Amyloid oligomers: diffuse oligomer-based transmission of yeast prions.
Prions are infectious proteins, in which self-propagating amyloid conformations of proteins are transmitted. The budding yeast Saccharomyces cerevisiae, one of the best-studied model eukaryotes, also has prions, and thus provides a tractable model system with which to understand the mechanisms of prion phenomena. The yeast prions are protein-based heritable elements, such as [PSI(+)], in which aggregates of prion proteins are transmitted to daughter cells in a non-Mendelian manner. Although the genetic approaches preceded the yeast prion studies, recent investigations of the dynamic aspects of the prion proteins have unraveled the molecular mechanisms by which prions are propagated and transmitted. In particular, several lines of evidence have revealed that the oligomeric species of prion proteins dispersed in the cytoplasm are critical for the transmission. This review summarizes the topics on the transmissible entities of yeast prions, focusing mainly on the Sup35 protein in [PSI(+)].
Department of Medical Genome Sciences, Graduate School of Frontier Sciences, University of Tokyo, Kashiwanoha, Kashiwa, Chiba, Japan. taguchi@k.u-tokyo.ac.jp
Hideki
H
Taguchi
Shigeko
S
Kawai-Noma
D000682:Amyloid / Q000648:ultrastructure*; D000818:Animals; D006801:Humans; D008954:Models, Biological; D046912:Multiprotein Complexes / Q000648:ultrastructure; D010454:Peptide Termination Factors / Q000502:physiology* / Q000648:ultrastructure; D011328:Prions / Q000502:physiology* / Q000648:ultrastructure; D029701:Saccharomyces cerevisiae Proteins / Q000502:physiology* / Q000648:ultrastructure
D000682:Amyloid; D046912:Multiprotein Complexes; D010454:Peptide Termination Factors; D011328:Prions; C068068:SUP35 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins