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- W4205656853 abstract "FtsA is an early component of the Z-ring, the structure that divides most bacteria, formed by tubulin-like FtsZ. FtsA belongs to the actin family of proteins, showing an unusual subdomain architecture. Here we reconstitute the tethering of FtsZ to the membrane via FtsA's C-terminal amphipathic helix in vitro using Thermotoga maritima proteins. A crystal structure of the FtsA:FtsZ interaction reveals 16 amino acids of the FtsZ tail bound to subdomain 2B of FtsA. The same structure and a second crystal form of FtsA reveal that FtsA forms actin-like protofilaments with a repeat of 48 Å. The identical repeat is observed when FtsA is polymerized using a lipid monolayer surface and FtsAs from three organisms form polymers in cells when overexpressed, as observed by electron cryotomography. Mutants that disrupt polymerization also show an elongated cell division phenotype in a temperature-sensitive FtsA background, demonstrating the importance of filament formation for FtsA's function in the Z-ring. PMID: 22473211 Funding information This work was supported by: Medical Research Council, United Kingdom Grant ID: U105184326 Medical Research Council, United Kingdom Grant ID: MC_U105184326" @default.
- W4205656853 created "2022-01-26" @default.
- W4205656853 creator A5043777416 @default.
- W4205656853 date "2012-04-19" @default.
- W4205656853 modified "2023-10-16" @default.
- W4205656853 title "Faculty Opinions recommendation of FtsA forms actin-like protofilaments." @default.
- W4205656853 doi "https://doi.org/10.3410/f.14267363.15779577" @default.
- W4205656853 hasPublicationYear "2012" @default.
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