The Plasma Membrane ATPase of Dunaliella parva

Plasma membrane Mg2+, Ca2+ ATPases were isolated from Dunaliella parva by differential centrifugation and subsequent sucrose gradient centrifugation and analyzed for their properties with special emphasis on ecophysiological requirements of this extremely salt-tolerant alga. Most properties (Vmax- and KM-values, substrate specificity, vanadate and DES sensitivity, resistance against ouabain) indicate that the ATPases of the plasma membrane of D. parva are basically of the same type as that found in the plasma membrane of other algae or higher plants. However, some interesting deviations from the normal characteristics of plasma membrane ATPases of plants were observed for the Dunaliella ATPases. These modifications partially may reflect adaptations of the ATPase and/or the microenvironment of the ATPase to the highly saline environment of this alga; 1) The plasma membrane ATPase of D. parva requires unusually high concentrations of divalent cations (up to 100 mM Mg2+ or Ca2+) for maximal activity. Both cations can substitute for each other. 2) The plasma membrane ATPase of D. parva is extremely resistant against salt. It was stimulated by NaCl or KC1 at concentrations up to 800 mM , whereas at higher salt concentrations the enzyme was inhibited. However, about 2.5 M NaCl was required for halfmaximal inhibition of ATPase activity. 3) The ATPase was inhibited by inhibitors of anion transport such as SITS and D ID S . which suggests direct or indirect involvement of ATPase in anion transport. The possible functions of the plasma membrane ATPases are discussed with special emphasis on problems related to the hypersaline environment of this alga.