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

Paulo Caldas, Mar López-Pelegrín, Daniel J. G. Pearce, Nazmi Burak Budanur, Jan Brugués and Martin Loose ()
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Paulo Caldas: Institute of Science and Technology Austria
Mar López-Pelegrín: Institute of Science and Technology Austria
Daniel J. G. Pearce: School of Chemistry and Biochemistry, University of Geneva
Nazmi Burak Budanur: Institute of Science and Technology Austria
Jan Brugués: Max Planck Institute of Molecular Cell Biology and Genetics
Martin Loose: Institute of Science and Technology Austria

Nature Communications, 2019, vol. 10, issue 1, 1-13

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-13702-4

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