Faculty Opinions recommendation of Peptidoglycan synthesis drives an FtsZ-treadmilling-independent step of cytokinesis.

Peptidoglycan (PG), the major component of the bacterial wall, protects cells from mechanical stress resulting from high intracellular turgor.PG biosynthesis (Fig. 1a) is very similar in all bacteria.Therefore, different bacterial shapes are mainly determined by the spatial and temporal regulation of PG synthesis, not by its chemical composition.Rodshaped bacteria, such as Bacillus subtilis or Escherichia coli, achieve their shape through the action of two PG synthesis machines that act at the septum and at the lateral wall, in processes coordinated by cytoskeletal proteins FtsZ and MreB, respectively 1,2 .The tubulin homologue FtsZ is the first protein recruited to the division site where it assembles in filaments (Z-ring) that undergo treadmilling and recruit later divisome proteins 3,4 .Importantly, the rate of treadmilling in B. subtilis controls both the rate of PG synthesis and of cell division 3 .The actin homologue MreB forms discrete patches that move circumferentially around the cell, in tracks perpendicular to the cell long axis, and organise insertion of new cell wall during elongation 5,6 .Cocci like Staphylococcus aureus possess only one PG synthesis machinery 7,8 , which is diverted from the cell periphery to the septum in preparation for division 9 .The molecular cue that coordinates this transition has remained elusive.Here, we investigated the localisation of S. aureus PG biosynthesis proteins and showed that the putative lipid II flippase MurJ is recruited to the septum by the DivIB/ DivIC/FtsL complex, driving PG incorporation to midcell.MurJ recruitment corresponds to Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.