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- W2922096027 abstract "Abstract For bacterial cell division, treadmilling filaments of FtsZ organize into a ring-like structure at the center of the cell. What governs the architecture and stability of this dynamic Z-ring is currently unknown, but FtsZ-associated proteins have been suggested to play an important role. Here, we used an in vitro reconstitution approach combined with fluorescence microscopy to study the influence of the well-conserved protein ZapA on the organization and dynamics of FtsZ filaments recruited to a supported membrane. We found that ZapA increases the spatial order and stabilizes the steady-state architecture of the FtsZ filament network in a highly cooperative manner. Despite its strong influence on their large-scale organization, ZapA binds only transiently to FtsZ filaments and has no effect on their treadmilling velocity. Together, our data explains how FtsZ-associated proteins can contribute to the precision and stability of the Z-ring without compromising treadmilling dynamics." @default.
- W2922096027 created "2019-03-22" @default.
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- W2922096027 date "2019-03-18" @default.
- W2922096027 modified "2023-10-16" @default.
- W2922096027 title "ZapA stabilizes FtsZ filament bundles without slowing down treadmilling dynamics" @default.
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- W2922096027 doi "https://doi.org/10.1101/580944" @default.
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