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FtsZ treadmilling is essential for Z-ring condensation and septal constriction initiation in Bacillus subtilis cell division

Lookup NU author(s): Dr Kevin WhitleyORCiD, Calum Jukes, Nicholas Tregidgo, Dr Eleni Karinou, Dr Yann Cesbron, Dr Seamus Holden

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This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).


Abstract

Despite the central role of division in bacterial physiology, how division proteins work together as a nanoscale machine to divide the cell remains poorly understood. Cell division by cell wall synthesis proteins is guided by the cytoskeleton protein FtsZ, which assembles at mid-cell as a dense Z-ring formed of treadmilling filaments. However, although FtsZ treadmilling is essential for cell division, the function of FtsZ treadmilling remains unclear. Here, we systematically resolve the function of FtsZ treadmilling across each stage of division in the Gram-positive model organism Bacillus subtilis using a combination of nanofabrication, advanced microscopy, and microfluidics to measure the division-protein dynamics in live cells with ultrahigh sensitivity. We find that FtsZ treadmilling has two essential functions: mediating condensation of diffuse FtsZ filaments into a dense Z-ring, and initiating constriction by guiding septal cell wall synthesis. After constriction initiation, FtsZ treadmilling has a dispensable function in accelerating septal constriction rate. Our results show that FtsZ treadmilling is critical for assembling and initiating the bacterial cell division machine.


Publication metadata

Author(s): Whitley KD, Jukes C, Tregidgo N, Karinou E, Almada P, Cesbron Y, Henriques R, Dekker C, Holden S

Publication type: Article

Publication status: Published

Journal: Nature Communications

Year: 2021

Volume: 12

Issue: 1

Online publication date: 27/04/2021

Acceptance date: 16/03/2021

Date deposited: 06/10/2023

ISSN (electronic): 2041-1723

Publisher: Nature Research

URL: https://doi.org/10.1038/s41467-021-22526-0

DOI: 10.1038/s41467-021-22526-0

PubMed id: 33907196


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Funding

Funder referenceFunder name
203276/Z/16/Z
206670/Z/17/ZWellcome Trust
669598
BBSRC
BB/M022374/1
EPSRC
ERC
MR/K015826/1
MRC
Netherlands Organisation for Scientific Research
Newcastle University Research Fellowship
NWO/OCW

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