IDENTIFICATION OF PROTEINS WHOSE AMOUNTS ARE ALTERED BY MUTATION IN THE PGSA GENE OF ESCHERICHIA-COLI

We identified proteins whose amounts were altered in an Escherichia co li pgsA3 mutant lacking the potential to synthesize phosphatidylglycer olphosphate, a precursor of phosphatidylglycerol. Proteins whose amoun ts were increased in the mutant were protease Do, periplasmic oligopep tide-binding protein, tryptophanase, and an unidentified protein, whil e the decreased one was flagellin. Transformation of the mutant with a plasmid containing the wild type pgsA gene complemented the phenotype , indicating that the pgsA3 mutation is responsible for the phenotype.