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- W4214532364 abstract "Although many components of the cell division machinery in bacteria have been identified1,2, the mechanisms by which they work together to divide the cell remain poorly understood. Key among these components is the tubulin FtsZ, which forms a Z ring at the midcell. FtsZ recruits the other cell division proteins, collectively called the divisome, and the Z ring constricts as the cell divides. We applied live-cell single-molecule imaging to describe the dynamics of the divisome in detail, and to evaluate the individual roles of FtsZ-binding proteins (ZBPs), specifically FtsA and the ZBPs EzrA, SepF and ZapA, in cytokinesis. We show that the divisome comprises two subcomplexes that move differently: stationary ZBPs that transiently bind to treadmilling FtsZ filaments, and a moving complex that includes cell wall synthases. Our imaging analyses reveal that ZBPs bundle FtsZ filaments together and condense them into Z rings, and that this condensation is necessary for cytokinesis. PMID: 33737746 Funding information This work was supported by: National Science Foundation (NSF), Grant ID: DGE1144152 U.S. Department of Health & Human Services | National Institutes of Health (NIH), Grant ID: DP2AI117923-01 National Science Foundation (NSF), Grant ID: 1764269 NIAID NIH HHS, United States Grant ID: DP2 AI117923" @default.
- W4214532364 created "2022-03-02" @default.
- W4214532364 creator A5030247767 @default.
- W4214532364 date "2021-05-24" @default.
- W4214532364 modified "2023-09-27" @default.
- W4214532364 title "Faculty Opinions recommendation of Single-molecule imaging reveals that Z-ring condensation is essential for cell division in Bacillus subtilis." @default.
- W4214532364 doi "https://doi.org/10.3410/f.739766772.793584640" @default.
- W4214532364 hasPublicationYear "2021" @default.
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