Fernandez-Bellot, E. and Guillemet, E. and Ness, F. and Baudin-Baillieu, A. and Ripaud, L. and Tuite, M.F. and Cullin, C. (2002) The [URE3] phenotype: evidence for a soluble prion in yeast. EMBO Reports, 3 (1). pp. 76-81. ISSN 1469-221X.
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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.
|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:||Faculties > Science Technology and Medical Studies > School of Biosciences > Protein Science Group|
|Depositing User:||Mick Tuite|
|Date Deposited:||09 Sep 2008 16:56|
|Last Modified:||14 Jan 2010 14:20|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/5468 (The current URI for this page, for reference purposes)|
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