Analysis of yeast prion aggregates with amyloid-staining compound in vivo.
Yeast prions are protein-based genetic elements whose non-Mendelian patterns of inheritance are explained by their inheritance of altered conformations. Here we showed that aggregates made by overexpression of two different prion domains of Sup35 and Rnq1, were stained in yeast by thioflavin-S, an amyloid binding compound. These results suggested that yeast prion domains take the form of amyloid in vivo, and supported the idea that the self-propagating property of amyloids is responsible for the heritable traits of yeast prions.
Kimura
Yoko
Y
Laboratory of Frontier Science, Tokyo Metropolitan Institute of Medical Science, Honkomagome, Bunkyo, Tokyo 113-8613, Japan. ykimura@rinshoken.or.jp
Koitabashi
Sumiko
S
Fujita
Takashi
T
D000682:Amyloid / Q000378:metabolism*; D052160:Benzothiazoles; D005456:Fluorescent Dyes / Q000378:metabolism; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D007150:Immunohistochemistry; D010454:Peptide Termination Factors; D011328:Prions / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013844:Thiazoles / Q000378:metabolism
D000682:Amyloid; D052160:Benzothiazoles; D005456:Fluorescent Dyes; D005656:Fungal Proteins; D010454:Peptide Termination Factors; D011328:Prions; C404807:RNQ1 protein, S cerevisiae; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D013844:Thiazoles; C009462:thioflavin T