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Nat Commun. 2019 Dec 17;10(1):5744. doi: 10.1038/s41467-019-13702-4.

Cooperative ordering of treadmilling filaments in cytoskeletal networks of FtsZ and its crosslinker ZapA.

Author information

1
Institute of Science and Technology Austria, 3400, Klosterneuburg, Austria.
2
School of Chemistry and Biochemistry, University of Geneva, 1211, Geneva, Switzerland.
3
Max Planck Institute of Molecular Cell Biology and Genetics, 01307, Dresden, Germany.
4
Max Planck Institute for the Physics of Complex Systems, 01187, Dresden, Germany.
5
Centre for Systems Biology Dresden, 01307, Dresden, Germany.
6
Cluster of Excellence Physics of Life, TU Dresden, 01062, Dresden, Germany.
7
Institute of Science and Technology Austria, 3400, Klosterneuburg, Austria. martin.loose@ist.ac.at.

Abstract

During bacterial cell division, the tubulin-homolog FtsZ forms a ring-like structure at the center of the cell. This Z-ring not only organizes the division machinery, but treadmilling of FtsZ filaments was also found to play a key role in distributing proteins at the division site. What regulates the architecture, dynamics and stability of the Z-ring is currently unknown, but FtsZ-associated proteins are known to play an important role. Here, using an in vitro reconstitution approach, we studied how the well-conserved protein ZapA affects FtsZ treadmilling and filament organization into large-scale patterns. Using high-resolution fluorescence microscopy and quantitative image analysis, we found that ZapA cooperatively increases the spatial order of the filament network, but binds only transiently to FtsZ filaments and has no effect on filament length and treadmilling velocity. Together, our data provides a model for how FtsZ-associated proteins can increase the precision and stability of the bacterial cell division machinery in a switch-like manner.

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