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Single-molecule imaging reveals that Z-ring condensation is essential for cell division in Bacillus subtilis
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Single-molecule imaging reveals that Z-ring condensation is essential for cell division in Bacillus subtilis
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Journal Article
Single-molecule imaging reveals that Z-ring condensation is essential for cell division in Bacillus subtilis
2021
Overview
Although many components of the cell division machinery in bacteria have been identified
1
,
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.
Live-cell single-molecule imaging of different
Bacillus subtilis
divisome proteins that interact with FtsZ (such as FtsA, EzrA, SepF and ZapA) reveals different subcomplexes with distinct motility: stationary FtsZ-binding proteins that bind transiently to treadmilling FtsZ filaments, and moving complexes containing cell wall synthases.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 14/35
/ 14/63
/ Bacillus subtilis - chemistry
/ Bacillus subtilis - cytology
/ Bacillus subtilis - genetics
/ Bacillus subtilis - metabolism
/ Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Biomedical and Life Sciences
/ Cytoskeletal Proteins - chemistry
/ Cytoskeletal Proteins - genetics
/ Cytoskeletal Proteins - metabolism
/ Letter
/ Proteins
/ Tubulin
/ Virology
