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000140086 0247_ $$2doi$$a10.1128/MCB.00111-18
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000140086 041__ $$aEnglish
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000140086 1001_ $$0P:(DE-2719)2810519$$aDürnberger, Yvonne$$b0$$eFirst author$$udzne
000140086 245__ $$aPrion Replication in the Mammalian Cytosol: Functional Regions within a Prion Domain Driving Induction, Propagation, and Inheritance.
000140086 260__ $$aWashington, DC$$bSoc.$$c2018
000140086 264_1 $$2Crossref$$3online$$bAmerican Society for Microbiology$$c2018-07-16
000140086 264_1 $$2Crossref$$3print$$bAmerican Society for Microbiology$$c2018-05-21
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000140086 3367_ $$2BibTeX$$aARTICLE
000140086 3367_ $$2ORCID$$aJOURNAL_ARTICLE
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000140086 520__ $$aPrions of lower eukaryotes are transmissible protein particles that propagate by converting homotypic soluble proteins into growing protein assemblies. Prion activity is conferred by so-called prion domains, regions of low complexity that are often enriched in glutamines and asparagines (Q/N). The compositional similarity of fungal prion domains with intrinsically disordered domains found in many mammalian proteins raises the question of whether similar sequence elements can drive prion-like phenomena in mammals. Here, we define sequence features of the prototype Saccharomyces cerevisiae Sup35 prion domain that govern prion activities in mammalian cells by testing the ability of deletion mutants to assemble into self-perpetuating particles. Interestingly, the amino-terminal Q/N-rich tract crucially important for prion induction in yeast was dispensable for the prion life cycle in mammalian cells. Spontaneous and template-assisted prion induction, growth, and maintenance were preferentially driven by the carboxy-terminal region of the prion domain that contains a putative soft amyloid stretch recently proposed to act as a nucleation site for prion assembly. Our data demonstrate that preferred prion nucleation domains can differ between lower and higher eukaryotes, resulting in the formation of prions with strikingly different amyloid cores.
000140086 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
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000140086 650_7 $$2NLM Chemicals$$aPeptide Termination Factors
000140086 650_7 $$2NLM Chemicals$$aPrion Proteins
000140086 650_7 $$2NLM Chemicals$$aPrions
000140086 650_7 $$2NLM Chemicals$$aProtein Aggregates
000140086 650_7 $$2NLM Chemicals$$aRecombinant Proteins
000140086 650_7 $$2NLM Chemicals$$aSUP35 protein, S cerevisiae
000140086 650_7 $$2NLM Chemicals$$aSaccharomyces cerevisiae Proteins
000140086 650_2 $$2MeSH$$aAmino Acid Sequence
000140086 650_2 $$2MeSH$$aAnimals
000140086 650_2 $$2MeSH$$aBinding Sites
000140086 650_2 $$2MeSH$$aCell Line
000140086 650_2 $$2MeSH$$aCytosol: metabolism
000140086 650_2 $$2MeSH$$aMice
000140086 650_2 $$2MeSH$$aModels, Molecular
000140086 650_2 $$2MeSH$$aMutation
000140086 650_2 $$2MeSH$$aPeptide Termination Factors: biosynthesis
000140086 650_2 $$2MeSH$$aPeptide Termination Factors: chemistry
000140086 650_2 $$2MeSH$$aPeptide Termination Factors: genetics
000140086 650_2 $$2MeSH$$aPrion Proteins: biosynthesis
000140086 650_2 $$2MeSH$$aPrion Proteins: chemistry
000140086 650_2 $$2MeSH$$aPrion Proteins: genetics
000140086 650_2 $$2MeSH$$aPrions: biosynthesis
000140086 650_2 $$2MeSH$$aPrions: chemistry
000140086 650_2 $$2MeSH$$aPrions: genetics
000140086 650_2 $$2MeSH$$aProtein Aggregates: genetics
000140086 650_2 $$2MeSH$$aProtein Aggregation, Pathological: genetics
000140086 650_2 $$2MeSH$$aProtein Aggregation, Pathological: metabolism
000140086 650_2 $$2MeSH$$aProtein Domains
000140086 650_2 $$2MeSH$$aProtein Folding
000140086 650_2 $$2MeSH$$aRecombinant Proteins: biosynthesis
000140086 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000140086 650_2 $$2MeSH$$aRecombinant Proteins: genetics
000140086 650_2 $$2MeSH$$aSaccharomyces cerevisiae Proteins: biosynthesis
000140086 650_2 $$2MeSH$$aSaccharomyces cerevisiae Proteins: chemistry
000140086 650_2 $$2MeSH$$aSaccharomyces cerevisiae Proteins: genetics
000140086 650_2 $$2MeSH$$aSequence Deletion
000140086 693__ $$0EXP:(DE-2719)IDAF-20190308$$5EXP:(DE-2719)IDAF-20190308$$eImage and Data Analysis Facility (CRFS-IDAF) / Bonn$$x0
000140086 7001_ $$0P:(DE-2719)2810461$$aLiu, Shu$$b1$$udzne
000140086 7001_ $$0P:(DE-2719)2811067$$aRiemschoß, Katrin$$b2$$udzne
000140086 7001_ $$0P:(DE-2719)2651099$$aPaulsen, Lydia$$b3$$udzne
000140086 7001_ $$aBester, Romina$$b4
000140086 7001_ $$0P:(DE-2719)2810327$$aKuhn, Peer-Hendrik$$b5$$udzne
000140086 7001_ $$0P:(DE-2719)2810990$$aSchölling, Manuel$$b6$$udzne
000140086 7001_ $$0P:(DE-2719)2181459$$aLichtenthaler, Stefan F$$b7$$udzne
000140086 7001_ $$0P:(DE-2719)2481765$$aVorberg, Ina$$b8$$udzne
000140086 77318 $$2Crossref$$3journal-article$$a10.1128/mcb.00111-18$$b : American Society for Microbiology, 2018-05-21$$n15$$tMolecular and Cellular Biology$$v38$$x0270-7306$$y2018
000140086 773__ $$0PERI:(DE-600)1474919-1$$a10.1128/MCB.00111-18$$gVol. 38, no. 15, p. e00111-18/mcb/38/15/e00111-18.atom$$n15$$pe00111-18/mcb/38/15/e00111-18.atom$$q38:15<e00111-18/mcb/38/15/e00111-18.atom$$tMolecular and cellular biology$$v38$$x0270-7306$$y2018
000140086 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC6048315
000140086 909CO $$ooai:pub.dzne.de:140086$$pVDB
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000140086 9131_ $$0G:(DE-HGF)POF3-342$$1G:(DE-HGF)POF3-340$$2G:(DE-HGF)POF3-300$$aDE-HGF$$bForschungsbereich Gesundheit$$lErkrankungen des Nervensystems$$vDisease Mechanisms and Model Systems$$x0
000140086 9141_ $$y2018
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