Pallarès, IrantzuGroot, Natalia S. deIglesias, ValentínSant'Anna, RicardoBiosca, ArnauFernàndez Busquets, XavierVentura, Salvador2019-06-122019-06-122018-08-071664-302Xhttps://hdl.handle.net/2445/134884Prions 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.13 p.application/pdfengcc by (c) Pallarès et al., 2018http://creativecommons.org/licenses/by/3.0/es/Plasmodium falciparumPrionsMètodes experimentalsExperimental methodsinfo:eu-repo/semantics/article2019-05-27info:eu-repo/semantics/openAccess30131778