Lipid and Temperature Dependence of Membrane-Bound ATPase Activity of Acholeplasma laidlawii

Abstract

Arrhenius plots (15–45 °C) of the ATPase activity of Acholeplasma laidlawii membranes enriched with either arachidoyl or saturated short-chain groups exhibited a pronounced discontinuity in slope around 25–30 °C, absent in oleoyl-enriched membranes. The membrane lipid fluidity was measured with a stearic acid spin label. At the growth temperature (37 °C) the membrane lipid fluidity was identical for all three kinds of enriched membranes. For membranes enriched with saturated acyl chains, a plot of the electron paramagnetic resonance anisotropy parameter 2T11vs. the reciprocal of temperature showed a biphasic profile with a discontinuity in slope around 25–30 °C. For oleoyl-group enriched membranes this plot yields only a straight line between 15 and 50 °C. Thus, lipids do play a role in the functioning of the membrane-bound ATPase. This enzyme is probably localized in the more fluid regions of the membrane.