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Significance Cytoskeletal proteins are tightly controlled to ensure their proper dynamics and function. Here, we study the regulation of the bacterial tubulin homolog FtsZ, a core component of the bacterial… Click to show full abstract
Significance Cytoskeletal proteins are tightly controlled to ensure their proper dynamics and function. Here, we study the regulation of the bacterial tubulin homolog FtsZ, a core component of the bacterial cell division apparatus, by its alphaproteobacterial regulator MipZ. FtsZ forms polarized, treadmilling filaments at the division site, passing through different conformational states during its polymerization cycle. Using a range of different approaches, including hydrogen–deuterium exchange and fluorescence correlation spectroscopy, we show that MipZ can sequester FtsZ monomers, affect the conformation of FtsZ, and block the polymerization interface at the (+)-end of FtsZ filaments, thereby disrupting their treadmilling dynamics and inducing filament disassembly. This combination of mechanisms may help to fine-tune the regulatory effect of MipZ and ensure robust division site placement.