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Free Content Multiple regulatory sites in the C-terminal autoinhibitory domain of the plasma membrane H+-ATPase

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The H+-ATPase activities of root and leaf plasma membranes from tobacco (Nicotiana tabacum) have been characterized with respect to Vmax, Km for ATP, pH dependence and activation involving the C-terminal autoinhibitory domain. With root plasma membranes, addition of lysophosphatidylcholine (lyso-PC) resulted in the expected increase in Vmax, a decrease in Km(ATP), and a shift in pH optimum to a more alkaline pH, typical for activation via the C-terminal inhibitory domain. With leaf plasma membranes, however, Km(ATP) was relatively low and the pH optimum was around pH 7.0 before the addition of lyso-PC and did not change upon addition of the activator, although Vmax increased twofold. Similar results were obtained with the in vivo activator fusicoccin. The results obtained with the leaf plasma membranes show that Vmax may be regulated independently of Km(ATP) and pH optimum, and suggest the presence of at least two regulatory sites within the C-terminal autoinhibitory domain of the H+-ATPase.
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Document Type: Short Communication

Publication date: December 1, 1995

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