ArticleBiochemistry2011
Amyloid of the Candida albicans Ure2p prion domain is infectious and has an in-register parallel β-sheet structure.
Article in Biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- Solid-State NMR Investigations of Extracellular Matrixes and Cell Walls of Algae, Bacteria, Fungi, and Plants.Chemical reviews · 2022Review
- Yeast and Fungal Prions.Cold Spring Harbor perspectives in biology · 2016Review
- Yeast and Fungal Prions: Amyloid-Handling Systems, Amyloid Structure, and Prion Biology.Advances in genetics · 2016Article
- Residue-by-Residue View of In Vitro FUS Granules that Bind the C-Terminal Domain of RNA Polymerase II.Molecular cell · 2015Article
- Yeast prions: structure, biology, and prion-handling systems.Microbiology and molecular biology reviews : MMBR · 2015Review
- Article
- The [URE3] prion in Candida.Eukaryotic cell · 2013Article
- Prions in yeast.Genetics · 2012Review
- The heat-induced molecular disaggregase Hsp104 of Candida albicans plays a role in biofilm formation and pathogenicity in a worm infection model.Eukaryotic cell · 2012Article
- Discovering protein-based inheritance through yeast genetics.The Journal of biological chemistry · 2012Review
- Strengthening relationships: amyloids create adhesion nanodomains in yeasts.Trends in microbiology · 2012Article
- Experimentally derived structural constraints for amyloid fibrils of wild-type transthyretin.Biophysical journal · 2011Article
- Site-specific structural analysis of a yeast prion strain with species-specific seeding activity.PrionArticle
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5 authors.
Funding
Abstract
Ure2p of Candida albicans (Ure2(albicans) or CaUre2p) can be a prion in Saccharomyces cerevisiae, but Ure2p of Candida glabrata (Ure2(glabrata)) cannot, even though the Ure2(glabrata) N-terminal domain is more similar to that of the S. cerevisiae Ure2p (Ure2(cerevisiae)) than Ure2(albicans) is. We show that the N-terminal N/Q-rich prion domain of Ure2(albicans) forms amyloid that is infectious, transmitting [URE3alb] to S. cerevisiae cells expressing only C. albicans Ure2p. Using solid-state nuclear magnetic resonance of selectively labeled C. albicans Ure2p(1-90), we show that this infectious amyloid has an in-register parallel β-sheet structure, like that of the S. cerevisiae Ure2p prion domain and other S. cerevisiae prion amyloids. In contrast, the N/Q-rich N-terminal domain of Ure2(glabrata) does not readily form amyloid, and that formed upon prolonged incubation is not infectious.
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