ArticleMolecular and cellular biology2000
[URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 159 papers.
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Who cites it
159 citing papers in PubMed.
- Modelling human proteostasis and organelle homeostasis disorders in yeast and its application in drug discovery.FEMS yeast research · 2026Review
- The p53 DNA-Binding (Core) Domain can form a prion that seeds prion formation in full-length p53.Microbial cell (Graz, Austria) · 2026Article
- Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025Review
- Human proteins curing yeast prions.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Hsp70 Binding to the N-terminal Domain of Hsp104 Regulates [Molecular and cellular biology · 2023Article
- Article
- Clearance of variant Creutzfeldt-Jakob disease prions in vivo by the Hsp70 disaggregase system.Brain : a journal of neurology · 2022Article
- Review
- Review
- Differential Interactions of Molecular Chaperones and Yeast Prions.Journal of fungi (Basel, Switzerland) · 2022Review
- Amyloid Fragmentation and Disaggregation in Yeast and Animals.Biomolecules · 2021Review
- Innate immunity to prions: anti-prion systems turn a tsunami of prions into a slow drip.Current genetics · 2021Review
- Yeast J-protein Sis1 prevents prion toxicity by moderating depletion of prion protein.Genetics · 2021Article
- Article
- Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit.Open biology · 2020Article
- Normal levels of ribosome-associated chaperones cure two groups of [PSI+] prion variants.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Mutations Outside the Ure2 Amyloid-Forming Region Disrupt [URE3] Prion Propagation and Alter Interactions with Protein Quality Control Factors.Molecular and cellular biology · 2020Article
- From Seeds to Fibrils and Back: Fragmentation as an Overlooked Step in the Propagation of Prions and Prion-Like Proteins.Biomolecules · 2020Review
- Mechanisms for Curing Yeast Prions.International journal of molecular sciences · 2020Review
- Three J-proteins impact Hsp104-mediated variant-specific prion elimination: a new critical role for a low-complexity domain.Current genetics · 2020Review
99 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The [URE3] nonchromosomal genetic element is an infectious form (prion) of the Ure2 protein, apparently a self-propagating amyloidosis. We find that an insertion mutation or deletion of HSP104 results in inability to propagate the [URE3] prion. Our results indicate that Hsp104 is a common factor in the maintenance of two independent yeast prions. However, overproduction of Hsp104 does not affect the stability of [URE3], in contrast to what is found for the [PSI(+)] prion, which is known to be cured by either overproduction or deficiency of Hsp104. Like Hsp104, the Hsp40 class chaperone Ydj1p, with the Hsp70 class Ssa1p, can renature proteins. We find that overproduction of Ydj1p results in a gradual complete loss of [URE3]. The involvement of protein chaperones in the propagation of [URE3] indicates a role for protein conformation in inheritance.
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Registered trials
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