Membrane binding properties of the cytoskeletal protein bactofilin.

ABSTRACT: Bactofilins are a widespread family of cytoskeletal proteins that are essential for bacterial morphogenesis, chromosome organization, and motility. They assemble into non-polar filaments independently of nucleotides and typically associate with the cytoplasmic membrane. Their membrane interaction is thought to involve a short N-terminal peptide, but the underlying mechanism is unclear. Here, we clarify the complete membrane-targeting sequence (MTS) of the Caulobacter crescentus bactofilin BacA and identify residues critical for its function. Using molecular dynamics simulations, we show that its affinity for membranes arises from hydrophobic residue-driven water exclusion and electrostatic interactions with negatively charged phospholipid headgroups. Bioinformatic analysis suggests

SUBMITTER: Liu Y 

PROVIDER: S-EPMC12448750 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature