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- W3048759819 abstract "Bacterial cellulose is a widespread biofilm component that can modulate microbial fitness and virulence both in the environment and infected hosts. Whereas its secretion generally involves an inner membrane c-di-GMP-dependent synthase tandem (BcsAB) across the bacterial domain of life, enterobacteria feature sophisticated Escherichia coli -like Bcs secretion systems, where multiple additional subunits are either required for secretion or contribute to the maximal production of the polysaccharide in vivo. Here, we demonstrate that essential-for-secretion BcsR and BcsQ regulate each other's folding and stability and are recruited to the inner membrane via c-di-GMP-sensing BcsE and its intraoperon partner, BcsF. Crystallographic and functional data reveal that BcsE features unexpected domain architecture and likely acts on multiple levels to fine-tune bacterial cellulose production, from the early stages of secretion system assembly to the maintenence of a membrane-proximal pool of dimeric c-di-GMP for processive synthase activation." @default.
- W3048759819 created "2020-08-18" @default.
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- W3048759819 date "2020-08-25" @default.
- W3048759819 modified "2023-10-06" @default.
- W3048759819 title "Structure and Multitasking of the c-di-GMP-Sensing Cellulose Secretion Regulator BcsE" @default.
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- W3048759819 doi "https://doi.org/10.1128/mbio.01303-20" @default.
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