FtsZ phosphorylation modulates tail-core binding to tune cell division in Bacillus subtilis.

ABSTRACT: The cell division protein FtsZ contains an intrinsically disordered C-terminal tail whose function remains poorly understood. Here we demonstrate that this tail serves as an autoinhibitory element through intramolecular interaction with FtsZ's globular core. In Bacillus subtilis, we show that FtsZ's tail is phosphorylated at serine 333 by the kinase PrkC during vegetative growth. We establish that the tail binds specifically to the core's C-terminal polymerization surface through a molecular recognition element spanning L330-H337. Using NMR spectroscopy, we reveal that phosphorylation of S333 induces structural collapse of the I334-K335 motif, sequestering these key residues from their binding sites and disrupting the tail-core interaction. Mutations at S333 reduce the critical concentrati

SUBMITTER: Mallard WJ 

PROVIDER: S-EPMC12747378 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature