INHIBITION OF PEPTIDOGLYCAN HYDROLASE ACTIVITY IN-VIVO AND IN-VITRO BY ENERGY UNCOUPLERS IN ESCHERICHIA-COLI

The effects of energy uncouplers on in vivo and in vitro peptidoglycan hydrolase activities in Escherichia coil were determined, Sodium azid e, potassium cyanide, and carbonyl cyanide m-chlorophenylhydrazone all inhibited ampicillin-induced lysis of exponential phase cultures, eve n when they were added to lysis-committed cultures, These energy uncou plers also inhibited the solubilization of radiolabeled peptidoglycan by bacterial suspensions that had been treated with 5% trichloroacetic acid by the method of Hartmann et al.(3) to activate the peptidoglyca n hydrolases, Therefore, the in vivo and in vitro activities of peptid oglycan hydrolases in E, coil are dependent on membrane energization.