Dictyostelium discoideum has a highly Q/N-rich proteome and shows an unusual resilience to protein aggregation
Malinovska L, Palm S, Gibson K, Verbavatz J, Alberti S. Dictyostelium discoideum has a highly Q/N-rich proteome and shows an unusual resilience to protein aggregation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2015, 112: e2620-e2629. PMID: 25941378, PMCID: PMC4443358, DOI: 10.1073/pnas.1504459112.Peer-Reviewed Original ResearchMeSH KeywordsDictyosteliumElectrophoresis, Polyacrylamide GelFluorescence Recovery After PhotobleachingHumansHuntingtin ProteinMicroscopy, ElectronMicroscopy, FluorescenceNerve Tissue ProteinsPeptide Termination FactorsPrionsProtein Aggregation, PathologicalProteomeProteostasis DeficienciesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsConceptsPrion-like proteinsD. discoideumMolecular chaperonesDictyostelium discoideumHuntingtin exon 1Yeast prion protein Sup35Prion-like domainsOverall aggregation propensityProtein-misfolding diseasesUbiquitin-proteasome systemPrion protein Sup35Rich proteomeHsp100 familyCellular proteostasisPrion stateCytosolic aggregatesSequence similarityPrion domainBioinformatics toolsProtein aggregationProteostatic capacityDiscoideumAggregation propensityProteomePrion protein