Effect of membrane-associated f1 bacteriophage coat protein upon the activity of Escherichia coli phosphatidylserine synthetase.
The effects of insertion of the major coat protein of f1 bacteriophage into Escherichia coli membranes were investigated under conditions allowing in vivo analysis of phosphatidylserine synthesis. An E. coli strain possessing a temperature-sensitive phosphatidylserine decarboxylase was utilized under conditions in which the decarboxylase activity was reduced but nonlethal. The presence of the coat protein in the host membranes inhibits the activity of the phosphatidylserine synthetase and perhaps affects the activity of the phosphatidylserine decarboxylase.
D010717:CDPdiacylglycerol-Serine O-Phosphatidyltransferase / Q000378:metabolism*; D002262:Carboxy-Lyases / Q000378:metabolism; D003090:Coliphages; D004926:Escherichia coli / Q000201:enzymology*; D010714:Phosphatidylethanolamines / Q000096:biosynthesis; D010715:Phosphatidylglycerols / Q000378:metabolism; D010718:Phosphatidylserines / Q000096:biosynthesis; D010743:Phospholipids / Q000378:metabolism; D010770:Phosphotransferases / Q000378:metabolism*; D014764:Viral Proteins / Q000494:pharmacology / Q000502:physiology*
D010714:Phosphatidylethanolamines; D010715:Phosphatidylglycerols; D010718:Phosphatidylserines; D010743:Phospholipids; D014764:Viral Proteins; D010770:Phosphotransferases; D010717:CDPdiacylglycerol-Serine O-Phosphatidyltransferase; D002262:Carboxy-Lyases