The pleiotropic character of the chain-forming mutant of was found to include leakage of periplasmic enzymes and an abnormal tendency to autolyse. Washed suspensions of cells released murein fragments into the supernatant, and cell extracts from the mutant were richer than those of the wild type in exo-β--acetylglucosaminidase (187% of the wild-type value) and in soluble endopeptidase (256%) activities, but -acetylmuramoylamidase, ,-carboxypeptidase, ,-carboxypeptidase and transglycosylase were not markedly different. When cells were grown in medium containing 0·58 -sucrose, the chains broke up into rods, the ,-carboxypeptidase activity increased about sixfold and ,-carboxypeptidase about twofold. It is suggested that ,-carboxypeptidase is involved in septum splitting. The results suggest that the triggering of autolysis in depends on the alteration of envelope constituents rather than on an enhanced activity of murein hydrolases.


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