Home >

news Help

Publication Information


Title
Japanese:Peptide sequences converting polyglutamine into a prion in yeast. 
English:Peptide sequences converting polyglutamine into a prion in yeast. 
Author
Japanese: Wataru Odani, Kazuhiro Urata, 奥田桃子, Shunsuke Okuma, Hiroko Koyama, Chan-Gi Pack, Kei Fujiwara, 野島達也, 金城 政孝, 河合 繁子, 田口英樹.  
English: Wataru Odani, Kazuhiro Urata, Momoko Okuda, Shunsuke Okuma, Hiroko Koyama, Chan-Gi Pack, Kei Fujiwara, Nojima Tatsuya, Masataka KINJO, Shigeko Kawai-Noma, HIDEKI TAGUCHI.  
Language English 
Journal/Book name
Japanese:FEBS Journal 
English:FEBS Journal 
Volume, Number, Page Volume 282        page 477-490
Published date Feb. 2015 
Publisher
Japanese: 
English: 
Conference name
Japanese: 
English: 
Conference site
Japanese: 
English: 
DOI https://doi.org/10.1111/febs.13152
Abstract Amyloids are ordered protein aggregates composed of cross-β sheet structures. Amyloids include prions, defined as infectious proteins, which are responsible for mammalian transmissible spongiform encephalopathies, and fungal prions. Although the conventional view is that typical amyloids are associated with nontransmissible mammalian neurodegenerative diseases such as Alzheimer's disease, increasing evidence suggests that the boundary between transmissible and nontransmissible amyloids is ambiguous. To clarify the mechanism underlying the difference in transmissibility, we investigated the dynamics and the properties of polyglutamine (polyQ) amyloids in yeast cells, in which the polyQ aggregates are not transmissible but can be converted into transmissible amyloids. We found that polyQ had an increased tendency to form aggregates compared to the yeast prion Sup35. In addition, we screened dozens of peptides that converted the nontransmissible polyQ to transmissible aggregates when they flanked the polyQ stretch, and also investigated their cellular dynamics aiming to understand the mechanism of transmission.

©2007 Tokyo Institute of Technology All rights reserved.