Amyloid oligomers: Diffuse oligomer-based transmission of yeast prions

22Citations
Citations of this article
75Readers
Mendeley users who have this article in their library.

This article is free to access.

Abstract

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+]. © 2010 FEBS.

Cite

CITATION STYLE

APA

Taguchi, H., & Kawai-Noma, S. (2010, March). Amyloid oligomers: Diffuse oligomer-based transmission of yeast prions. FEBS Journal. https://doi.org/10.1111/j.1742-4658.2010.07569.x

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free