Peptide sequences converting polyglutamine into a prion in yeast

Wataru Odani, Kazuhiro Urata, Momoko Okuda, Shunsuke Okuma, Hiroko Koyama, Chan Gi Pack, Kei Fujiwara, Tatsuya Nojima, Masataka Kinjo, Shigeko Kawai-Noma, Hideki Taguchi

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish
Pages (from-to)477-490
Number of pages14
JournalFEBS Journal
Issue number3
Publication statusPublished - 2015 Feb


  • Amyloids
  • Fluorescence correlation spectroscopy
  • Polyglutamine
  • Sup35
  • Yeast prions

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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