Specific inhibition of phospholipid synthesis in plsA mutants of Escherichia coli.
plsA mutants of Escherichia 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 nonpermissive temperature range. This inhibition is not due to inactivation of the adenylate kinase activity since nucleic acid (and hence adenosine 5'-triphosphate) synthesis is 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.
D000217:Acyltransferases / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000096:biosynthesis; D000263:Adenylate Kinase / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology / Q000378:metabolism*; D005992:Glycerol-3-Phosphate O-Acyltransferase / Q000378:metabolism*; D009154:Mutation; D009696:Nucleic Acids / Q000096:biosynthesis; D010743:Phospholipids / Q000096:biosynthesis*; D010770:Phosphotransferases / Q000378:metabolism*; D013696:Temperature
D009696:Nucleic Acids; D010743:Phospholipids; D000255:Adenosine Triphosphate; D000217:Acyltransferases; D005992:Glycerol-3-Phosphate O-Acyltransferase; D010770:Phosphotransferases; D000263:Adenylate Kinase