The PomXYZ Proteins Self-Organize on the Bacterial Nucleoid to Stimulate Cell Division

TL;DR

This study reveals a novel self-organizing mechanism involving PomXYZ proteins that localize at the bacterial division site by biased diffusion and fluxes on the nucleoid, guiding cell division in Myxococcus xanthus.

Contribution

It uncovers a new flux-based self-organization mechanism for positioning division machinery in bacteria, expanding understanding of cellular spatial regulation.

Findings

PomXYZ proteins form a nucleoid-associated complex that localizes at midcell.

Self-organized biased motion of PomXYZ guides division site placement.

Flux differences of PomZ generate concentration gradients that direct complex localization.

Abstract

Cell division site positioning is precisely regulated to generate correctly sized and shaped daughters. We uncover a novel strategy to position the FtsZ cytokinetic ring at midcell in the social bacterium Myxococcus xanthus. PomX, PomY and the nucleoid-binding ParA/MinD ATPase PomZ self-assemble forming a large nucleoid-associated complex that localizes at the division site before FtsZ to directly guide and stimulate division. PomXYZ localization is generated through self-organized biased random motion on the nucleoid towards midcell and constrained motion at midcell. Experiments and theory show that PomXYZ motion is produced by diffusive PomZ fluxes on the nucleoid into the complex. Flux differences scale with the intracellular asymmetry of the complex and are converted into a local PomZ concentration gradient across the complex with translocation towards the higher PomZ concentration. At midcell, fluxes equalize resulting in constrained motion. Flux-based mechanisms may represent a general paradigm for positioning of macromolecular structures in bacteria.