Dimerization or oligomerization of the actin-like FtsA protein enhances the integrity of the cytokinetic Z ring.

ABSTRACT: In bacteria, the actin-like FtsA protein interacts with the tubulin-like FtsZ protein, helping to assemble the cytokinetic Z ring, anchor it to the cytoplasmic membrane and recruit other essential divisome proteins. FtsA also interacts with itself, but it is not clear whether this self-interaction is required for its full functionality. Here we describe new dominant negative missense mutations in Escherichia coli ftsA that specifically inhibit FtsA homodimerization and simultaneously cause disruption of Z rings. The negative effects of one mutation, M71A, were suppressed by altering levels of certain division proteins or by additional mutations in ftsA that promote increased integrity of the Z ring. Remarkably, when FtsA, FtsA-M71A, and other mutants of FtsA that compromise self-interactio

SUBMITTER: Shiomi D 

PROVIDER: S-EPMC4764085 | biostudies-literature | 2007 Dec

REPOSITORIES: biostudies-literature