Jossé, Lyne and Marchante, Ricardo and Zenthon, Jo and von der Haar, Tobias and Tuite, Mick F. (2012) Probing the role of structural features of mouse PrP in yeast by expression as Sup35-PrP fusions. Prion, 6 (3). pp. 201-210. ISSN 1933-6896. (doi:https://doi.org/10.4161/pri.19214) (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)
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The yeast Saccharomyces cerevisiae is a tractable model organism in which both to explore the molecular mechanisms underlying the generation of disease-associated protein misfolding and to map the cellular responses to potentially toxic misfolded proteins. Specific targets have included proteins which in certain disease states form amyloids and lead to neurodegeneration. Such studies are greatly facilitated by the extensive ‘toolbox’ available to the yeast researcher that provides a range of cell engineering options. Consequently, a number of assays at the cell and molecular level have been set up to report on specific protein misfolding events associated with endogenous or heterologous proteins. One major target is the mammalian prion protein PrP because we know little about what specific sequence and/or structural feature(s) of PrP are important for its conversion to the infectious prion form, PrPSc. Here, using a study of the expression in yeast of fusion proteins comprising the yeast prion protein Sup35 fused to various regions of mouse PrP protein, we show how PrP sequences can direct the formation of non-transmissible amyloids and focus in particular on the role of the mouse octarepeat region. Through this study we illustrate the benefits and limitations of yeast-based models for protein misfolding disorders.
|Divisions:||Faculties > Sciences > School of Biosciences|
|Depositing User:||Sue Davies|
|Date Deposited:||23 Aug 2012 13:53 UTC|
|Last Modified:||07 Apr 2014 10:18 UTC|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/30230 (The current URI for this page, for reference purposes)|