Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes.

ABSTRACT: Virtually all integral outer membrane proteins (OMPs) produced by Gram-negative bacteria contain a unique 'β barrel' structure that serves as a membrane spanning domain. The universal barrel assembly machine (BAM) catalyzes OMP assembly (folding and membrane insertion) in vivo, and purified Escherichia coli BAM that is reconstituted into proteoliposomes catalyzes OMP assembly in vitro. Here we show that BAM also catalyzes the assembly of OMPs into outer membrane fractions ('native OMs') that are purified by optimized conventional methods. Interestingly, we found that OMP assembly was moderately impaired when native OMs were isolated from a mlaA^- strain that is deficient in maintaining OM lipid homeostasis but was strongly reduced when native OMs were isolated from a pldA^-</

SUBMITTER: Nilaweera TD 

PROVIDER: S-EPMC12923597 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature