Specific inhibition of phospholipid synthesis in plsA mutants of Escherichia coli

plsA mutants of E. coli are temperature sensitive strains which possess two enzymes of abnormal thermolability, sn glycerol 3 phosphate acyltransferase and adenylate kinase. Phospholipid synthesis is inhibited after shift of plsA mutants to temperatures at the lower end of the nonpermisive temperature range. This inhibition is not due to inactivation of the adenylate kinase activity since nucleic acid (and hence adenosine 5' triphosphate) synthesis in inhibited only slightly. These results show that in vivo inactivation of the sn glycerol 3 phosphate acyltransferase can be observed under conditions which allow normal adenylate kinase function.