Fernandez-Bellot, Eric, Guillemet, Elisabeth, Ness, Frederique, Baudin-Baillieu, Agnes, Ripaud, Leslie, Tuite, Mick F., Cullin, Christophe (2002) The [URE3] phenotype: evidence for a soluble prion in yeast. EMBO Reports, 3 (1). pp. 76-81. ISSN 1469-221X. (doi:10.1093/embo-reports/kvf011) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:5468)
The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. | |
Official URL: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=... |
Abstract
The aggregation of the two yeast proteins Sup35p and Ure2p is widely accepted as a model for explaining the prion propagation of the phenotypes [PSI+] and [URE3], respectively. Here, we demonstrate that the propagation of [URE3] cannot simply be the consequence of generating large aggregates of Ure2p, because such aggregation can be found in some conditions that are not related to the prion state of Ure2p. A comparison of [PSI+] and [URE3] aggregation demonstrates differences between these two prion mechanisms. Our findings lead us to propose a new unifying model for yeast prion propagation.
Item Type: | Article |
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DOI/Identification number: | 10.1093/embo-reports/kvf011 |
Additional information: | 1469-221X (Print) Journal Article Research Support, Non-U.S. Gov't |
Uncontrolled keywords: | Amino Acid Sequence Molecular Sequence Data Phenotype Prions/*chemistry/genetics Protein Isoforms/chemistry/genetics Protein Structure, Tertiary Recombinant Fusion Proteins/chemistry/genetics Saccharomyces cerevisiae/*chemistry/genetics Saccharomyces cerevisiae Proteins/*chemistry/genetics Solubility |
Subjects: | Q Science > QR Microbiology |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Michael Tuite |
Date Deposited: | 09 Sep 2008 16:56 UTC |
Last Modified: | 05 Nov 2024 09:37 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/5468 (The current URI for this page, for reference purposes) |
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