ArticleProceedings of the National Academy of Sciences of the United States of America2012
Heritable yeast prions have a highly organized three-dimensional architecture with interfiber structures.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Cryo-EM structure of ex vivo Sup35 yeast prion and the factors defining prion phenotype.Nature communications · 2026Article
- 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025Review
- Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures.Viruses · 2022Review
- Extracellular Vesicles-Encapsulated Yeast Prions and What They Can Tell Us about the Physical Nature of Propagons.International journal of molecular sciences · 2020Review
- Investigating eukaryotic cells with cryo-ET.Molecular biology of the cell · 2020Article
- Cryo-EM of amyloid fibrils and cellular aggregates.Current opinion in structural biology · 2019Review
- A new era for understanding amyloid structures and disease.Nature reviews. Molecular cell biology · 2018Review
- Protein Co-Aggregation Related to Amyloids: Methods of Investigation, Diversity, and Classification.International journal of molecular sciences · 2018Review
- Translational Control by Prion-like Proteins.Trends in cell biology · 2018Review
- Molecular and structural architecture of polyQ aggregates in yeast.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- The Insoluble Protein Deposit (IPOD) in Yeast.Frontiers in molecular neuroscience · 2018Article
- Heterogeneous interaction network of yeast prions and remodeling factors detected in live cells.BMB reports · 2017Article
- Prion-Associated Toxicity is Rescued by Elimination of Cotranslational Chaperones.PLoS genetics · 2016Article
- Prion Aggregates Are Recruited to the Insoluble Protein Deposit (IPOD) via Myosin 2-Based Vesicular Transport.PLoS genetics · 2016Article
- Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Protein aggregates are associated with replicative aging without compromising protein quality control.eLife · 2015Article
- Specific chaperones and regulatory domains in control of amyloid formation.The Journal of biological chemistry · 2015Review
- Article
- Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.The Journal of cell biology · 2015Article
- Hsp31 Is a Stress Response Chaperone That Intervenes in the Protein Misfolding Process.The Journal of biological chemistry · 2015Article
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13 authors.
Funding
Abstract
Yeast prions constitute a "protein-only" mechanism of inheritance that is widely deployed by wild yeast to create diverse phenotypes. One of the best-characterized prions, [PSI(+)], is governed by a conformational change in the prion domain of Sup35, a translation-termination factor. When this domain switches from its normal soluble form to an insoluble amyloid, the ensuing change in protein synthesis creates new traits. Two factors make these traits heritable: (i) the amyloid conformation is self-templating; and (ii) the protein-remodeling factor heat-shock protein (Hsp)104 (acting together with Hsp70 chaperones) partitions the template to daughter cells with high fidelity. Prions formed by several other yeast proteins create their own phenotypes but share the same mechanistic basis of inheritance. Except for the amyloid fibril itself, the cellular architecture underlying these protein-based elements of inheritance is unknown. To study the 3D arrangement of prion assemblies in their cellular context, we examined yeast [PSI(+)] prions in the native, hydrated state in situ, taking advantage of recently developed methods for cryosectioning of vitrified cells. Cryo-electron tomography of the vitrified sections revealed the prion assemblies as aligned bundles of regularly spaced fibrils in the cytoplasm with no bounding structures. Although the fibers were widely spaced, other cellular complexes, such as ribosomes, were excluded from the fibril arrays. Subtomogram image averaging, made possible by the organized nature of the assemblies, uncovered the presence of an additional array of densities between the fibers. We suggest these structures constitute a self-organizing mechanism that coordinates fiber deposition and the regulation of prion inheritance.
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