Analysis of Yeast Prion Aggregates with Amyloid-staining Compound In Vivo

Cell Structure and Function

Sumiko Koitabashi²  Takashi Fujita²  Yoko Kimura¹ 

[1] Laboratory of Frontier Science;Department of Tumor Cell Biology Tokyo Metropolitan Institute of Medical Science

关键词: yeast;    prion;    amyloid;    thioflavin-S;    Hsp104;   

DOI  :  10.1247/csf.28.187

学科分类：分子生物学，细胞生物学和基因

来源: Japan Society for Cell Biology

【 摘 要 】

References(37)Cited-By(17)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.

【 授权许可】

Unknown