ArticleThe Journal of biological chemistry2011
Hierarchical organization in the amyloid core of yeast prion protein Ure2.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Review
- Innate immunity to prions: anti-prion systems turn a tsunami of prions into a slow drip.Current genetics · 2021Review
- Effect of spin labelling on the aggregation kinetics of yeast prion protein Ure2.Royal Society open science · 2021Article
- Atomic-level differences between brain parenchymal- and cerebrovascular-seeded Aβ fibrils.Scientific reports · 2021Article
- How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020Review
- Spin Label Scanning Reveals Likely Locations of β-Strands in the Amyloid Fibrils of the Ure2 Prion Domain.ACS omega · 2020Article
- Thioflavin T as an amyloid dye: fibril quantification, optimal concentration and effect on aggregation.Royal Society open science · 2017Article
- A new structural model of Alzheimer's Aβ42 fibrils based on electron paramagnetic resonance data and Rosetta modeling.Journal of structural 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
- Locating folds of the in-register parallel β-sheet of the Sup35p prion domain infectious amyloid.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Antiparallel triple-strand architecture for prefibrillar Aβ42 oligomers.The Journal of biological chemistry · 2014Article
- The BAG homology domain of Snl1 cures yeast prion [URE3] through regulation of Hsp70 chaperones.G3 (Bethesda, Md.) · 2014Article
- Amyloids and yeast prion biology.Biochemistry · 2013Article
- Prions in yeast.Genetics · 2012Review
- Fibrillogenesis of huntingtin and other glutamine containing proteins.Sub-cellular biochemistry · 2012Review
- Prion domain of yeast Ure2 protein adopts a completely disordered structure: a solid-support EPR study.PloS one · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formation of amyloid fibrils is involved in a range of fatal human disorders including Alzheimer, Parkinson, and prion diseases. Yeast prions, despite differences in sequence from their mammalian counterparts, share similar features with mammalian prions including infectivity, prion strain phenomenon, and species barrier and thus are good model systems for human prion diseases. Yeast prions normally have long prion domains that presumably form multiple β strands in the fibril, and structural knowledge about the yeast prion fibrils has been limited. Here we use site-directed spin labeling and electron paramagnetic resonance (EPR) spectroscopy to investigate the structures of amyloid fibrils of Ure2 prion domain. We show that 15 spin-labeled Ure2 mutants, with spin labels at every 5th residue from position 5 to position 75, show a single-line or nearly single-line feature in their EPR spectra as a result of strong spin exchange interactions. These results suggest that a parallel in-register β structure exists at these spin-labeled positions. More interestingly, we also show that residues in the segment 30-65 have stronger spin exchange interactions, higher local stability, and lower solvent accessibility than segments 5-25 and 70-75, suggesting different local environment at these segments. We propose a hierarchical organization in the amyloid core of Ure2, with the segment 30-65 forming an inner core and the segments 5-25 and 70-75 forming an outer core. The hierarchical organization in the amyloid core may be a structural origin for polymorphism in fibrils and prion strains.
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