ArticleProceedings of the National Academy of Sciences of the United States of America2007
Prion species barrier between the closely related yeast proteins is detected despite coaggregation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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45 citing papers in PubMed, 65 citations in OpenAlex.
- Deletion Analysis of Phase Separation, Amyloid Formation and Prion Propagation by the Intrinsically Disordered Region of Yeast Sup35 Protein.International journal of molecular sciences · 2026Article
- Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025Review
- Osmotic stress induces formation of both liquid condensates and amyloids by a yeast prion domain.The Journal of biological chemistry · 2024Article
- Review
- Innate immunity to prions: anti-prion systems turn a tsunami of prions into a slow drip.Current genetics · 2021Review
- How Do Yeast Cells Contend with Prions?International journal of molecular sciences · 2020Review
- Short disordered protein segment regulates cross-species transmission of a yeast prion.Nature chemical biology · 2020Article
- [PIN+]ing down the mechanism of prion appearance.FEMS yeast research · 2018Review
- Yeast and Fungal Prions.Cold Spring Harbor perspectives in biology · 2016Review
- Strain conformation controls the specificity of cross-species prion transmission in the yeast model.Prion · 2016Article
- Prions are affected by evolution at two levels.Cellular and molecular life sciences : CMLS · 2016Review
- Contributions of the Prion Protein Sequence, Strain, and Environment to the Species Barrier.The Journal of biological chemistry · 2016Article
- Yeast and Fungal Prions: Amyloid-Handling Systems, Amyloid Structure, and Prion Biology.Advances in genetics · 2016Article
- Mechanisms of amyloid formation revealed by solution NMR.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- Yeast prions: structure, biology, and prion-handling systems.Microbiology and molecular biology reviews : MMBR · 2015Review
- W8, a new Sup35 prion strain, transmits distinctive information with a conserved assembly scheme.Prion · 2015Article
- Article
- Amyloid diseases of yeast: prions are proteins acting as genes.Essays in biochemistry · 2014Article
- Ion-specific effects on prion nucleation and strain formation.The Journal of biological chemistry · 2013Article
- 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
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prions are self-perpetuating and, in most cases, aggregation-prone protein isoforms that transmit neurodegenerative diseases in mammals and control heritable traits in yeast. Prion conversion requires a very high level of identity of the interacting protein sequences. Decreased transmission of the prion state between divergent proteins is termed "species barrier" and was thought to occur because of the inability of divergent prion proteins to coaggregate. Species barrier can be overcome in cross-species infections, e.g., from "mad cows" to humans. We studied the counterparts of yeast prion protein Sup35, originated from three different species of the Saccharomyces sensu stricto group and exhibiting the range of prion domain divergence that overlaps with the range of divergence observed among distant mammalian species. All three proteins were capable of forming a prion in Saccharomyces cerevisiae, although prions formed by heterologous proteins were usually less stable than the endogenous S. cerevisiae prion. Heterologous Sup35 proteins coaggregated in the S. cerevisiae cells. However, in vivo cross-species prion conversion was decreased and in vitro polymerization was cross-inhibited in at least some heterologous combinations, thus demonstrating the existence of prion species barrier. Moreover, the barrier between the S. cerevisiae protein and its Saccharomyces paradoxus and Saccharomyces bayanus counterparts was asymmetric both in vivo and in vitro. Our data show that a decreased cross-species prion transmission does not necessarily correlate with a lack of cross-species coaggregation, suggesting that species-specificity of prion transmission is controlled at the level of conformational transition rather than coaggregation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.