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Yeast prions form infectious amyloid inclusion bodies in bacteria
Espargaró Colomé, Alba (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")
Ventura i Zamora, Salvador (Institut de Biotecnologia i de Biomedicina "Vicent Villar Palasí")

Data: 2012
Resum: Background: Prions 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. Results: Here 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. Conclusions: An 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.
Drets: Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial i la comunicació pública de l'obra, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original. No es permet la creació d'obres derivades. Creative Commons
Llengua: Anglès
Document: article ; publishedVersion
Matèria: Protein aggregation ; Inclusion bodies ; Prions ; Sup35-NM ; Ure2p ; Amyloid fibrils ; E. coli
Publicat a: Microbial cell factories, Vol. 11, N. 89 (June 2012) , p. 1-12, ISSN 1475-2859

DOI: 10.1186/1475-2859-11-89
PMID: 22731490

12 p, 2.5 MB

Additional file 1
1 p, 111.7 KB

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