Avui, dijous 7 de maig, el Dipòsit Digital no estarà operatiu per tasques d'actualització. Disculpeu les molèsties.
Hoy, jueves 7 de mayo, el Dipòsit Digital no estará operativo debido a tareas de actualización. Disculpen las molestias.
Today, Thursday, May 7th, the Digital Repository will be unavailable due to a system update.

Fitxers

642560.pdf (2.42 MB)

Tipus de document

Article

Versió

Versió publicada

Data de publicació

2012-06-25

Tots els drets reservats

Si us plau utilitzeu sempre aquest identificador per citar o enllaçar aquest document: https://hdl.handle.net/2445/191002

Yeast prions form infectious amyloid inclusion bodies in bacteria

Títol de la revista

Autors

Director/Tutor

ISSN de la revista

Títol del volum

Recurs relacionat

https://doi.org/10.1186/1475-2859-11-89

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.

Matèries

Prions, Bacteris, Proteïnes

Matèries (anglès)

Prions, Bacteria, Proteins

Citació

Col·leccions

Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica)

Citació

ESPARGARÓ COLOMÉ, Alba, et al. Yeast prions form infectious amyloid inclusion bodies in bacteria. Microbial Cell Factories. 2012. Vol. 11, núm. 89. ISSN 1475-2859. [consulta: 8 de maig de 2026]. Disponible a: https://hdl.handle.net/2445/191002

Exportar metadades

JSON - METS

Compartir registre