Role of the antiparallel double-stranded filament form of FtsA in activating the Escherichia coli divisome.

ABSTRACT: The actin-like FtsA protein is essential for function of the cell division machinery, or divisome, in many bacteria including Escherichia coli. Previous in vitro studies demonstrated that purified wild-type FtsA assembles into closed mini-rings on lipid membranes, but oligomeric variants of FtsA such as FtsA^R286W and FtsA^G50E can bypass certain divisome defects and form arc and double-stranded (DS) oligomeric states, respectively, which may reflect conversion of an inactive to an active form of FtsA. Yet, it remains unproven which oligomeric forms of FtsA are responsible for assembling and activating the divisome. Here we used an in vivo crosslinking assay for FtsA DS filaments to show that they largely depend on proper divisome assembly and are p

SUBMITTER: Perkins A 

PROVIDER: S-EPMC11230281 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature