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

ABSTRACT: 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 are coordinated by the tubulin-related GTPase FtsZ, which was found to form treadmilling filaments on supported bilayers in vitro¹, as well as in live cells, in which filaments circle around the cell division site^2,3. Treadmilling of FtsZ is thought to actively move proteins around the division septum, thereby distributing peptidoglycan synthesis and coordinating the inward growth of the septum to form the new poles of the daughter cells⁴. However, the molecular mechanisms underlying this function are largely unknown. Here, to study how FtsZ polymerization dyn

SUBMITTER: Baranova N 

PROVIDER: S-EPMC7048620 | biostudies-literature | 2020 Mar

REPOSITORIES: biostudies-literature