Yeast prions form infectious amyloid inclusion bodies in bacteria
<p>Abstract</p> <p>Background</p> <p>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 sel...
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| Format: | Article |
| Language: | English |
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BMC
2012-06-01
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| Series: | Microbial Cell Factories |
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| Online Access: | http://www.microbialcellfactories.com/content/11/1/89 |
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| author | Espargaró Alba Villar-Piqué Anna Sabaté Raimon Ventura Salvador |
| author_facet | Espargaró Alba Villar-Piqué Anna Sabaté Raimon Ventura Salvador |
| author_sort | Espargaró Alba |
| collection | DOAJ |
| description | <p>Abstract</p> <p>Background</p> <p>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 [<it>PSI+</it>] and [<it>URE3</it>] phenotypes, respectively.</p> <p>Results</p> <p>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 [<it>PSI+</it>] phenotypes in yeast, indicating that at least a fraction of the protein embedded in these deposits adopts an infectious prion fold.</p> <p>Conclusions</p> <p>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 [<it>PSI+</it>] phenotypes depends on the conditions under which the prionogenic aggregates are formed in <it>E. coli</it>, suggesting that bacterial systems might become useful tools to generate prion strain diversity.</p> |
| first_indexed | 2024-12-17T05:25:14Z |
| format | Article |
| id | doaj.art-3d570a28d20741e2b69c1846e8a2b3f0 |
| institution | Directory Open Access Journal |
| issn | 1475-2859 |
| language | English |
| last_indexed | 2024-12-17T05:25:14Z |
| publishDate | 2012-06-01 |
| publisher | BMC |
| record_format | Article |
| series | Microbial Cell Factories |
| spelling | doaj.art-3d570a28d20741e2b69c1846e8a2b3f02022-12-21T22:01:52ZengBMCMicrobial Cell Factories1475-28592012-06-011118910.1186/1475-2859-11-89Yeast prions form infectious amyloid inclusion bodies in bacteriaEspargaró AlbaVillar-Piqué AnnaSabaté RaimonVentura Salvador<p>Abstract</p> <p>Background</p> <p>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 [<it>PSI+</it>] and [<it>URE3</it>] phenotypes, respectively.</p> <p>Results</p> <p>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 [<it>PSI+</it>] phenotypes in yeast, indicating that at least a fraction of the protein embedded in these deposits adopts an infectious prion fold.</p> <p>Conclusions</p> <p>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 [<it>PSI+</it>] phenotypes depends on the conditions under which the prionogenic aggregates are formed in <it>E. coli</it>, suggesting that bacterial systems might become useful tools to generate prion strain diversity.</p>http://www.microbialcellfactories.com/content/11/1/89Protein aggregationInclusion bodiesPrionsSup35-NMUre2pAmyloid fibrils<it>E. coli</it> |
| spellingShingle | Espargaró Alba Villar-Piqué Anna Sabaté Raimon Ventura Salvador Yeast prions form infectious amyloid inclusion bodies in bacteria Microbial Cell Factories Protein aggregation Inclusion bodies Prions Sup35-NM Ure2p Amyloid fibrils <it>E. coli</it> |
| title | Yeast prions form infectious amyloid inclusion bodies in bacteria |
| title_full | Yeast prions form infectious amyloid inclusion bodies in bacteria |
| title_fullStr | Yeast prions form infectious amyloid inclusion bodies in bacteria |
| title_full_unstemmed | Yeast prions form infectious amyloid inclusion bodies in bacteria |
| title_short | Yeast prions form infectious amyloid inclusion bodies in bacteria |
| title_sort | yeast prions form infectious amyloid inclusion bodies in bacteria |
| topic | Protein aggregation Inclusion bodies Prions Sup35-NM Ure2p Amyloid fibrils <it>E. coli</it> |
| url | http://www.microbialcellfactories.com/content/11/1/89 |
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