ArticleMolecular and cellular biology2015
Distinct amino acid compositional requirements for formation and maintenance of the [PSI⁺] prion in yeast.
Article in Molecular and cellular biology, 2015. 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, 34 citations in OpenAlex.
- Compositionally Biased Regions Within Structured Protein Domains.Biomolecules · 2026Article
- Article
- How Big Is the Yeast Prion Universe?International journal of molecular sciences · 2023Review
- Article
- The Hunt for Ancient Prions: Archaeal Prion-Like Domains Form Amyloid-Based Epigenetic Elements.Molecular biology and evolution · 2021Article
- From Prions to Stress Granules: Defining the Compositional Features of Prion-Like Domains That Promote Different Types of Assemblies.International journal of molecular sciences · 2021Review
- Sky1: at the intersection of prion-like proteins and stress granule regulation.Current genetics · 2020Review
- Natural and pathogenic protein sequence variation affecting prion-like domains within and across human proteomes.BMC genomics · 2020Article
- Article
- Aggregation and degradation scales for prion-like domains: sequence features and context weigh in.Current genetics · 2019Review
- Conservation of Prion-Like Composition and Sequence in Prion-Formers and Prion-Like Proteins ofFrontiers in molecular biosciences · 2019Article
- Sequence features governing aggregation or degradation of prion-like proteins.PLoS genetics · 2018Article
- Chaperone functional specificity promotes yeast prion diversity.PLoS pathogens · 2018Article
- PrP P102L and Nearby Lysine Mutations Promote SpontaneousJournal of virology · 2017Article
- Article
- Article
- Epigenetic inheritance, prions and evolution.Journal of genetics · 2017Review
- 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
- Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo.PLoS genetics · 2016Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Multiple yeast prions have been identified that result from the structural conversion of proteins into a self-propagating amyloid form. Amyloid-based prion activity in yeast requires a series of discrete steps. First, the prion protein must form an amyloid nucleus that can recruit and structurally convert additional soluble proteins. Subsequently, maintenance of the prion during cell division requires fragmentation of these aggregates to create new heritable propagons. For the Saccharomyces cerevisiae prion protein Sup35, these different activities are encoded by different regions of the Sup35 prion domain. An N-terminal glutamine/asparagine-rich nucleation domain is required for nucleation and fiber growth, while an adjacent oligopeptide repeat domain is largely dispensable for prion nucleation and fiber growth but is required for chaperone-dependent prion maintenance. Although prion activity of glutamine/asparagine-rich proteins is predominantly determined by amino acid composition, the nucleation and oligopeptide repeat domains of Sup35 have distinct compositional requirements. Here, we quantitatively define these compositional requirements in vivo. We show that aromatic residues strongly promote both prion formation and chaperone-dependent prion maintenance. In contrast, nonaromatic hydrophobic residues strongly promote prion formation but inhibit prion propagation. These results provide insight into why some aggregation-prone proteins are unable to propagate as prions.
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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.