Yeast prions form infectious amyloid inclusion bodies in bacteria

Microbial Cell Factories

Research

Anna Villar-Piqué¹  Raimon Sabaté²  Alba Espargaró³  Salvador Ventura⁴ 

[1]Departament de Bioquímica i Biologia Molecular, Facultat de Ciències, Universitat Autònoma de Barcelona, E-08193, Bellaterra, Spain

[2]Departament de Fisicoquímica, Facultat de Farmàcia, Universitat de Barcelona, Avda. Joan XXIII s/n, E-08193, Bellaterra, Spain

[3]Institut de Nanociència i Nanotecnologia (IN2UB), Barcelona, Spain

[4]Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, E-08193, Bellaterra, Spain

[5]Institut de Biotecnologia i de Biomedicina, Universitat Autònoma de Barcelona, E-08193, Bellaterra, Spain

[6]Departament de Bioquímica i Biologia Molecular, Facultat de Ciències, Universitat Autònoma de Barcelona, E-08193, Bellaterra, Spain

关键词: Protein aggregation;    Inclusion bodies;    Prions;    Sup35-NM;    Ure2p;    Amyloid fibrils;    E. coli;   

DOI  :  10.1186/1475-2859-11-89

 received in 2012-02-05, accepted in 2012-05-27,  发布年份 2012

来源: Springer

【 摘 要 】

BackgroundPrions were first identified as infectious proteins associated with fatal brain diseases in mammals. However, fungal prions behave as epigenetic regulators that can alter a range of cellular processes. These proteins propagate as self-perpetuating amyloid aggregates being an example of structural inheritance. The best-characterized examples are the Sup35 and Ure2 yeast proteins, corresponding to [PSI+] and [URE3] phenotypes, respectively.ResultsHere we show that both the prion domain of Sup35 (Sup35-NM) and the Ure2 protein (Ure2p) form inclusion bodies (IBs) displaying amyloid-like properties when expressed in bacteria. These intracellular aggregates template the conformational change and promote the aggregation of homologous, but not heterologous, soluble prionogenic molecules. Moreover, in the case of Sup35-NM, purified IBs are able to induce different [PSI+] phenotypes in yeast, indicating that at least a fraction of the protein embedded in these deposits adopts an infectious prion fold.ConclusionsAn important feature of prion inheritance is the existence of strains, which are phenotypic variants encoded by different conformations of the same polypeptide. We show here that the proportion of infected yeast cells displaying strong and weak [PSI+] phenotypes depends on the conditions under which the prionogenic aggregates are formed in E. coli, suggesting that bacterial systems might become useful tools to generate prion strain diversity.

【 授权许可】

Unknown   
© Espargaró et al.; licensee BioMed Central Ltd. 2012. This article is published under license to BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.