Direct Interaction between the Two Z Ring Membrane Anchors FtsA and ZipA.

ABSTRACT: The initiation of Escherichia coli cell division requires three proteins, FtsZ, FtsA, and ZipA, which assemble in a dynamic ring-like structure at midcell. Along with the transmembrane protein ZipA, the actin-like FtsA helps to tether treadmilling polymers of tubulin-like FtsZ to the membrane. In addition to forming homo-oligomers, FtsA and ZipA interact directly with the C-terminal conserved domain of FtsZ. Gain-of-function mutants of FtsA are deficient in forming oligomers and can bypass the need for ZipA, suggesting that ZipA may normally function to disrupt FtsA oligomers, although no direct interaction between FtsA and ZipA has been reported. Here, we use in vivo cross-linking to show that FtsA and ZipA indeed interact directly. We identify the exposed surface of FtsA he

SUBMITTER: Vega DE 

PROVIDER: S-EPMC6351747 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature