In vitro peptidoglycan synthesis by envelopes from Escherichia coli tolM mutants is inhibited by colicin M

Abstract

An in vitro peptidoglycan synthesis reaction was employed to further characterize the role of the tolM product in colicin M-induced inhibition of peptidoglycan synthesis. It was found that the tolM product is not the colicin M target and that this gene product does not play a role in the interaction of the colicin with its target. Colicin M remained associated with envelopes prepared from colicin-treated tolM mutants. These findings suggested that the tolM product most likely is involved with the internalization of colicin M.