A conserved editing mechanism for the fidelity of bacterial cell wall biosynthesis.

ABSTRACT: Peptidoglycan (PG), a defining feature of the bacterial cell envelope, is crucial for cell integrity and morphology. PG is a macromolecular mesh consisting of glycan polymers crosslinked by short peptides encasing the cytoplasmic membrane. PG peptides contain two to five amino acids of both L- and D-configuration, with a conserved L-alanine residue at the first position in most bacteria. We previously identified a β-lactam hypersensitive mutant of Escherichia coli lacking yfiH (renamed pgeF) that shows incorporation of L-serine or glycine instead of L-alanine. Here, we demonstrate that PgeF is an editing enzyme that imparts fidelity to the biosynthesis of PG peptides across bacterial genera. Using extensive mass spectrometry, we find accumulation of misincorporated cyt

SUBMITTER: Garde S 

PROVIDER: S-EPMC12280929 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature