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

Author

Listed:
  • 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)

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.

Suggested Citation

  • 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 & Jian Liu, 2021. "Treadmilling FtsZ polymers drive the directional movement of sPG-synthesis enzymes via a Brownian ratchet mechanism," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
  • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-020-20873-y
    DOI: 10.1038/s41467-020-20873-y
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    Cited by:

    1. Zhixin Lyu & Atsushi Yahashiri & Xinxing Yang & Joshua W. McCausland & Gabriela M. Kaus & Ryan McQuillen & David S. Weiss & Jie Xiao, 2022. "FtsN maintains active septal cell wall synthesis by forming a processive complex with the septum-specific peptidoglycan synthases in E. coli," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    2. Brooke M. Britton & Remy A. Yovanno & Sara F. Costa & Joshua McCausland & Albert Y. Lau & Jie Xiao & Zach Hensel, 2023. "Conformational changes in the essential E. coli septal cell wall synthesis complex suggest an activation mechanism," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    3. Junso Fujita & Hiroshi Amesaka & Takuya Yoshizawa & Kota Hibino & Natsuki Kamimura & Natsuko Kuroda & Takamoto Konishi & Yuki Kato & Mizuho Hara & Tsuyoshi Inoue & Keiichi Namba & Shun-ichi Tanaka & H, 2023. "Structures of a FtsZ single protofilament and a double-helical tube in complex with a monobody," Nature Communications, Nature, vol. 14(1), pages 1-13, December.
    4. Bill Söderström & Matthew J. Pittorino & Daniel O. Daley & Iain G. Duggin, 2022. "Assembly dynamics of FtsZ and DamX during infection-related filamentation and division in uropathogenic E. coli," Nature Communications, Nature, vol. 13(1), pages 1-13, December.
    5. Philipp Radler & Natalia Baranova & Paulo Caldas & Christoph Sommer & Mar López-Pelegrín & David Michalik & Martin Loose, 2022. "In vitro reconstitution of Escherichia coli divisome activation," Nature Communications, Nature, vol. 13(1), pages 1-15, December.

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