Lipid dependence and activity control of phosphatidylserine synthase from Escherichia coli.
The activity of phosphatidylserine synthase from Escherichia coli depends significantly on the nature and level of the lipids in the matrix, at which the enzyme is operating. To elucidate the role of anionic lipids in the regulation of PtdSer synthase, its activity was studied in mixed micelles containing phosphatidylglycerol (one charge) or diphosphatidylglycerol (two charges), the two main anionic membrane lipids in E. coli. Membrane association and activity of PtdSer synthase were increased by the two lipids, indicating their essential role in the positive regulation mechanism of the phosphatidylethanolamine level in the E. coli membrane.
Linde
Kajsa
K
Department of Biophysical Chemistry, Umeå University, SE-901 87 Umeå, Sweden. kajsa.linde@chem.umu.se
Gröbner
Gerhard
G
Rilfors
Leif
L
D010717:CDPdiacylglycerol-Serine O-Phosphatidyltransferase / Q000378:metabolism*; D002308:Cardiolipins / Q000737:chemistry / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D029968:Escherichia coli Proteins / Q000378:metabolism*; D008563:Membrane Lipids / Q000737:chemistry / Q000378:metabolism; D008823:Micelles; D010715:Phosphatidylglycerols / Q000737:chemistry / Q000378:metabolism*
D002308:Cardiolipins; D029968:Escherichia coli Proteins; D008563:Membrane Lipids; D008823:Micelles; D010715:Phosphatidylglycerols; D010717:CDPdiacylglycerol-Serine O-Phosphatidyltransferase