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http://hdl.handle.net/2445/134884
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DC Field | Value | Language |
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dc.contributor.author | Pallarès, Irantzu | - |
dc.contributor.author | Groot, Natalia S. de | - |
dc.contributor.author | Iglesias, Valentín | - |
dc.contributor.author | Sant'Anna, Ricardo | - |
dc.contributor.author | Biosca, Arnau | - |
dc.contributor.author | Fernàndez Busquets, Xavier | - |
dc.contributor.author | Ventura, Salvador | - |
dc.date.accessioned | 2019-06-12T08:08:45Z | - |
dc.date.available | 2019-06-12T08:08:45Z | - |
dc.date.issued | 2018-08-07 | - |
dc.identifier.issn | 1664-302X | - |
dc.identifier.uri | http://hdl.handle.net/2445/134884 | - |
dc.description.abstract | Prions are a singular subset of proteins able to switch between a soluble conformation and a self-perpetuating amyloid state. Traditionally associated with neurodegenerative diseases, increasing evidence indicates that organisms exploit prion-like mechanisms for beneficial purposes. The ability to transit between conformations is encoded in the so-called prion domains, long disordered regions usually enriched in glutamine/asparagine residues. Interestingly, " - ", the parasite that causes the most virulent form of malaria, is exceptionally rich in proteins bearing long Q/N-rich sequence stretches, accounting for roughly 30% of the proteome. This biased composition suggests that these protein regions might correspond to prion-like domains (PrLDs) and potentially form amyloid assemblies. To investigate this possibility, we performed a stringent computational survey for Q/N-rich PrLDs on " - ". Our data indicate that \xE2\x88\xBC10% of " - " protein sequences have prionic signatures, and that this subproteome is enriched in regulatory proteins, such as transcription factors and RNA-binding proteins. Furthermore, we experimentally demonstrate for several of the identified PrLDs that, despite their disordered nature, they contain inner short sequences able to spontaneously self-assemble into amyloid-like structures. Although the ability of these sequences to nucleate the conformational conversion of the respective full-length proteins should still be demonstrated, our analysis suggests that, as previously described for other organisms, prion-like proteins might also play a functional role in P. falciparum. | - |
dc.format.extent | 13 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | 108258 - Frontiers Media - N | - |
dc.relation.isformatof | Reproducció del document publicat a: http://dx.doi.org/10.3389/fmicb.2018.01737 | - |
dc.relation.ispartof | Frontiers in Microbiology, 2018, vol. 9 | - |
dc.relation.uri | http://dx.doi.org/10.3389/fmicb.2018.01737 | - |
dc.rights | cc by (c) Pallarès et al., 2018 | - |
dc.rights.uri | http://creativecommons.org/licenses/by/3.0/es/ | - |
dc.source | Articles publicats en revistes (ISGlobal) | - |
dc.subject.classification | Plasmodium falciparum | - |
dc.subject.classification | Prions | - |
dc.subject.classification | Mètodes experimentals | - |
dc.subject.other | Experimental methods | - |
dc.title | Discovering Putative Prion-Like Proteins in Plasmodium falciparum: A Computational and Experimental Analysis | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/publishedVersion | - |
dc.date.updated | 2019-05-27T09:01:36Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 30131778 | - |
Appears in Collections: | Articles publicats en revistes (ISGlobal) |
Files in This Item:
File | Description | Size | Format | |
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PallaresI_Front_Microbiol_2018.pdf | 5.25 MB | Adobe PDF | View/Open |
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