ArticleProceedings of the National Academy of Sciences of the United States of America2002
Conservation of a portion of the S. cerevisiae Ure2p prion domain that interacts with the full-length protein.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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Who cites it
51 citing papers in PubMed, 77 citations in OpenAlex.
- Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025Review
- Anti-Prion Systems inViruses · 2022Review
- Review
- Innate immunity to prions: anti-prion systems turn a tsunami of prions into a slow drip.Current genetics · 2021Review
- Proteasome Control of [URE3] Prion Propagation by Degradation of Anti-Prion Proteins Cur1 and Btn2 in Saccharomyces cerevisiae.Genetics · 2021Article
- Article
- Effect of spin labelling on the aggregation kinetics of yeast prion protein Ure2.Royal Society open science · 2021Article
- Spin Label Scanning Reveals Likely Locations of β-Strands in the Amyloid Fibrils of the Ure2 Prion Domain.ACS omega · 2020Article
- Nonsense Mutations in the YeastInternational journal of molecular sciences · 2020Article
- Anti-Prion Systems in Yeast and Inositol Polyphosphates.Biochemistry · 2018Article
- Study of Amyloids Using Yeast.Methods in molecular biology (Clifton, N.J.) · 2018Article
- Yeast and Fungal Prions.Cold Spring Harbor perspectives in biology · 2016Review
- Prions are affected by evolution at two levels.Cellular and molecular life sciences : CMLS · 2016Review
- Yeast and Fungal Prions: Amyloid-Handling Systems, Amyloid Structure, and Prion Biology.Advances in genetics · 2016Article
- Yeast prions: structure, biology, and prion-handling systems.Microbiology and molecular biology reviews : MMBR · 2015Review
- Proteins with Intrinsically Disordered Domains Are Preferentially Recruited to Polyglutamine Aggregates.PloS one · 2015Article
- Article
- Amyloid diseases of yeast: prions are proteins acting as genes.Essays in biochemistry · 2014Article
- The [URE3] prion in Candida.Eukaryotic cell · 2013Article
- Amyloids and yeast prion biology.Biochemistry · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The [URE3] prion of Saccharomyces cerevisiae is a self-propagating inactive amyloid form of the Ure2 protein. Ure2p residues 1-65 constitute the prion domain, and the remaining C-terminal portion regulates nitrogen catabolism. We have examined the URE2 genes of wild-type isolates of S. cerevisiae and those of several pathogenic yeasts and a filamentous fungus. We find that the normal function of the S. cerevisiae Ure2p in nitrogen regulation is fully complemented by the Ure2p of Candida albicans, Candida glabrata, Candida kefyr, Candida maltosa, Saccharomyces bayanus, and Saccharomyces paradoxus, all of which have high homology in the C-terminal nitrogen regulation domain. However, there is considerable divergence of their N-terminal domains from that of Ure2p of S. cerevisiae. [URE3(Sc)] showed efficient transmission into S. cerevisiae ure2Delta cells if expressing a Ure2p of species within Saccharomyces. However, [URE3(Sc)] did not seed self-propagating inactivation of the Ure2p's from the other yeasts. When overexpressed as a fusion with green fluorescent protein, residues 5-47 of the S. cerevisiae prion domain are necessary for curing the [URE3] prion. Residues 11-39 are necessary for an inactivating interaction with the full-length Ure2p. A nearly identical region is highly conserved among many of the yeasts examined in this study, despite the wide divergence of sequences found in other parts of the N-terminal domains.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.