Toggle Main Menu Toggle Search

Open Access padlockePrints

Self-organization of mortal filaments and its role in bacterial division ring formation

Lookup NU author(s): Dr Kevin WhitleyORCiD

Downloads


Licence

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


Abstract

Filaments in the cell commonly treadmill. Driven by energy consumption, they grow on one end while shrinking on the other, causing filaments to appear motile even though individual proteins remain static. This process is characteristic of cytoskeletal filaments and leads to collective filament self-organization. Here we show that treadmilling drives filament nematic ordering by dissolving misaligned filaments. Taking the bacterial FtsZ protein involved in cell division as an example, we show that this mechanism aligns FtsZ filaments in vitro and drives the organization of the division ring in living Bacillus subtilis cells. We find that ordering via local dissolution also allows the system to quickly respond to chemical and geometrical biases in the cell, enabling us to quantitatively explain the ring formation dynamics in vivo. Beyond FtsZ and other cytoskeletal filaments, our study identifies a mechanism for self-organization via constant birth and death of energy-consuming filaments.


Publication metadata

Author(s): Vanhille-Campos C, Whitley KD, Radler P, Loose M, Holden S, Saric A

Publication type: Article

Publication status: Published

Journal: Nature Physics

Year: 2024

Pages: epub ahead of print

Online publication date: 12/08/2024

Acceptance date: 27/06/2024

Date deposited: 05/09/2024

ISSN (print): 1745-2473

ISSN (electronic): 1745-2481

Publisher: Springer Nature

URL: https://doi.org/10.1038/s41567-024-02597-8

DOI: 10.1038/s41567-024-02597-8

Data Access Statement: The simulation data presented in this work are available from the University College London public data repository at https://doi.org/10.5522/04/24754527 (ref. 74). Live-cell imaging of FtsZ rings data presented in this work are from ref. 23. High-speed atomic force microscopy data presented in this work are from ref. 9. Total internal reflection fluorescence microscopy data presented in this work are from refs. 37,75,76. Code availability Appropriate documentation and example files to replicate the simulation results presented in this work are available from the University College London public data repository at https://doi.org/10.5522/04/24754527 (ref. 74). The remaining statement can be found in the article.


Altmetrics

Altmetrics provided by Altmetric


Funding

Funder referenceFunder name
Austrian Science Fund (FWF) Stand-Alone P34607 (M.L.)
European Union’s Horizon 2020 Research and Innovation Programme (grant no. 802960; A.Š.)
Royal Society (grant no. UF160266; C.V.-C. and A.Š.)
Wellcome Trust and Royal Society Sir Henry Dale Fellowship (grant no. 206670/Z/17/Z; S.H. and K.D.W.).

Share