ArticleMolecular microbiology2011
In Sup35p filaments (the [PSI+] prion), the globular C-terminal domains are widely offset from the amyloid fibril backbone.
Article in Molecular microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 44 citations in OpenAlex.
- Prion-Dependent Lethality ofInternational journal of molecular sciences · 2025Article
- The middle domain of Hsp104 can ensure substrates are functional after processing.PLoS genetics · 2024Article
- Genetic Functionalization of Protein-Based Biomaterials via Protein Fusions.Biomacromolecules · 2024Review
- Beyond Amyloid Fibers: Accumulation, Biological Relevance, and Regulation of Higher-Order Prion Architectures.Viruses · 2022Review
- Amyloid fibril length distribution from dynamic light scattering data.European biophysics journal : EBJ · 2022Article
- Structural Bases of Prion Variation in Yeast.International journal of molecular sciences · 2022Review
- Amyloid Fragmentation and Disaggregation in Yeast and Animals.Biomolecules · 2021Review
- Yeast J-protein Sis1 prevents prion toxicity by moderating depletion of prion protein.Genetics · 2021Article
- Extracellular Vesicles-Encapsulated Yeast Prions and What They Can Tell Us about the Physical Nature of Propagons.International journal of molecular sciences · 2020Review
- Article
- Review
- Amyloid fibrils embodying distinctive yeast prion phenotypes exhibit diverse morphologies.FEMS yeast research · 2018Article
- Prion aggregate structure in yeast cells is determined by the Hsp104-Hsp110 disaggregase machinery.The Journal of cell biology · 2015Article
- PrionW: a server to identify proteins containing glutamine/asparagine rich prion-like domains and their amyloid cores.Nucleic acids research · 2015Article
- The 26S Proteasome Degrades the Soluble but Not the Fibrillar Form of the Yeast Prion Ure2p In Vitro.PloS one · 2015Article
- Review
- Evolutionary link between metazoan RHIM motif and prion-forming domain of fungal heterokaryon incompatibility factor HET-s/HET-s.Scientific reports · 2014Article
- Amyloid-associated activity contributes to the severity and toxicity of a prion phenotype.Nature communications · 2014Article
- Extensive diversity of prion strains is defined by differential chaperone interactions and distinct amyloidogenic regions.PLoS genetics · 2014Article
- Effect of charged residues in the N-domain of Sup35 protein on prion [PSI+] stability and propagation.The Journal of biological chemistry · 2013Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
In yeast cells infected with the [PSI+] prion, Sup35p forms aggregates and its activity in translation termination is downregulated. Transfection experiments have shown that Sup35p filaments assembled in vitro are infectious, suggesting that they reproduce or closely resemble the prion. We have used several EM techniques to study the molecular architecture of filaments, seeking clues as to the mechanism of downregulation. Sup35p has an N-terminal 'prion' domain; a highly charged middle (M-)domain; and a C-terminal domain with the translation termination activity. By negative staining, cryo-EM and scanning transmission EM (STEM), filaments of full-length Sup35p show a thin backbone fibril surrounded by a diffuse 65-nm-wide cloud of globular C-domains. In diameter (∼8 nm) and appearance, the backbones resemble amyloid fibrils of N-domains alone. STEM mass-per-unit-length data yield ∼1 subunit per 0.47 nm for N-fibrils, NM-filaments and Sup35p filaments, further supporting the fibril backbone model. The 30 nm radial span of decorating C-domains indicates that the M-domains assume highly extended conformations, offering an explanation for the residual Sup35p activity in infected cells, whereby the C-domains remain free enough to interact with ribosomes.
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