Treadmilling FtsZ polymers drive the directional movement of sPG-synthesis enzymes via a Brownian ratchet mechanism.

McCausland, JW; Yang, X; Squyres, GR; Lyu, Z; Bruce, KE; Lamanna, MM; Söderström, B; Garner, EC; Winkler, ME; Xiao, J; Liu, J

Treadmilling FtsZ polymers drive the directional movement of sPG-synthesis enzymes via a Brownian ratchet mechanism.

McCausland, JW Yang, X Squyres, GR Lyu, Z Bruce, KE Lamanna, MM Söderström, B Garner, EC Winkler, ME Xiao, J Liu, J

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Publisher:: Springer Science and Business Media LLC
Publication Type:: Journal Article
Citation:: Nature communications, 2021, 12, (1), pp. 609
Issue Date:: 2021-01-27

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Field	Value	Language
dc.contributor.author	McCausland, JW
dc.contributor.author	Yang, X
dc.contributor.author	Squyres, GR
dc.contributor.author	Lyu, Z
dc.contributor.author	Bruce, KE
dc.contributor.author	Lamanna, MM
dc.contributor.author	Söderström, B
dc.contributor.author	Garner, EC
dc.contributor.author	Winkler, ME
dc.contributor.author	Xiao, J
dc.contributor.author	Liu, J
dc.date.accessioned	2021-02-18T23:24:21Z
dc.date.available	2020-12-15
dc.date.available	2021-02-18T23:24:21Z
dc.date.issued	2021-01-27
dc.identifier.citation	Nature communications, 2021, 12, (1), pp. 609
dc.identifier.issn	2041-1723
dc.identifier.issn	2041-1723
dc.identifier.uri	http://hdl.handle.net/10453/146220
dc.description.abstract	The FtsZ protein is a central component of the bacterial cell division machinery. It polymerizes at mid-cell and recruits more than 30 proteins to assemble into a macromolecular complex to direct cell wall constriction. FtsZ polymers exhibit treadmilling dynamics, driving the processive movement of enzymes that synthesize septal peptidoglycan (sPG). Here, we combine theoretical modelling with single-molecule imaging of live bacterial cells to show that FtsZ's treadmilling drives the directional movement of sPG enzymes via a Brownian ratchet mechanism. The processivity of the directional movement depends on the binding potential between FtsZ and the sPG enzyme, and on a balance between the enzyme's diffusion and FtsZ's treadmilling speed. We propose that this interplay may provide a mechanism to control the spatiotemporal distribution of active sPG enzymes, explaining the distinct roles of FtsZ treadmilling in modulating cell wall constriction rate observed in different bacteria.
dc.format	Electronic
dc.language	eng
dc.publisher	Springer Science and Business Media LLC
dc.relation.ispartof	Nature communications
dc.relation.isbasedon	10.1038/s41467-020-20873-y
dc.rights	info:eu-repo/semantics/openAccess
dc.rights	This is a post-peer-review, pre-copyedit version of an article published in Nature communications. The final authenticated version is available online at: https://dx.doi.org/10.1038/s41467-020-20873-y.	en_US
dc.subject.mesh	Biopolymers
dc.subject.mesh	Enzymes
dc.subject.mesh	Peptidoglycan
dc.subject.mesh	Bacterial Proteins
dc.subject.mesh	Models, Biological
dc.subject.mesh	Single Molecule Imaging
dc.subject.mesh	Bacterial Proteins
dc.subject.mesh	Biopolymers
dc.subject.mesh	Enzymes
dc.subject.mesh	Models, Biological
dc.subject.mesh	Peptidoglycan
dc.subject.mesh	Single Molecule Imaging
dc.title	Treadmilling FtsZ polymers drive the directional movement of sPG-synthesis enzymes via a Brownian ratchet mechanism.
dc.type	Journal Article
utslib.citation.volume	12
utslib.location.activity	England
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
pubs.organisational-group	/University of Technology Sydney
utslib.copyright.status	open_access	*
dc.date.updated	2021-02-18T23:24:03Z
pubs.issue	1
pubs.publication-status	Published
pubs.volume	12
utslib.citation.issue	1

Abstract:

The FtsZ protein is a central component of the bacterial cell division machinery. It polymerizes at mid-cell and recruits more than 30 proteins to assemble into a macromolecular complex to direct cell wall constriction. FtsZ polymers exhibit treadmilling dynamics, driving the processive movement of enzymes that synthesize septal peptidoglycan (sPG). Here, we combine theoretical modelling with single-molecule imaging of live bacterial cells to show that FtsZ's treadmilling drives the directional movement of sPG enzymes via a Brownian ratchet mechanism. The processivity of the directional movement depends on the binding potential between FtsZ and the sPG enzyme, and on a balance between the enzyme's diffusion and FtsZ's treadmilling speed. We propose that this interplay may provide a mechanism to control the spatiotemporal distribution of active sPG enzymes, explaining the distinct roles of FtsZ treadmilling in modulating cell wall constriction rate observed in different bacteria.

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http://hdl.handle.net/10453/146220