ArticleProceedings of the National Academy of Sciences of the United States of America2015
Generating new prions by targeted mutation or segment duplication.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 24 citations in OpenAlex.
- Anti-Prion Systems in Saccharomyces cerevisiae.Journal of neurochemistry · 2025Review
- Defining Key Residues of the Swi1 Prion Domain in Prion Formation and Maintenance.Molecular and cellular biology · 2021Article
- Composition-based prediction and rational manipulation of prion-like domain recruitment to stress granules.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- AMYCO: evaluation of mutational impact on prion-like proteins aggregation propensity.BMC bioinformatics · 2019Article
- The causes of evolvability and their evolution.Nature reviews. Genetics · 2019Review
- Evolutionary behaviour of bacterial prion-like proteins.PloS one · 2019Article
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- Prion-based memory of heat stress in yeast.Prion · 2017Article
- Effects of Mutations on the Aggregation Propensity of the Human Prion-Like Protein hnRNPA2B1.Molecular and cellular biology · 2017Article
- Amino acid composition predicts prion activity.PLoS computational biology · 2017Article
- Yeast Short-Lived Actin-Associated Protein Forms a Metastable Prion in Response to Thermal Stress.Cell reports · 2017Article
- Characterization of Amyloid Cores in Prion Domains.Scientific reports · 2016Article
- Prion-like domains as epigenetic regulators, scaffolds for subcellular organization, and drivers of neurodegenerative disease.Brain research · 2016Review
- Prions are affected by evolution at two levels.Cellular and molecular life sciences : CMLS · 2016Review
- Emergence and evolution of yeast prion and prion-like proteins.BMC evolutionary biology · 2016Article
- Yeast and Fungal Prions: Amyloid-Handling Systems, Amyloid Structure, and Prion Biology.Advances in genetics · 2016Article
- Proline and lysine residues provide modulatory switches in amyloid formation: Insights from prion protein.Prion · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Yeasts contain various protein-based genetic elements, termed prions, that result from the structural conversion of proteins into self-propagating amyloid forms. Most yeast prion proteins contain glutamine/asparagine (Q/N)-rich prion domains that drive prion activity. Here, we explore two mechanisms by which new prion domains could evolve. First, it has been proposed that mutation and natural selection will tend to result in proteins with aggregation propensities just low enough to function under physiological conditions and thus that a small number of mutations are often sufficient to cause aggregation. We hypothesized that if the ability to form prion aggregates was a sufficiently generic feature of Q/N-rich domains, many nonprion Q/N-rich domains might similarly have aggregation propensities on the edge of prion formation. Indeed, we tested four yeast Q/N-rich domains that had no detectable aggregation activity; in each case, a small number of rationally designed mutations were sufficient to cause the proteins to aggregate and, for two of the domains, to create prion activity. Second, oligopeptide repeats are found in multiple prion proteins, and expansion of these repeats increases prion activity. However, it is unclear whether the effects of repeat expansion are unique to these specific sequences or are a generic result of adding additional aggregation-prone segments into a protein domain. We found that within nonprion Q/N-rich domains, repeating aggregation-prone segments in tandem was sufficient to create prion activity. Duplication of DNA elements is a common source of genetic variation and may provide a simple mechanism to rapidly evolve prion activity.
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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.