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- W3132319289 abstract "Many species of bacteria adapt to energy dearth environment, using subcellular membrane less organelles called bacterial microcompartments (BMC). BMCs are very small in size (100-150 nm) and are formed by the self-assembly of thousands of protein subunits, all encoded by genes belonging to a single operon. The operon contains genes that encode for enzymes and shell proteins. The shell proteins self-assemble to form the outer coat of the compartment and enzymes are encapsulated within. A puzzling question in BMC biology is to understand the mechanism which governs the formation of these small yet complex assemblages of proteins. In this work we use I,2-propanediol utilization microcompartments (PduBMC) as a model to identify the factors that drive the self-assembly of BMC proteins. We find that the major shell protein PduBB’ tend to self-associate with the increase in ionic strength of solution. Presence of a divalent cation Mg2+ and a crowding agent triggers liquid-liquid phase separation resulting in the formation of shell protein droplets. These protein droplets exhibit coalescing property when observed under fluorescence microscope. A combination of spectroscopic and imaging techniques further confirms that Mg2+ is indeed crucial to the assembly and stability of PduBMC. The shell protein PduBB’ interacts with the enzyme diol-dehydratase PduCDE and co-assemble into phase separated liquid droplets. The co-assembly of PduCDE and PduBB’ results in the enhancement of catalytic activity of the enzyme. Together our results suggest the combined role of protein-protein interactions and phase separation in the self-assembly of proteins in PduBMC." @default.
- W3132319289 created "2021-03-01" @default.
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- W3132319289 date "2021-02-01" @default.
- W3132319289 modified "2023-09-30" @default.
- W3132319289 title "Unraveling the Driving Forces Behind the Biogenesis of Bacterial Microcompartments" @default.
- W3132319289 doi "https://doi.org/10.1016/j.bpj.2020.11.1420" @default.
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