A multi-layered protein network stabilizes the Escherichia coli FtsZ-ring and modulates constriction dynamics.

ABSTRACT: The prokaryotic tubulin homolog, FtsZ, forms a ring-like structure (FtsZ-ring) at midcell. The FtsZ-ring establishes the division plane and enables the assembly of the macromolecular division machinery (divisome). Although many molecular components of the divisome have been identified and their interactions extensively characterized, the spatial organization of these proteins within the divisome is unclear. Consequently, the physical mechanisms that drive divisome assembly, maintenance, and constriction remain elusive. Here we applied single-molecule based superresolution imaging, combined with genetic and biophysical investigations, to reveal the spatial organization of cellular structures formed by four important divisome proteins in E. coli: FtsZ, ZapA, ZapB and MatP. We show that these

SUBMITTER: Buss J 

PROVIDER: S-EPMC4388696 | biostudies-literature | 2015 Apr

REPOSITORIES: biostudies-literature