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Journal Article

PomX, a ParA/MinD ATPase activating protein, is a triple regulator of cell division in Myxococcus xanthus

MPS-Authors
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Schumacher,  Dominik
Bacterial Adaption and Differentiation, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

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Harms,  Andrea
Bacterial Adaption and Differentiation, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

/persons/resource/persons254723

Søgaard-Andersen,  Lotte       
Bacterial Adaption and Differentiation, Department of Ecophysiology, Max Planck Institute for Terrestrial Microbiology, Max Planck Society;

External Resource

https://doi.org/10.7554/eLife.66160
(Publisher version)

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Citation

Schumacher, D., Harms, A., Bergeler, S., Frey, E., & Søgaard-Andersen, L. (2021). PomX, a ParA/MinD ATPase activating protein, is a triple regulator of cell division in Myxococcus xanthus. eLife, 10: e66160. doi:10.7554/eLife.66160.


Cite as: https://hdl.handle.net/21.11116/0000-0008-BDE6-0
Abstract
Cell division site positioning is precisely regulated but the underlying
mechanisms are incompletely understood. In the social bacterium
Myxococcus xanthus, the similar to 15 MDa tripartite PomX/Y/Z complex
associates with and translocates across the nucleoid in a PomZ
ATPase-dependent manner to directly position and stimulate formation of
the cytokinetic FtsZ-ring at midcell, and then undergoes fission during
division. Here, we demonstrate that PomX consists of two functionally
distinct domains and has three functions. The N-terminal domain
stimulates ATPase activity of the ParA/MinD ATPase PomZ. The C-terminal
domain interacts with PomY and forms polymers, which serve as a scaffold
for PomX/Y/Z complex formation. Moreover, the PomX/PomZ interaction is
important for fission of the PomX/Y/Z complex. These observations
together with previous work support that the architecturally diverse
ATPase activating proteins of ParA/MinD ATPases are highly modular and
use the same mechanism to activate their cognate ATPase via a short
positively charged N-terminal extension.