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bioRxiv · 10.1101/2020.12.14.422651

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

Schumacher, D.·Harms, A.·Bergeler, S.·Frey, E.·Sogaard-Andersen, L.
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Abstract

Cell division is precisely regulated to generate daughter cells of correct size and shape. In the social bacterium Myxococcus xanthus, the tripartite PomX/Y/Z complex directly stimulates positioning of the cytokinetic FtsZ-ring at midcell to mark the division site. The [~]15 MDa PomX/Y/Z complex associates with the nucleoid in a PomZ-dependent manner, translocates to midcell to stimulate FtsZ-ring formation, and undergoes fission during division. We demonstrate that PomX consists of two functionally distinct domains and has three functions. The N-terminal domain interacts with the ParA/MinD ATPase PomZ and stimulates PomZ ATPase activity. The C-terminal domain mediates PomX self-interaction, interaction to PomY, and serves as a scaffold for PomX/Y/Z complex formation. Moreover, the PomX/PomZ interaction is important for fission. 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.

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Schumacher, D., Harms, A., Bergeler, S., Frey, E., Sogaard-Andersen, L.. 2020-12-14. PomX, a ParA/MinD ATPase activating protein, is a triple regulator of cell division in Myxococcus xanthus. https://doi.org/10.1101/2020.12.14.422651

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