Lévy Flight Foraging of a Cell Wall Biosynthetic Enzyme Condensate in the Bacterial Cytoplasm

Abstract

Bacterial cell wall synthesis (CWS) requires spatial coordination of membrane-bound CWS enzymes by MreB, but little attention has been given to the organization of cytoplasmic enzymes at earlier steps of CWS. Performing fluorescent time-lapse imaging we find that in Bacillus subtilis MreBH, a less-characterized MreB-homolog, is essential for Levy flight-like foraging motion of a cytoplasmic condensate of the CWS enzyme MurAA during exponential growth. Movement in the cytoplasm ceases in presence of a MurAA catalytic inhibitor, deletion of mreBH, or ablation of cell-wall hydrolysis, suggesting that MreBH links MurAA condensates with active CWS zones. A biophysical model demonstrates the unique advantage given by the Levy flight trajectory and catalytic properties of this enzyme condensate over diffuse enzymes, enhancing local enzymatic reaction rates and leading to faster cell division rates.