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• W2601083114 abstract "Abstract Microcin E492 (Mcc) is a pore-forming bacteriotoxin. Mcc activity is inhibited at the stationary phase by formation of amyloid-like aggregates in the culture. Here we report that, in a similar manner as prions, Mcc naturally exists as two conformers: a β-sheet-rich, protease-resistant, aggregated, inactive form (Mcc ia ), and a soluble, protease-sensitive, active form (Mcc a ). The exogenous addition of culture medium containing Mcc ia or purified in vitro -generated Mcc ia into the culture induces the rapid and efficient conversion of Mcc a into Mcc ia , which is maintained indefinitely after passaging, changing the bacterial phenotype. Mcc ia prion-like activity is conformation-dependent and could be reduced by immunodepleting Mcc ia . Interestingly, an internal region of Mcc shares sequence similarity with the central domain of the prion protein, which is key to the formation of mammalian prions. A synthetic peptide spanning this sequence forms amyloid-like fibrils in vitro and is capable of inducing the conversion of Mcc a into Mcc ia in vivo , suggesting that this region corresponds to the prion domain of Mcc. Our findings suggest that Mcc is the first prokaryotic protein with prion properties which harnesses prion-like transmission to regulate protein function, suggesting that propagation of biological information using a prion-based conformational switch is an evolutionary conserved mechanism." @default.
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• W2601083114 date "2017-03-31" @default.
• W2601083114 modified "2023-10-11" @default.
• W2601083114 title "Prion-like characteristics of the bacterial protein Microcin E492" @default.
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• W2601083114 doi "https://doi.org/10.1038/srep45720" @default.
• W2601083114 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5374632" @default.
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