Characterization of soft amyloid cores in human prion-like proteins
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- dc.contributor.author Batlle, Cristinaca
- dc.contributor.author Sanchez de Groot, Nataliaca
- dc.contributor.author Iglesias, Valentinca
- dc.contributor.author Navarro, Susannaca
- dc.contributor.author Ventura, Salvadorca
- dc.date.accessioned 2018-07-16T08:17:03Z
- dc.date.available 2018-07-16T08:17:03Z
- dc.date.issued 2017
- dc.description.abstract Prion-like behaviour is attracting much attention due to the growing evidences that amyloid-like self-assembly may reach beyond neurodegeneration and be a conserved functional mechanism. The best characterized functional prions correspond to a subset of yeast proteins involved in translation or transcription. Their conformational promiscuity is encoded in Prion Forming Domains (PFDs), usually long and intrinsically disordered protein segments of low complexity. The compositional bias of these regions seems to be important for the transition between soluble and amyloid-like states. We have proposed that the presence of cryptic soft amyloid cores embedded in yeast PFDs can also be important for their assembly and demonstrated their existence and self-propagating abilities. Here, we used an orthogonal approach in the search of human domains that share yeast PFDs compositional bias and exhibit a predicted nucleating core, identifying 535 prion-like candidates. We selected seven proteins involved in transcriptional or translational regulation and associated to disease to characterize the properties of their amyloid cores. All of them self-assemble spontaneously into amyloid-like structures able to propagate their polymeric state. This provides support for the presence of short sequences able to trigger conformational conversion in prion-like human proteins, potentially regulating their functionality.
- dc.description.sponsorship This work was funded supported by the Spanish Ministry of Economy and Competitiveness [BIO2016-783-78310-R to S.V] and by ICREA [ICREA-Academia 2015 to S.V.]
- dc.format.mimetype application/pdf
- dc.identifier.citation Batlle C, de Groot NS, Iglesias V, Navarro S, Ventura S. Characterization of Soft Amyloid Cores in Human Prion-Like Proteins. Sci Rep. 2017 Sep 21;7(1):12134. DOI: 10.1038/s41598-017-09714-z
- dc.identifier.doi http://dx.doi.org/10.1038/s41598-017-09714-z
- dc.identifier.issn 2045-2322
- dc.identifier.uri http://hdl.handle.net/10230/35160
- dc.language.iso eng
- dc.publisher Nature Publishing Groupca
- dc.relation.ispartof Scientific Reports. 2017 Sep 21;7(1):12134
- dc.relation.projectID info:eu-repo/grantAgreement/ES/1PE/BIO2016-783-78310-R
- dc.rights © The Author(s) 2017. Open Access. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
- dc.rights.accessRights info:eu-repo/semantics/openAccess
- dc.rights.uri http://creativecommons.org/licenses/by/4.0/
- dc.subject.keyword Prions
- dc.subject.keyword Protein aggregation
- dc.title Characterization of soft amyloid cores in human prion-like proteinsca
- dc.type info:eu-repo/semantics/article
- dc.type.version info:eu-repo/semantics/publishedVersion