Minimization of the Bacillus subtilis divisome suggests FtsZ and SepF can form an active Z-ring, and reveals the amino acid transporter BraB as a new cell division influencing factor.

ABSTRACT: Bacterial cytokinesis begins with polymerization of the tubulin homologue FtsZ into a ring-like structure at midcell, the Z-ring, which recruits the late cell division proteins that synthesize the division septum. Assembly of FtsZ is carefully regulated and supported by a dozen conserved cell division proteins. Generally, these proteins are not essential, but removing more than one is in many cases lethal. Therefore, it is still not fully clear how the different protein components contribute to cell division, and whether there is a minimal set of proteins that can execute cell division. In this study, we tried to find the minimal set of proteins that is required to establish an active Z-ring in the model bacterium Bacillus subtilis. By making use of known suppressor mutations we were able

SUBMITTER: Gulsoy IC 

PROVIDER: S-EPMC11790237 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature