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Characterization of soft amyloid cores in human prion-like proteins
- Source :
- Recercat. Dipósit de la Recerca de Catalunya, instname, Scientific Reports, Dipòsit Digital de Documents de la UAB, Universitat Autònoma de Barcelona, Scientific Reports, Vol 7, Iss 1, Pp 1-16 (2017)
- Publication Year :
- 2017
- Publisher :
- Nature Publishing Group, 2017.
-
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. 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.]
- Subjects :
- 0301 basic medicine
Amyloid
Prions
Protein domain
lcsh:Medicine
Computational biology
Biology
Protein aggregation
Bioinformatics
Prion Proteins
Article
DEAD-box RNA Helicases
Fungal Proteins
Nuclear Receptor Coactivator 2
Protein Aggregates
03 medical and health sciences
Protein Domains
Transcription (biology)
Yeasts
Translational regulation
medicine
Humans
Amino Acid Sequence
Prion protein
lcsh:Science
Databases, Protein
Nuclear Factor 90 Proteins
Peptide sequence
Polycomb Repressive Complex 1
Mediator Complex
Multidisciplinary
030102 biochemistry & molecular biology
lcsh:R
Neurodegeneration
Intracellular Signaling Peptides and Proteins
Nuclear Proteins
medicine.disease
Yeast
T-Cell Intracellular Antigen-1
Intrinsically Disordered Proteins
030104 developmental biology
Solubility
lcsh:Q
Protein Tyrosine Phosphatases
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- Recercat. Dipósit de la Recerca de Catalunya, instname, Scientific Reports, Dipòsit Digital de Documents de la UAB, Universitat Autònoma de Barcelona, Scientific Reports, Vol 7, Iss 1, Pp 1-16 (2017)
- Accession number :
- edsair.doi.dedup.....72b4cfd25a4f63b2c66651df707e4c3a