Document Type
Article
Language
eng
Publication Date
2017
Publisher
Taylor & Francis
Source Publication
Prion
Source ISSN
1933-6896
Abstract
Prions are misfolded, aggregated, infectious proteins found in a range of organisms from mammals to bacteria. In mammals, prion formation is difficult to study because misfolding and aggregation take place prior to symptom presentation. The study of the yeast prion [PSI+], which is the misfolded infectious form of Sup35p, provides a tractable system to monitor prion formation in real time. Recently, we showed that the de novo formation of prion aggregates begins with the appearance of highly mobile cytoplasmic foci, called early foci, which assemble into larger ring or dot structures. We also observed SDS-resistant oligomers during formation, and lysates containing newly formed oligomers can convert [psi−] cells to the [PSI+] state, suggesting that these oligomers have infectious potential. Here, we further characterize two aspects of prion formation: spatial sequestration of early foci and oligomerization of endogenous Sup35p. Our data provides important insights into the process of prion formation and explores the minimal oligomer requirement for infectivity.
Creative Commons License
This work is licensed under a Creative Commons Attribution-NonCommercial-No Derivative Works 4.0 International License.
Recommended Citation
Lyke, Douglas and Manogaran, Anita L., "Spatial Sequestration and Oligomer Remodeling During de novo [PSI+] Formation" (2017). Biological Sciences Faculty Research and Publications. 607.
https://epublications.marquette.edu/bio_fac/607
Comments
Published version. Prion, Vol. 11, No. 5 (2017): 332-337. DOI. © 2017 The Author(s). Published with license by Taylor & Francis Group, LLC© Douglas R. Lyke and Anita L. Manogaran.
This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non- Commercial-No-Derivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.