ArticleMolecular and cellular biology2002
Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p.
Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.
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Who cites it
116 citing papers in PubMed, 173 citations in OpenAlex.
- Intracellular aggregation of the transthyretin protein is limited by Hsp70 chaperones.bioRxiv : the preprint server for biology · 2025Article
- Stress granules and protein aggregates reveal intracellular resource competition.bioRxiv : the preprint server for biology · 2025Article
- Yeast Chaperone Hsp70-Ssb Modulates a Variety of Protein-Based Heritable Elements.International journal of molecular sciences · 2023Article
- A SingleInternational journal of molecular sciences · 2022Article
- Review
- Differential Interactions of Molecular Chaperones and Yeast Prions.Journal of fungi (Basel, Switzerland) · 2022Review
- Do Transgenerational Epigenetic Inheritance and Immune System Development Share Common Epigenetic Processes?Journal of developmental biology · 2021Review
- Differential role of cytosolic Hsp70s in longevity assurance and protein quality control.PLoS genetics · 2021Article
- Understanding and exploiting interactions between cellular proteostasis pathways and infectious prion proteins for therapeutic benefit.Open biology · 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
- Mechanisms for Curing Yeast Prions.International journal of molecular sciences · 2020Review
- How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020Review
- Not quite the SSAme: unique roles for the yeast cytosolic Hsp70s.Current genetics · 2019Review
- Article
- The C-terminal GGAP motif of Hsp70 mediates substrate recognition and stress response in yeast.The Journal of biological chemistry · 2018Article
- The yeast stress inducible Ssa Hsp70 reduces α-synuclein toxicity by promoting its degradation through autophagy.PLoS genetics · 2018Article
- Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification.International journal of molecular sciences · 2018Review
- Generation and propagation of yeast prion [URE3] are elevated under electromagnetic field.Cell stress & chaperones · 2018Article
- Article
- Differential effects of chaperones on yeast prions: CURrent view.Current genetics · 2018Review
56 more citing papers are in PubMed but not listed here.
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The yeast [PSI(+)], [URE3], and [PIN(+)] genetic elements are prion forms of Sup35p, Ure2p, and Rnq1p, respectively. Overexpression of Sup35p, Ure2p, or Rnq1p leads to increased de novo appearance of [PSI(+)], [URE3], and [PIN(+)], respectively. This inducible appearance of [PSI(+)] was shown to be dependent on the presence of [PIN(+)] or [URE3] or overexpression of other yeast proteins that have stretches of polar residues similar to the prion-determining domains of the known prion proteins. In a similar manner, [PSI(+)] and [URE3] facilitate the appearance of [PIN(+)]. In contrast to these positive interactions, here we find that in the presence of [PIN(+)], [PSI(+)] and [URE3] repressed each other's propagation and de novo appearance. Elevated expression of Hsp104 and Hsp70 (Ssa2p) had little effect on these interactions, ruling out competition between the two prions for limiting amounts of these protein chaperones. In contrast, we find that constitutive overexpression of SSA1 but not SSA2 cured cells of [URE3], uncovering a specific interaction between Ssa1p and [URE3] and a functional distinction between these nearly identical Hsp70 isoforms. We also find that Hsp104 abundance, which critically affects [PSI(+)] propagation, is elevated when [URE3] is present. Our results are consistent with the notion that proteins that have a propensity to form prions may interact with heterologous prions but, as we now show, in a negative manner. Our data also suggest that differences in how [PSI(+)] and [URE3] interact with Hsp104 and Hsp70 may contribute to their antagonistic interactions.
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Registered trials
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