology · 2018Article
- Real-time imaging of yeast cells reveals several distinct mechanisms of curing of the [URE3] prion.The Journal of biological chemistry · 2018Article
- Curing of [PSIPrion · 2018Article
- Heat shock protein 104 (Hsp104)-mediated curing of [The Journal of biological chemistry · 2017Article
- The small heat shock protein Hsp31 cooperates with Hsp104 to modulate Sup35 prion aggregation.Prion · 2016Article
- Hsp104 overexpression cures Saccharomyces cerevisiae [PSI+] by causing dissolution of the prion seeds.Eukaryotic cell · 2014Article
- Physiological and environmental control of yeast prions.FEMS microbiology reviews · 2014Review
- Yeast prions help identify and define chaperone interaction networks.Current pharmaceutical biotechnology · 2014Review
- Schizosaccharomyces pombe disaggregation machinery chaperones support Saccharomyces cerevisiae growth and prion propagation.Eukaryotic cell · 2013Article
- Defining the limits: Protein aggregation and toxicity in vivo.Critical reviews in biochemistry and molecular biologyReview
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
[PSI(+)] yeast, containing the misfolded amyloid conformation of Sup35 prion, is cured by inactivation of Hsp104. There has been controversy as to whether inactivation of Hsp104 by guanidine treatment or by overexpression of the dominant negative Hsp104 mutant, Hsp104-2KT, cures [PSI(+)] by the same mechanism- inhibition of the severing of the prion seeds. Using live cell imaging of Sup35-GFP, overexpression of Hsp104-2KT caused the foci to increase in size, then decrease in number, and finally disappear when the cells were cured, similar to that observed in cells cured by depletion of Hsp104. In contrast, guanidine initially caused an increase in foci size but then the foci disappeared before the cells were cured. By starving the yeast to make the foci visible in cells grown with guanidine, the number of cells with foci was found to correlate exactly with the number of [PSI(+)] cells, regardless of the curing method. Therefore, the fluorescent foci are the prion seeds required for maintenance of [PSI(+)] and inactivation of Hsp104 cures [PSI(+)] by preventing severing of the prion seeds. During curing with guanidine, the reduction in seed size is an Hsp104-dependent effect that cannot be explained by limited severing of the seeds. Instead, in the presence of guanidine, Hsp104 retains an activity that trims or reduces the size of the prion seeds by releasing Sup35 molecules that are unable to form new prion seeds. This Hsp104 activity may also occur in propagating yeast.
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