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- W2911432880 abstract "Recent work in micron-sized bacteria has highlighted the presence of membrane-less microdomains that organize protein signaling complexes. In addition to well understood “lock and key” protein domains that lie at the core of cell signaling, we are beginning to understand the role of unstructured protein bimolecular condensates in intracellular communication. However, the molecular principles that organize chemical reactions in these domains are poorly understood. In order to understand these principles, we have used a combination of in vitro reconstitution and single-molecule fluorescence techniques to study one of the two cell pole microdomains in the Gram negative bacterium, Caulobacter crescentus. Caulobacter divides asymmetrically into a sessile stalked cell and a flagellated swarmer cell. Much of this asymmetric division is regulated through different signaling pathways that reside in microdomains at the two cell poles. Specifically, at the stalked pole, two intrinsically disordered proteins, PopZ and SpmX, form a stable bimolecular condensate. PopZ recruits the lysozyme homolog SpmX, which further recruits the kinase DivJ to establish the stalked cell identity. Reconstitution of this signaling complex on supported lipid bilayers revealed that SpmX and PopZ can form phase-separated droplets that sequester DivJ and control its kinase activity. Further, we have identified molecular determinants of SpmX and PopZ phase separation that control the material properties and enzyme kinetics in this condensate. Our results underscore the relationship between IDR mediated interactions that govern the physical environment around signaling proteins, and demonstrate the applications of disordered scaffolds to modulate biochemical reactions in vivo." @default.
- W2911432880 created "2019-02-21" @default.
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- W2911432880 date "2019-02-01" @default.
- W2911432880 modified "2023-09-28" @default.
- W2911432880 title "Dissection of Protein Function Within a Bacterial Biomolecular Condensate by In Vitro Reconstitution" @default.
- W2911432880 doi "https://doi.org/10.1016/j.bpj.2018.11.2475" @default.
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