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Peptide sequences converting polyglutamine into a prion in yeast
Author(s) -
Odani Wataru,
Urata Kazuhiro,
Okuda Momoko,
Okuma Shunsuke,
Koyama Hiroko,
Pack ChanGi,
Fujiwara Kei,
Nojima Tatsuya,
Kinjo Masataka,
KawaiNoma Shigeko,
Taguchi Hideki
Publication year - 2015
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/febs.13152
Subject(s) - yeast , prion protein , protein aggregation , amyloid (mycology) , biology , mechanism (biology) , fungal prion , microbiology and biotechnology , chemistry , saccharomyces cerevisiae , biochemistry , virology , disease , medicine , philosophy , botany , epistemology , pathology
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.