Rapid cessation of phospholipid synthesis in fructose-1,6-diphosphate aldolase mutants of Escherichia coli.
Escherichia coli GH352, which was originally described as a temperature-sensitive strain containing a thermolabile acyl coenzyme A:monoacylglycerol 3-phosphate acyltransferase, does not now contain a thermolabile form of this enzyme. It has a defect in fructose-1,6-diphosphate aldolase and at least one additional temperature-sensitive lesion. Both strains GH352 and NP315, a temperature-sensitive aldolase mutant, show rapid cessation of 32-P1 incorporation into nucleic acids and phospholipids at 42 C. These characteristics of strain GH352 are therefore no longer attributed to thermolabile phospholipid synthesis, but can be attributed to the fructose-1,6-diphophate aldolase lesion.
D000217:Acyltransferases / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology*; D005634:Fructose-Bisphosphate Aldolase / Q000378:metabolism*; D005838:Genotype; D006358:Hot Temperature; D009154:Mutation; D010743:Phospholipids / Q000096:biosynthesis*; D010761:Phosphorus Radioisotopes; D013045:Species Specificity
D010743:Phospholipids; D010761:Phosphorus Radioisotopes; D000217:Acyltransferases; D005634:Fructose-Bisphosphate Aldolase