A Predicted Helix-Turn-Helix Core Is Critical for Bacteriophage Kil Peptide to Disrupt <i>Escherichia coli</i> Cell Division.

ABSTRACT: Background/objectives: FtsZ, a eukaryotic tubulin homolog and an essential component of the bacterial divisome, is the target of numerous antimicrobial compounds as well as proteins and peptides, most of which inhibit FtsZ polymerization dynamics. We previously showed that the Kil peptide from bacteriophage λ inhibits Escherichia coli cell division by disrupting FtsZ ring assembly, and this inhibition requires the presence of the essential FtsZ membrane anchor protein ZipA. Methods: To investigate Kil's molecular mechanism further, we employed deletions, truncations, and molecular modeling to identify the minimal residues necessary for its activity. Results: Modeling suggested that Kil's core segment folds into a helix-turn-helix (HTH) structure. Deleting either

SUBMITTER: Naha A 

PROVIDER: S-EPMC11762379 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature