Please use this identifier to cite or link to this item:
http://hdl.handle.net/2445/134884
Title: | Discovering Putative Prion-Like Proteins in Plasmodium falciparum: A Computational and Experimental Analysis |
Author: | Pallarès, Irantzu Groot, Natalia S. de Iglesias, Valentín Sant'Anna, Ricardo Biosca, Arnau Fernàndez Busquets, Xavier Ventura, Salvador |
Keywords: | Plasmodium falciparum Prions Mètodes experimentals Experimental methods |
Issue Date: | 7-Aug-2018 |
Publisher: | 108258 - Frontiers Media - N |
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. |
Note: | Reproducció del document publicat a: http://dx.doi.org/10.3389/fmicb.2018.01737 |
It is part of: | Frontiers in Microbiology, 2018, vol. 9 |
URI: | http://hdl.handle.net/2445/134884 |
Related resource: | http://dx.doi.org/10.3389/fmicb.2018.01737 |
ISSN: | 1664-302X |
Appears in Collections: | Articles publicats en revistes (ISGlobal) |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
PallaresI_Front_Microbiol_2018.pdf | 5.25 MB | Adobe PDF | View/Open |
This item is licensed under a Creative Commons License