Diffusion and capture permits dynamic coupling between treadmilling FtsZ filaments and cell division proteins

Most bacteria accomplish cell division with the help of a dynamic protein complex called the divisome, which spans the cell envelope in the plane of division. Assembly and activation of this machinery is coordinated by the tubulin-related GTPase FtsZ, which was found to form treadmilling filaments on supported bilayers in vitro(1) and in live cells where they circle around the cell division site(2,3). Treadmilling of FtsZ is thought to actively move proteins around the cell thereby distributing peptidoglycan synthesis and coordinating the inward growth of the septum to form the new poles of the daughter cells(4). However, the molecular mechanisms underlying this function are largely unknown. Here, to study how FtsZ polymerization dynamics are coupled to downstream proteins, we reconstituted part of the bacterial cell division machinery using its purified components FtsZ, FtsA and truncated transmembrane proteins essential for cell division. We found that the membrane-bound cytosolic peptides of FtsN and FtsQ co-migrated with treadmilling FtsZ-FtsA filaments, but despite their directed collective behavior, individual peptides showed random motion and transient confinement. Our work suggests that divisome proteins follow treadmilling FtsZ filaments by a diffusion-and-capture mechanism, which can give rise to a moving zone of signaling activity at the division site.