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 journalArticle

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.

Original languageEnglish
Pages (from-to)477-490
Number of pages14
JournalFEBS Journal
Volume282
Issue number3
DOIs
Publication statusPublished - 2015

Fingerprint

Prions
Yeast
Amyloid
Yeasts
Peptides
Neurodegenerative diseases
Amyloidogenic Proteins
Prion Diseases
Neurodegenerative Diseases
polyglutamine
Alzheimer Disease
Cells
Proteins

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology
  • Medicine(all)

Cite this

Odani, W., Urata, K., Okuda, M., Okuma, S., Koyama, H., Pack, C. G., ... Taguchi, H. (2015). Peptide sequences converting polyglutamine into a prion in yeast. FEBS Journal, 282(3), 477-490. https://doi.org/10.1111/febs.13152

Peptide sequences converting polyglutamine into a prion in yeast. / Odani, Wataru; Urata, Kazuhiro; Okuda, Momoko; Okuma, Shunsuke; Koyama, Hiroko; Pack, Chan Gi; Fujiwara, Kei; Nojima, Tatsuya; Kinjo, Masataka; Kawai-Noma, Shigeko; Taguchi, Hideki.

In: FEBS Journal, Vol. 282, No. 3, 2015, p. 477-490.

Research output: Contribution to journalArticle

Odani, W, Urata, K, Okuda, M, Okuma, S, Koyama, H, Pack, CG, Fujiwara, K, Nojima, T, Kinjo, M, Kawai-Noma, S & Taguchi, H 2015, 'Peptide sequences converting polyglutamine into a prion in yeast', FEBS Journal, vol. 282, no. 3, pp. 477-490. https://doi.org/10.1111/febs.13152
Odani W, Urata K, Okuda M, Okuma S, Koyama H, Pack CG et al. Peptide sequences converting polyglutamine into a prion in yeast. FEBS Journal. 2015;282(3):477-490. https://doi.org/10.1111/febs.13152
Odani, Wataru ; Urata, Kazuhiro ; Okuda, Momoko ; Okuma, Shunsuke ; Koyama, Hiroko ; Pack, Chan Gi ; Fujiwara, Kei ; Nojima, Tatsuya ; Kinjo, Masataka ; Kawai-Noma, Shigeko ; Taguchi, Hideki. / Peptide sequences converting polyglutamine into a prion in yeast. In: FEBS Journal. 2015 ; Vol. 282, No. 3. pp. 477-490.
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