Lipid requirements of the plasma membrane ATPases from oat roots and yeast

The lipid specificity of the plasma membrane ATPases from oat roots and yeast has been investigated by reconstituting delipidated enzyme with phospholipid vesicles and with micelles of lysophospholipids and other detergents. The plant ATPase is activated by Triton X-100 and by all phospholipid and lysophospholipid species, exhibiting only a slight preference for zwitterionic polar heads (phosphorylcholine and phosphorylethanolamine). No unsaturation is required on the hydrophobic chain. On the other hand, the yeast ATPase requires a negatively charged polar head (with preference for phosphorylglycerol and phosphorylinositol) and an unsaturated hydrophobic chain.