The proline-rich antimicrobial peptide Api137 disrupts large ribosomal subunit assembly and induces misfolding.

ABSTRACT: The proline-rich antimicrobial designer peptide Api137 inhibits protein expression in bacteria by binding simultaneously to the ribosomal polypeptide exit tunnel and the release factor (RF), depleting the cellular RF pool and leading to ribosomal arrest at stop codons. This study investigates the additional effect of Api137 on the assembly of ribosomes using an Escherichia coli reporter strain expressing one ribosomal protein per 30S and 50S subunit tagged with mCherry and EGFP, respectively. Separation of cellular extracts derived from cells exposed to Api137 in a sucrose gradient reveals elevated levels of partially assembled and not fully matured precursors of the 50S subunit (pre-50S). High-resolution structures obtained by cryogenic electron microscopy demonstrate that a large proport

SUBMITTER: Lauer SM 

PROVIDER: S-EPMC11723945 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature