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000139830 0247_ $$2doi$$a10.1074/jbc.M117.809004
000139830 0247_ $$2pmid$$apmid:29330303
000139830 0247_ $$2pmc$$apmc:PMC5836139
000139830 0247_ $$2ISSN$$a0021-9258
000139830 0247_ $$2ISSN$$a1067-8816
000139830 0247_ $$2ISSN$$a1083-351X
000139830 0247_ $$2altmetric$$aaltmetric:31662760
000139830 037__ $$aDZNE-2020-06152
000139830 041__ $$aEnglish
000139830 082__ $$a540
000139830 1001_ $$aChandramowlishwaran, Pavithra$$b0
000139830 245__ $$aMammalian amyloidogenic proteins promote prion nucleation in yeast.
000139830 260__ $$aBethesda, Md.$$bSoc.60645$$c2018
000139830 264_1 $$2Crossref$$3online$$bAmerican Society for Biochemistry & Molecular Biology (ASBMB)$$c2018-01-12
000139830 264_1 $$2Crossref$$3print$$bAmerican Society for Biochemistry & Molecular Biology (ASBMB)$$c2018-03-02
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000139830 3367_ $$2ORCID$$aJOURNAL_ARTICLE
000139830 3367_ $$00$$2EndNote$$aJournal Article
000139830 520__ $$aFibrous cross-β aggregates (amyloids) and their transmissible forms (prions) cause diseases in mammals (including humans) and control heritable traits in yeast. Initial nucleation of a yeast prion by transiently overproduced prion-forming protein or its (typically, QN-rich) prion domain is efficient only in the presence of another aggregated (in most cases, QN-rich) protein. Here, we demonstrate that a fusion of the prion domain of yeast protein Sup35 to some non-QN-rich mammalian proteins, associated with amyloid diseases, promotes nucleation of Sup35 prions in the absence of pre-existing aggregates. In contrast, both a fusion of the Sup35 prion domain to a multimeric non-amyloidogenic protein and the expression of a mammalian amyloidogenic protein that is not fused to the Sup35 prion domain failed to promote prion nucleation, further indicating that physical linkage of a mammalian amyloidogenic protein to the prion domain of a yeast protein is required for the nucleation of a yeast prion. Biochemical and cytological approaches confirmed the nucleation of protein aggregates in the yeast cell. Sequence alterations antagonizing or enhancing amyloidogenicity of human amyloid-β (associated with Alzheimer's disease) and mouse prion protein (associated with prion diseases), respectively, antagonized or enhanced nucleation of a yeast prion by these proteins. The yeast-based prion nucleation assay, developed in our work, can be employed for mutational dissection of amyloidogenic proteins. We anticipate that it will aid in the identification of chemicals that influence initial amyloid nucleation and in searching for new amyloidogenic proteins in a variety of proteomes.
000139830 536__ $$0G:(DE-HGF)POF3-342$$a342 - Disease Mechanisms and Model Systems (POF3-342)$$cPOF3-342$$fPOF III$$x0
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000139830 650_7 $$2NLM Chemicals$$aAmyloid
000139830 650_7 $$2NLM Chemicals$$aAmyloid beta-Peptides
000139830 650_7 $$2NLM Chemicals$$aPeptide Fragments
000139830 650_7 $$2NLM Chemicals$$aPeptide Termination Factors
000139830 650_7 $$2NLM Chemicals$$aProtein Aggregates
000139830 650_7 $$2NLM Chemicals$$aSUP35 protein, S cerevisiae
000139830 650_7 $$2NLM Chemicals$$aSaccharomyces cerevisiae Proteins
000139830 650_7 $$2NLM Chemicals$$aamyloid beta-protein (1-40)
000139830 650_7 $$2NLM Chemicals$$aamyloid beta-protein (1-42)
000139830 650_2 $$2MeSH$$aAmyloid: metabolism
000139830 650_2 $$2MeSH$$aAmyloid beta-Peptides: metabolism
000139830 650_2 $$2MeSH$$aHumans
000139830 650_2 $$2MeSH$$aPeptide Fragments: metabolism
000139830 650_2 $$2MeSH$$aPeptide Termination Factors: chemistry
000139830 650_2 $$2MeSH$$aPeptide Termination Factors: metabolism
000139830 650_2 $$2MeSH$$aProtein Aggregates
000139830 650_2 $$2MeSH$$aProtein Domains
000139830 650_2 $$2MeSH$$aSaccharomyces cerevisiae Proteins: chemistry
000139830 650_2 $$2MeSH$$aSaccharomyces cerevisiae Proteins: metabolism
000139830 7001_ $$aSun, Meng$$b1
000139830 7001_ $$aCasey, Kristin L$$b2
000139830 7001_ $$aRomanyuk, Andrey V$$b3
000139830 7001_ $$aGrizel, Anastasiya V$$b4
000139830 7001_ $$aSopova, Julia V$$b5
000139830 7001_ $$aRubel, Aleksandr A$$b6
000139830 7001_ $$aNussbaum-Krammer, Carmen$$b7
000139830 7001_ $$0P:(DE-2719)2481765$$aVorberg, Ina M$$b8$$udzne
000139830 7001_ $$0P:(DE-HGF)0$$aChernoff, Yury O$$b9$$eCorresponding author
000139830 77318 $$2Crossref$$3journal-article$$a10.1074/jbc.m117.809004$$b : American Society for Biochemistry & Molecular Biology (ASBMB), 2018-01-12$$n9$$p3436-3450$$tJournal of Biological Chemistry$$v293$$x0021-9258$$y2018
000139830 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M117.809004$$gVol. 293, no. 9, p. 3436 - 3450$$n9$$p3436-3450$$q293:9<3436 - 3450$$tThe journal of biological chemistry$$v293$$x0021-9258$$y2018
000139830 8567_ $$2Pubmed Central$$uhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC5836139
000139830 909CO $$ooai:pub.dzne.de:139830$$pVDB
000139830 9101_ $$0I:(DE-588)1065079516$$6P:(DE-2719)2481765$$aDeutsches Zentrum für Neurodegenerative Erkrankungen$$b8$$kDZNE
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000139830 9141_ $$y2018
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