Interdependence of amyloid formation in yeast: Implications for polyglutamine disorders and biological functions

In eukaryotic cells amyloid aggregates may incorporate various functionally unrelated proteins. In mammalian diseases this may cause amyloid toxicity, while in yeast this could contribute to prion phenotypes. Insolubility of amyloids in the presence of strong ionic detergents, such as SDS or sarcosy...

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Bibliographic Details
Published in:Prion 2010-01, Vol.4 (1), p.45-52
Main Authors: Urakov, Valery N., Vishnevskaya, Aleksandra B., Alexandrov, Ilya M., Kushnirov, Vitaly V., Smirnov, Vladimir N., Ter-Avanesyan, Michael D.
Format: Article
Language:English
Subjects:
Amyloid - genetics
Amyloid - metabolism
Binding
Biology
Bioscience
Calcium
Cancer
Cell
Cycle
Landes
Neurodegenerative Diseases - metabolism
Organogenesis
Peptide Termination Factors - genetics
Peptide Termination Factors - metabolism
Peptides - metabolism
Poly(A)-Binding Proteins - genetics
Poly(A)-Binding Proteins - metabolism
Prions - genetics
Prions - metabolism
Protein Multimerization
Proteins
Research Papers
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
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Summary:In eukaryotic cells amyloid aggregates may incorporate various functionally unrelated proteins. In mammalian diseases this may cause amyloid toxicity, while in yeast this could contribute to prion phenotypes. Insolubility of amyloids in the presence of strong ionic detergents, such as SDS or sarcosyl, allows discrimination between amorphous and amyloid aggregates. Here, we used this property of amyloids to study the interdependence of their formation in yeast. We observed that SDS-resistant polymers of proteins with extended polyglutamine domains caused the appearance of SDS or sarcosyl-insoluble polymers of three tested chromosomally-encoded Q/N-rich proteins, Sup35, Rnq1 and Pub1. These polymers were non-heritable, since they could not propagate in the absence of polyglutamine polymers. Sup35 prion polymers caused the appearance of non-heritable sarcosyl-resistant polymers of Pub1. Since eukaryotic genomes encode hundreds of proteins with long Q/N-rich regions, polymer interdependence suggests that conversion of a single protein into polymer form may significantly affect cell physiology by causing partial transfer of other Q/N-rich proteins into a non-functional polymer state.
ISSN:1933-6896
1933-690X
DOI:10.4161/pri.4.1.11074