ArticleThe Journal of biological chemistry2008
Appearance and propagation of polyglutamine-based amyloids in yeast: tyrosine residues enable polymer fragmentation.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 54 citations in OpenAlex.
- Article
- Article
- Amyloid Fragmentation and Disaggregation in Yeast and Animals.Biomolecules · 2021Review
- Huntingtin Polyglutamine Fragments Are a Substrate for Hsp104 in Saccharomyces cerevisiae.Molecular and cellular biology · 2021Article
- Periphilin self-association underpins epigenetic silencing by the HUSH complex.Nucleic acids research · 2020Article
- Short disordered protein segment regulates cross-species transmission of a yeast prion.Nature chemical biology · 2020Article
- Article
- [PIN+]ing down the mechanism of prion appearance.FEMS yeast research · 2018Review
- Chaperone functional specificity promotes yeast prion diversity.PLoS pathogens · 2018Article
- Distinct Prion Domain Sequences Ensure Efficient Amyloid Propagation by Promoting Chaperone Binding or Processing In Vivo.PLoS genetics · 2016Article
- A protein polymerization cascade mediates toxicity of non-pathological human huntingtin in yeast.Scientific reports · 2015Article
- Distinct amino acid compositional requirements for formation and maintenance of the [PSI⁺] prion in yeast.Molecular and cellular biology · 2015Article
- Increasing prion propensity by hydrophobic insertion.PloS one · 2014Article
- Exploring the basis of [PIN(+)] variant differences in [PSI(+)] induction.Journal of molecular biology · 2013Article
- De novo design of synthetic prion domains.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- The effects of amino acid composition of glutamine-rich domains on amyloid formation and fragmentation.PloS one · 2012Article
- Genomic clustering and homology between HET-S and the NWD2 STAND protein in various fungal genomes.PloS one · 2012Article
- Article
- Amyloid-mediated sequestration of essential proteins contributes to mutant huntingtin toxicity in yeast.PloS one · 2012Article
- Molecular basis for transmission barrier and interference between closely related prion proteins in yeast.The Journal of biological chemistry · 2011Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
In yeast, fragmentation of amyloid polymers by the Hsp104 chaperone allows them to propagate as prions. The prion-forming domain of the yeast Sup35 protein is rich in glutamine, asparagine, tyrosine, and glycine residues, which may define its prion properties. Long polyglutamine stretches can also drive amyloid polymerization in yeast, but these polymers are unable to propagate because of poor fragmentation and exist through constant seeding with the Rnq1 prion polymers. We proposed that fragmentation of polyglutamine amyloids may be improved by incorporation of hydrophobic amino acid residues into polyglutamine stretches. To investigate this, we constructed sets of polyglutamine with or without tyrosine stretches fused to the non-prion domains of Sup35. Polymerization of these chimeras started rapidly, and its efficiency increased with stretch size. Polymerization of proteins with polyglutamine stretches shorter than 70 residues required Rnq1 prion seeds. Proteins with longer stretches polymerized independently of Rnq1 and thus could propagate. The presence of tyrosines within polyglutamine stretches dramatically enhanced polymer fragmentation and allowed polymer propagation in the absence of Rnq1 and, in some cases, of Hsp104.
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