Affiliation:
1. Department of Chemical and Systems Biology, Stanford University, Stanford, CA 94305, USA
2. Department of Developmental Biology, Stanford University, Stanford, CA 94305, USA
Abstract
Protein aggregation, particularly in its prion-like form, has long been thought to be detrimental. However, recent studies have identified multiple instances where protein aggregation is important for normal physiological functions. Combining mass spectrometry and cell biological approaches, we developed a strategy for the identification of protein aggregates in cell lysates. We used this approach to characterize prion-based traits in pathogenic strains of the yeast
Saccharomyces cerevisiae
isolated from immunocompromised human patients. The proteins that we found, including the metabolic enzyme Cdc19, the translation elongation factor Yef3 and the fibrillarin homologue Nop1, are known to assemble under certain physiological conditions. Yet, such assemblies have not been reported to be stable or heritable. Our data suggest that some proteins which aggregate in response to stress have the capacity to acquire diverse assembled states, certain ones of which can be propagated across generations in a form of protein-based epigenetics.
This article is part of the theme issue ‘How does epigenetics influence the course of evolution?’
Funder
Zaffaroni Foundation
David and Lucile Packard Foundation
Vallee Foundation
Alzheimer's Disease Research Center, Stanford University
Glenn Foundation for Medical Research
National Science Foundation
National Institutes of Health
Subject
General Agricultural and Biological Sciences,General Biochemistry, Genetics and Molecular Biology
Cited by
3 articles.
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