Use of yeast as a system to study amyloid toxicity.
The formation of amyloid-like fibrils is a hallmark of several neurodegenerative diseases. How the assembly of amyloid-like fibrils contributes to cell death is a major unresolved question in the field. The budding yeast Saccharomyces cerevisiae is a powerful model organism to study basic mechanisms for how cellular pathways regulate amyloid assembly and proteotoxicity. For example, studies of the amyloidogenic yeast prion [RNQ(+)] have revealed novel roles by which molecular chaperones protect cells from the accumulation of cytotoxic protein species. In budding yeast there are a variety of cellular assays that can be employed to analyze the assembly of amyloid-like aggregates and mechanistically dissect how cellular pathways influence proteotoxicity. In this review, we describe several assays that are routinely used to investigate aggregation and toxicity of the [RNQ(+)] prion in yeast.
Department of Cell and Developmental Biology, University of North Carolina at Chapel Hill, 526 Taylor Hall CB# 7090, Chapel Hill, NC 27514, USA. daniel_summers@med.unc.edu
Daniel W
DW
Summers
Douglas M
DM
Cyr
D000682:Amyloid / Q000096:biosynthesis*; D052160:Benzothiazoles; D002498:Centrifugation; D002850:Chromatography, Gel; D004587:Electrophoresis, Agar Gel; D050296:Microbial Viability; D008856:Microscopy, Fluorescence; D019636:Neurodegenerative Diseases / Q000473:pathology; D030781:Organisms, Genetically Modified; D011328:Prions / Q000096:biosynthesis*; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000254:growth & development / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000096:biosynthesis*; D013194:Staining and Labeling; D013844:Thiazoles
D000682:Amyloid; D052160:Benzothiazoles; D011328:Prions; C404807:RNQ1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D013844:Thiazoles; C009462:thioflavin T