TY - JOUR TI - PomX, a ParA/MinD ATPase activating protein, is a triple regulator of cell division in Myxococcus xanthus AU - Schumacher, Dominik AU - Harms, Andrea AU - Bergeler, Silke AU - Frey, Erwin AU - Søgaard-Andersen, Lotte A2 - Storz, Gisela A2 - Lutkenhaus, Joe VL - 10 PY - 2021 DA - 2021/03/18 SP - e66160 C1 - eLife 2021;10:e66160 DO - 10.7554/eLife.66160 UR - https://doi.org/10.7554/eLife.66160 AB - Cell division site positioning is precisely regulated but the underlying mechanisms are incompletely understood. In the social bacterium Myxococcus xanthus, the ~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. KW - bacterial cell division KW - ParA KW - ParB KW - MinE KW - MinD KW - FtsZ JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -