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http://hdl.handle.net/2445/106928
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DC Field | Value | Language |
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dc.contributor.author | Daskalov, Asen | - |
dc.contributor.author | Habenstein, Birgi | - |
dc.contributor.author | Martínez, Denis | - |
dc.contributor.author | Debets, Alfons J. M. | - |
dc.contributor.author | Sabaté Lagunas, Raimon | - |
dc.contributor.author | Loquet, Antoine | - |
dc.contributor.author | Saupe, Sven J. | - |
dc.date.accessioned | 2017-02-14T15:57:32Z | - |
dc.date.available | 2017-02-14T15:57:32Z | - |
dc.date.issued | 2015-02-11 | - |
dc.identifier.issn | 1544-9173 | - |
dc.identifier.uri | http://hdl.handle.net/2445/106928 | - |
dc.description.abstract | In the fungus Podospora anserina, the [Het-s] prion induces programmed cell death by activating the HET-S pore-forming protein. The HET-s β-solenoid prion fold serves as a template for converting the HET-S prion-forming domain into the same fold. This conversion, in turn, activates the HET-S pore-forming domain. The gene immediately adjacent to het-S encodes NWD2, a Nod-like receptor (NLR) with an N-terminal motif similar to the elementary repeat unit of the β-solenoid fold. NLRs are immune receptors controlling cell death and host defense processes in animals, plants and fungi. We have proposed that, analogously to [Het-s], NWD2 can activate the HET-S pore-forming protein by converting its prion-forming region into the β-solenoid fold. Here, we analyze the ability of NWD2 to induce formation of the β-solenoid prion fold. We show that artificial NWD2 variants induce formation of the [Het-s] prion, specifically in presence of their cognate ligands. The N-terminal motif is responsible for this prion induction, and mutations predicted to affect the β-solenoid fold abolish templating activity. In vitro, the N-terminal motif assembles into infectious prion amyloids that display a structure resembling the β-solenoid fold. In vivo, the assembled form of the NWD2 N-terminal region activates the HET-S pore-forming protein. This study documenting the role of the β-solenoid fold in fungal NLR function further highlights the general importance of amyloid and prion-like signaling in immunity-related cell fate pathways. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Public Library of Science (PLoS) | - |
dc.relation.isformatof | Reproducció del document publicat a: https://doi.org/10.1371/journal.pbio.1002059 | - |
dc.relation.ispartof | PLoS Biology, 2015, vol. 13, num. 2, p. e1002059 | - |
dc.relation.uri | https://doi.org/10.1371/journal.pbio.1002059 | - |
dc.rights | cc-by (c) Daskalov, Asen et al., 2015 | - |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es | - |
dc.source | Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica) | - |
dc.subject.classification | Proteïnes | - |
dc.subject.classification | Prions | - |
dc.subject.classification | Amiloïdosi | - |
dc.subject.other | Proteins | - |
dc.subject.other | Prions | - |
dc.subject.other | Amyloidosis | - |
dc.title | Signal Transduction by a Fungal NOD-Like Receptor Based on Propagation of a Prion Amyloid Fold | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.identifier.idgrec | 647317 | - |
dc.date.updated | 2017-02-14T15:57:32Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 25671553 | - |
Appears in Collections: | Articles publicats en revistes (Institut de Nanociència i Nanotecnologia (IN2UB)) Articles publicats en revistes (Farmàcia, Tecnologia Farmacèutica i Fisicoquímica) |
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647317.pdf | 3.33 MB | Adobe PDF | View/Open |
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