Mechanism for the Activation of Plasma Membrane H⁺-ATPase from Rice (Oryza sativa L.) Culture Cells by Molecular Species of a Phospholipid

Abstract

The activation of H+-ATPase solubilized from plasma membrane of rice (Oryza sativa L. var Nipponbare) culture cells was examined by the exogenous addition of various phospholipids, free fatty acids, glycerides, polar head groups of phospholipids and molecular species of phosphatidylcholine (PC). H+-ATPase activity appeared to be stimulated by phospholipids in the following order: asolectin > phosphatidylserine > PC > lysophosphatidylcholine > phosphatidylglycerol, and maximal ATPase activation was noted at around 0.05 to 0.03% (w/v) of asolectin or molecular species of PC. Polar head groups such as glycerol, inositol, and serine only slightly activated ATPase activity or not at all, while ethanolamine and choline had no effect. Activation was dependent on the degree of saturation or unsaturation of the fatty acyl chain and its length. The plasma membrane of plant cells contains a H+-ATPase which produces a proton electrochemical gradient across the plasma membrane, thereby providing the driving force for transporting nutrients into cells (19,20). Acidification stimulated by auxin may also cause the loosening required for cell enlargement, suggesting that the plasma membrane H+-ATPase is involved in auxin action (13). The mechanism for regulation of the ATPase by auxin is unknown (17). In our previous paper (10) and other reports (2,3,18), plasma membrane H+-ATPase was shown to require phospholipids for its activation, indicating that its activity may be regulated by interactions between this protein and the phospholipid environment in the plasma membrane. However, the effects

Plant Plasma Membrane H+-ATPase in Adaptation of Plants to Abiotic Stresses

“…The modulation of the phospholipid environment of the plasma membrane regulates the activity of H + -ATPase. This enzyme protein activity was abolished upon the removal of membrane lipids by detergents, but it was restored by exogenous addition of phospholipids (Kasamo & Nouchi, 1987, Kasamo 1990. The activation of H + -ATPase is dependent on the degree of saturation or unsaturation of the fatty acyl chain and its length.…”

Oxidative Stress Results in Increased Sinks for Metabolic Energy during Aging and Sprouting of Potato Seed-Tubers

“…In particular, ATPase activity can be altered by variation in lipid polar head group, fatty acid chain length, and degree of unsaturation (Sinesnsky et al, 1979;Palmgren et al, 1988;Palmgren and Sommarin, 1989;Cooke and Burden, 1990;Kasamo and Yamanishi, 1991). Direct interactions between active sites of the enzyme and hydrophobic environment of the PM (especially fatty acid acyl chains of phospholipids) are important in regulating ATPase activity (Kasamo, 1982(Kasamo, , 1990.…”

Plant lipid environment and membrane enzymes: the case of the plasma membrane H+-ATPase

“…In addition to Brij 58, Lubrol WX or polyethylene glycolmonocetyl ether (HO(CH 2 CH 2 O) n C 16 H 33 ) is another detergent that lacks the inhibitory effect on the ATPase activity at high concentrations (Palmgren et al 1990c) (Table 1), apparently by allowing the ATP access to the catalytic site of the enzyme. Helianthus annuus Memon et al (1989) Oryza sativa Kasamo (1990) Vigna radiata Kasamo and Nouchi (1987) Zea mays Brauer and Tu (1989) Phosphatidylethanolamine (PE) No effect Avena sativa Serrano et al (1988) Oryza sativa Kasamo (1990) Raphanus sativus Coccuci and Marré (1984) Vigna radiata Kasamo and Nouchi (1987), Kasamo and Yamanishi (1991) Zea mays Brauer and Tu (1989) Sterols Cholesterol Stimulation Avena Sativa Cooke et al (1993Cooke et al ( , 1994 Beta vulgaris Oryza sativa Kasamo (1990) Sitosterol Inhibition Avena sativa Cooke et al (1993Cooke et al ( , 1994 Beta vulgaris Another non-ionic detergent, Triton X-100 or polyoxyethylene octyl phenyl ether (C 14 H 22 O (C 2 H 4 O) n ), produced stimulation and then inhibition of the activity in plasma membrane vesicles obtained from Avena sativa (A. sativa). This inhibition was reversible when the surfactant was diluted out (Sandstrom et al 1987) (Table 1).…”

“…No effect Arabidopsis thaliana Gomès et al (1996) Spinacia olerancea Johansson et al (1994) Glycerolipids Asolectin Stimulation Oryza sativa Kasamo (1990) Spinacia olerancea Johansson et al (1994) Vigna radiata Kasamo and Nouchi (1987), Kasamo and Yamanishi (1991) Zea mays Brauer and Tu (1989) Phosphatidylcholine (PC) Stimulation Avena sativa Serrano et al (1988) Oryza sativa Kasamo (1990) Vigna radiata Kasamo and Nouchi (1987), Kasamo and Yamanishi (1991) Phosphatidylglycerol (PG) Stimulation Avena sativa Serrano et al (1988) Oryza sativa Kasamo (1990) Raphanus sativus Coccuci and Marré (1984) Vigna radiata Kasamo and Nouchi (1987), Kasamo and Yamanishi (1991) Zea mays Brauer and Tu (1989) Phosphatidylserine (PS) Stimulation Avena sativa Serrano et al (1988) Oryza sativa Kasamo (1990) Raphanus sativus Coccuci and Marré (1984) Vigna radiata Kasamo and Nouchi (1987), Kasamo and Yamanishi (1991) Zea mays Brauer and Tu (1989) Phosphatidic acid (PA) Stimulation Avena sativa Serrano et al (1988) Zea mays Brauer and Tu (1989) Inhibition Oryza sativa Kasamo (1990) Vigna radiata. Kasamo and Nouchi (1987), Kasamo and Yamanishi (1991) Plant Cell Rep…”