Activation of the membrane glucolipid synthesis in Acholeplasma laidlawii by phosphatidylglycerol and other anionic lipids.

In membrane lipids of the prokaryote Acholeplasma laidlawii similar phase equilibria and a nearly constant spontaneous curvature are maintained by an extensive metabolic regulation of especially the major polar lipids monoglucosyldiacylglycerol (MGlcDAG) and diglucosyldiacylglycerol (DGlcDAG), forming nonlamellar and lamellar phases, respectively. A constant surface charge density is maintained by the anionic phospholipid fraction. These lipids are synthesized from phosphatidic acid in two competing pathways. The in vitro synthesis of MGlcDAG and DGlcDAG were totally lost upon delipidation of the membrane proteins by detergent solubilization or solvent extraction of lyophilized cells. Activities were restored by critical concentrations of anionic lipids, but not by bilayer or nonbilayer zwitterionic phospholipids or glucolipids. Phosphatidylglycerol (PG), and to a lesser extent certain other anionic lipids, could activate the synthesis of MGlcDAG in lipid bilayers, whereas the synthesis of DGlcDAG was similarly dependent upon PG only. Two endogenous phosphoglucolipids with no activating potency could partially replace the PG activator for the MGlcDAG synthesis but less so for DGlcDAG formation. A change of inert matrix from phosphatidylcholine to DGlcDAG lowered the apparent cooperativity, but enhanced the efficiency, of activation by PG for both glucolipid synthesizing enzymes, most strongly the synthesis of DGlcDAG. These results indicate that the enzymatic formation of MGlcDAG is regulated by the lipid surface charge density, whereas the consecutive step to DGlcDAG is more dependent upon the specific properties of PG. The modulating effect of the surrounding matrix on the activator efficiencies and cooperativity may constitute part of the bilayer-nonbilayer lipid regulation mechanism.