ArticleProceedings of the National Academy of Sciences of the United States of America2014
Fungal prion HET-s as a model for structural complexity and self-propagation in prions.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Regulated cell death in fungi from a comparative immunology perspective.Cell death and differentiation · 2026Review
- Exogenous prion-like proteins and their potential to trigger cognitive dysfunction.Molecular systems biology · 2025Article
- What are the 100 most cited fungal genera?Studies in mycology · 2024Article
- Rational design of structure-based vaccines targeting misfolded alpha-synuclein conformers of Parkinson's disease and related disorders.Bioengineering & translational medicine · 2024Article
- Structural and molecular basis of cross-seeding barriers in amyloids.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Asparagine and Glutamine Side-Chains and Ladders in HET-s(218-289) Amyloid Fibrils Studied by Fast Magic-Angle Spinning NMR.Frontiers in molecular biosciences · 2020Article
- Comparing the Folds of Prions and Other Pathogenic Amyloids.Pathogens (Basel, Switzerland) · 2018Review
- Toward a Soluble Model System for the Amyloid State.Journal of the American Chemical Society · 2017Article
- A 31-residue peptide induces aggregation of tau's microtubule-binding region in cells.Nature chemistry · 2017Article
- Structural Biology of PrP Prions.Cold Spring Harbor perspectives in medicine · 2017Review
- Diversity of Amyloid Motifs in NLR Signaling in Fungi.Biomolecules · 2017Review
- Article
- Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.PloS one · 2017Article
- Characterization of Amyloid Cores in Prion Domains.Scientific reports · 2016Article
- Article
- The HET-S/s Prion Motif in the Control of Programmed Cell Death.Cold Spring Harbor perspectives in biology · 2016Review
- A glass menagerie of low complexity sequences.Current opinion in structural biology · 2016Review
- Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein.Nature structural & molecular biology · 2016Article
- Theme and variations: evolutionary diversification of the HET-s functional amyloid motif.Scientific reports · 2015Article
- Signal transduction by a fungal NOD-like receptor based on propagation of a prion amyloid fold.PLoS biology · 2015Article
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Authors and funding
2 authors.
Funding
Abstract
The highly ordered and reproducible structure of the fungal prion HET-s makes it an excellent model system for studying the inherent properties of prions, self-propagating infectious proteins that have been implicated in a number of fatal diseases. In particular, the HET-s prion-forming domain readily folds into a relatively complex two-rung β-solenoid amyloid. The faithful self-propagation of this fold involves a diverse array of inter- and intramolecular structural features. These features include a long flexible loop connecting the two rungs, buried polar residues, salt bridges, and asparagine ladders. We have used site-directed mutagenesis and X-ray fiber diffraction to probe the relative importance of these features for the formation of β-solenoid structure, as well as the cumulative effects of multiple mutations. Using fibrillization kinetics and chemical stability assays, we have determined the biophysical effects of our mutations on the assembly and stability of the prion-forming domain. We have found that a diversity of structural features provides a level of redundancy that allows robust folding and stability even in the face of significant sequence alterations and suboptimal environmental conditions. Our findings provide fundamental insights into the structural interactions necessary for self-propagation. Propagation of prion structure seems to require an obligatory level of complexity that may not be reproducible in short peptide models.
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