ArticleEukaryotic cell2013
The [URE3] prion in Candida.
Article in Eukaryotic cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 18 citations in OpenAlex.
- Distinct properties of human pathogenicmSystems · 2026Article
- Yeast J-protein Sis1 prevents prion toxicity by moderating depletion of prion protein.Genetics · 2021Article
- Conservation of Prion-Like Composition and Sequence in Prion-Formers and Prion-Like Proteins ofFrontiers in molecular biosciences · 2019Article
- An Evolutionary Perspective on Yeast Mating-Type Switching.Genetics · 2017Review
- Yeast and Fungal Prions.Cold Spring Harbor perspectives in biology · 2016Review
- Emergence and evolution of yeast prion and prion-like proteins.BMC evolutionary biology · 2016Article
- 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
- Article
- Mating-type switching by chromosomal inversion in methylotrophic yeasts suggests an origin for the three-locus Saccharomyces cerevisiae system.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
- The Candida pathogenic species complex.Cold Spring Harbor perspectives in medicine · 2014Review
- Effect of domestication on the spread of the [PIN+] prion in Saccharomyces cerevisiae.Genetics · 2014Article
- Amyloids and yeast prion biology.Biochemistry · 2013Article
- Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
Ure2p, normally a regulator of nitrogen catabolism in Saccharomyces cerevisiae, can be a prion (infectious protein) by forming a folded in-register parallel amyloid called [URE3]. Using S. cerevisiae as a test bed, we previously showed that Ure2p of Candida albicans (CaUre2p) can also form a prion, but that Ure2p of C. glabrata (CgUre2p) cannot. Here, we constructed C. glabrata strains to test whether CgUre2p can form a prion in its native environment. We find that while CaUre2p can form a [URE3] in C. glabrata, CgUre2p cannot, although the latter has a prion domain sequence more similar to that of ScUre2p than that of CaUre2p. This supports the notion that prion formation is not a conserved property of Ure2p but is a pathology arising sporadically. We find that some [URE3albicans] variants are restricted in their transmissibility to certain recipient strains. In addition, we show that the C. glabrata HO can induce switching of the C. glabrata mating type locus.
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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.