ArticleMolecular and cellular biology2001
Induction of distinct [URE3] yeast prion strains.
Article in Molecular and cellular biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.
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Who cites it
94 citing papers in PubMed, 153 citations in OpenAlex.
- The p53 DNA-Binding (Core) Domain can form a prion that seeds prion formation in full-length p53.Microbial cell (Graz, Austria) · 2026Article
- Detection system- and strain-dependent diversity of de novo [PSI+] prion generation and phenotypes in Saccharomyces cerevisiae.Journal of microbiology (Seoul, Korea) · 2025Article
- A Story Between s and S: [Het-s] Prion of the FungusMycobiology · 2024Review
- Amyloids and prions in the light of evolution.Current genetics · 2023Review
- MIL-CELL: a tool for multi-scale simulation of yeast replication and prion transmission.European biophysics journal : EBJ · 2023Article
- Yeast Chaperone Hsp70-Ssb Modulates a Variety of Protein-Based Heritable Elements.International journal of molecular sciences · 2023Article
- Review
- Antiprion systems in yeast cooperate to cure or prevent the generation of nearly all [Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022Review
- Biochemical Principles in Prion-Based Inheritance.Epigenomes · 2022Review
- Proteasome Control of [URE3] Prion Propagation by Degradation of Anti-Prion Proteins Cur1 and Btn2 in Saccharomyces cerevisiae.Genetics · 2021Article
- Article
- Extracellular Vesicles and the Propagation of Yeast Prions.Current topics in microbiology and immunology · 2021Article
- Extracellular Vesicles-Encapsulated Yeast Prions and What They Can Tell Us about the Physical Nature of Propagons.International journal of molecular sciences · 2020Review
- 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
- The actin cytoskeletal network plays a role in yeast prion transmission and contributes to prion stability.Molecular microbiology · 2020Article
- How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020Review
- The role of prion strain diversity in the development of successful therapeutic treatments.Progress in molecular biology and translational science · 2020Review
- Identifying Anti-prion Chemical Compounds Using a Newly Established Yeast High-Throughput Screening System.Cell chemical biology · 2019Article
34 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 2 institutions in 3 countries.
Funding
Abstract
[URE3] is a non-Mendelian genetic element in Saccharomyces cerevisiae, which is caused by a prion-like, autocatalytic conversion of the Ure2 protein (Ure2p) into an inactive form. The presence of [URE3] allows yeast cells to take up ureidosuccinic acid in the presence of ammonia. This phenotype can be used to select for the prion state. We have developed a novel reporter, in which the ADE2 gene is controlled by the DAL5 regulatory region, which allows monitoring of Ure2p function by a colony color phenotype. Using this reporter, we observed induction of different [URE3] prion variants ("strains") following overexpression of the N-terminal Ure2p prion domain (UPD) or full-length Ure2p. Full-length Ure2p induced two types of [URE3]: type A corresponds to conventional [URE3], whereas the novel type B variant is characterized by relatively high residual Ure2p activity and efficient curing by coexpression of low amounts of a UPD-green fluorescent protein fusion protein. Overexpression of UPD induced type B [URE3] but not type A. Both type A and B [URE3] strains, as well as weak and strong isolates of type A, were shown to stably maintain different prion strain characteristics. We suggest that these strain variants result from different modes of aggregation of similar Ure2p monomers. We also demonstrate a procedure to counterselect against the [URE3] state.
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