ArticlePLoS pathogens2014
Contribution of specific residues of the β-solenoid fold to HET-s prion function, amyloid structure and stability.
Article in PLoS pathogens, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 50 citations in OpenAlex.
- Prion propagation is controlled by discrete structural regions of PrP rather than overall stability.The Journal of biological chemistry · 2026Article
- Characterization of an amyloid-based antiphage defence system in Escherichia coli.Nature microbiology · 2025Article
- Homonuclear J-couplings and heteronuclear structural constraints.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2024Article
- Accurate model and ensemble refinement using cryo-electron microscopy maps and Bayesian inference.PLoS computational biology · 2024Article
- Analytical Framework to Understand the Origins of Methyl Side-Chain Dynamics in Protein Assemblies.Journal of the American Chemical Society · 2024Article
- Site specific NMR characterization of abeta-40 oligomers cross seeded by abeta-42 oligomers.Chemical science · 2022Article
- Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022Review
- Structural and molecular basis of cross-seeding barriers in amyloids.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structures of Pathological and Functional Amyloids and Prions, a Solid-State NMR Perspective.Frontiers in molecular neuroscience · 2021Review
- Functional Amyloids.Cold Spring Harbor perspectives in biology · 2019Review
- Cryo-EM of amyloid fibrils and cellular aggregates.Current opinion in structural biology · 2019Review
- Probing the mechanism of inhibition of amyloid-β(1-42)-induced neurotoxicity by the chaperonin GroEL.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Quantifying Nucleation In Vivo Reveals the Physical Basis of Prion-like Phase Behavior.Molecular cell · 2018Article
- Organizing biochemistry in space and time using prion-like self-assembly.Current opinion in systems biology · 2018Article
- Toward a Soluble Model System for the Amyloid State.Journal of the American Chemical Society · 2017Article
- Chaperonin GroEL accelerates protofibril formation and decorates fibrils of the Het-s prion protein.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Diversity of Amyloid Motifs in NLR Signaling in Fungi.Biomolecules · 2017Review
- Mapping the Broad Structural and Mechanical Properties of Amyloid Fibrils.Biophysical journal · 2017Article
- The Three-Dimensional Structures of Amyloids.Cold Spring Harbor perspectives in biology · 2017Review
- Protein folding, misfolding and aggregation: The importance of two-electron stabilizing interactions.PloS one · 2017Article
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Authors and funding
13 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The [Het-s] prion of the fungus Podospora anserina represents a good model system for studying the structure-function relationship in amyloid proteins because a high resolution solid-state NMR structure of the amyloid prion form of the HET-s prion forming domain (PFD) is available. The HET-s PFD adopts a specific β-solenoid fold with two rungs of β-strands delimiting a triangular hydrophobic core. A C-terminal loop folds back onto the rigid core region and forms a more dynamic semi-hydrophobic pocket extending the hydrophobic core. Herein, an alanine scanning mutagenesis of the HET-s PFD was conducted. Different structural elements identified in the prion fold such as the triangular hydrophobic core, the salt bridges, the asparagines ladders and the C-terminal loop were altered and the effect of these mutations on prion function, fibril structure and stability was assayed. Prion activity and structure were found to be very robust; only a few key mutations were able to corrupt structure and function. While some mutations strongly destabilize the fold, many substitutions in fact increase stability of the fold. This increase in structural stability did not influence prion formation propensity in vivo. However, if an Ala replacement did alter the structure of the core or did influence the shape of the denaturation curve, the corresponding variant showed a decreased prion efficacy. It is also the finding that in addition to the structural elements of the rigid core region, the aromatic residues in the C-terminal semi-hydrophobic pocket are critical for prion propagation. Mutations in the latter region either positively or negatively affected prion formation. We thus identify a region that modulates prion formation although it is not part of the rigid cross-β core, an observation that might be relevant to other amyloid models.
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