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dc.contributor.authorYuan, Andy Hen_US
dc.contributor.authorGarrity, Sean Jen_US
dc.contributor.authorNako, Entelaen_US
dc.contributor.authorHochschild, Annen_US
dc.date.accessioned2014-11-03T17:40:29Z
dc.date.issued2014en_US
dc.identifier.citationYuan, Andy H, Sean J Garrity, Entela Nako, and Ann Hochschild. 2014. “Prion propagation can occur in a prokaryote and requires the ClpB chaperone.” eLife 3 (1): e02949. doi:10.7554/eLife.02949. http://dx.doi.org/10.7554/eLife.02949.en
dc.identifier.issn2050-084Xen
dc.identifier.urihttp://nrs.harvard.edu/urn-3:HUL.InstRepos:13347619
dc.description.abstractPrions are self-propagating protein aggregates that are characteristically transmissible. In mammals, the PrP protein can form a prion that causes the fatal transmissible spongiform encephalopathies. Prions have also been uncovered in fungi, where they act as heritable, protein-based genetic elements. We previously showed that the yeast prion protein Sup35 can access the prion conformation in Escherichia coli. Here, we demonstrate that E. coli can propagate the Sup35 prion under conditions that do not permit its de novo formation. Furthermore, we show that propagation requires the disaggregase activity of the ClpB chaperone. Prion propagation in yeast requires Hsp104 (a ClpB ortholog), and prior studies have come to conflicting conclusions about ClpB's ability to participate in this process. Our demonstration of ClpB-dependent prion propagation in E. coli suggests that the cytoplasmic milieu in general and a molecular machine in particular are poised to support protein-based heredity in the bacterial domain of life. DOI: http://dx.doi.org/10.7554/eLife.02949.001en
dc.language.isoen_USen
dc.publishereLife Sciences Publications, Ltden
dc.relation.isversionofdoi:10.7554/eLife.02949en
dc.relation.hasversionhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC4150125/pdf/en
dash.licenseLAAen_US
dc.subjectprionsen
dc.subjectchaperonesen
dc.subjectSup35en
dc.subjectClpBen
dc.subjectprotein-based heredityen
dc.subjecten
dc.titlePrion propagation can occur in a prokaryote and requires the ClpB chaperoneen
dc.typeJournal Articleen_US
dc.description.versionVersion of Recorden
dc.relation.journaleLifeen
dash.depositing.authorYuan, Andy Hen_US
dc.date.available2014-11-03T17:40:29Z
dc.identifier.doi10.7554/eLife.02949*
dash.contributor.affiliatedYuan, Andy
dash.contributor.affiliatedHochschild, Ann


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