| http://purl.uniprot.org/citations/26809710 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/26809710 | http://www.w3.org/2000/01/rdf-schema#comment | "BackgroundPrions are transmissible, propagating alternative states of proteins, and are usually made from the fibrillar, beta-sheet-rich assemblies termed amyloid. Prions in the budding yeast Saccharomyces cerevisiae propagate heritable phenotypes, uncover hidden genetic variation, function in large-scale gene regulation, and can act like diseases. Almost all these amyloid prions have asparagine/glutamine-rich (N/Q-rich) domains. Other proteins, that we term here 'prionogenic amyloid formers' (PAFs), have been shown to form amyloid in vivo, and to have N/Q-rich domains that can propagate heritable states in yeast cells. Also, there are >200 other S.cerevisiae proteins with prion-like N/Q-rich sequence composition. Furthermore, human proteins with such N/Q-rich composition have been linked to the pathomechanisms of neurodegenerative amyloid diseases.ResultsHere, we exploit the increasing abundance of complete fungal genomes to examine the ancestry of prions/PAFs and other N/Q-rich proteins across the fungal kingdom. We find distinct evolutionary behavior for Q-rich and N-rich prions/PAFs; those of ancient ancestry (outside the budding yeasts, Saccharomycetes) are Q-rich, whereas N-rich cases arose early in Saccharomycetes evolution. This emergence of N-rich prion/PAFs is linked to a large-scale emergence of N-rich proteins during Saccharomycetes evolution, with Saccharomycetes showing a distinctive trend for population sizes of prion-like proteins that sets them apart from all the other fungi. Conversely, some clades, e.g. Eurotiales, have much fewer N/Q-rich proteins, and in some cases likely lose them en masse, perhaps due to greater amyloid intolerance, although they contain relatively more non-N/Q-rich predicted prions. We find that recent mutational tendencies arising during Saccharomycetes evolution (i.e., increased numbers of N residues and a tendency to form more poly-N tracts), contributed to the expansion/development of the prion phenomenon. Variation in these mutational tendencies in Saccharomycetes is correlated with the population sizes of prion-like proteins, thus implying that selection pressures on N/Q-rich protein sequences against amyloidogenesis are not generally maintained in budding yeasts.ConclusionsThese results help to delineate further the limits and origins of N/Q-rich prions, and provide insight as a case study of the evolution of compositionally-defined protein domains."xsd:string |
| http://purl.uniprot.org/citations/26809710 | http://purl.org/dc/terms/identifier | "doi:10.1186/s12862-016-0594-3"xsd:string |
| http://purl.uniprot.org/citations/26809710 | http://purl.uniprot.org/core/author | "Fitzpatrick D."xsd:string |
| http://purl.uniprot.org/citations/26809710 | http://purl.uniprot.org/core/author | "Harrison P.M."xsd:string |
| http://purl.uniprot.org/citations/26809710 | http://purl.uniprot.org/core/author | "An L."xsd:string |
| http://purl.uniprot.org/citations/26809710 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/26809710 | http://purl.uniprot.org/core/name | "BMC Evol Biol"xsd:string |
| http://purl.uniprot.org/citations/26809710 | http://purl.uniprot.org/core/pages | "24"xsd:string |
| http://purl.uniprot.org/citations/26809710 | http://purl.uniprot.org/core/title | "Emergence and evolution of yeast prion and prion-like proteins."xsd:string |
| http://purl.uniprot.org/citations/26809710 | http://purl.uniprot.org/core/volume | "16"xsd:string |
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