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

Joshua W. McCausland, Xinxing Yang, Georgia R. Squyres, Zhixin Lyu, Kevin E. Bruce, Melissa M. Lamanna, Bill Söderström, Ethan C. Garner, Malcolm E. Winkler, Jie Xiao () and Jian Liu ()
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Joshua W. McCausland: Johns Hopkins School of Medicine
Xinxing Yang: Johns Hopkins School of Medicine
Georgia R. Squyres: Harvard University
Zhixin Lyu: Johns Hopkins School of Medicine
Kevin E. Bruce: Indiana University Bloomington
Melissa M. Lamanna: Indiana University Bloomington
Bill Söderström: University of Technology Sydney
Ethan C. Garner: Harvard University
Malcolm E. Winkler: Indiana University Bloomington
Jie Xiao: Johns Hopkins School of Medicine
Jian Liu: Johns Hopkins School of Medicine

Nature Communications, 2021, vol. 12, issue 1, 1-13

Abstract: 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.

Date: 2021
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DOI: 10.1038/s41467-020-20873-y

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