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Biochim Biophys Acta. 2000 May 1;1465(1-2):17-36.

Structure, function and regulation of the plant vacuolar H(+)-translocating ATPase.

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Darmstadt University of Technology, Institute of Botany, Schnittspahnstrasse 3-5, D-64287, Darmstadt, Germany.


The plant V-ATPase is a primary-active proton pump present at various components of the endomembrane system. It is assembled by different protein subunits which are located in two major domains, the membrane-integral V(o)-domain and the membrane peripheral V(1)-domain. At the plant vacuole the V-ATPase is responsible for energization of transport of ions and metabolites, and thus the V-ATPase is important as a 'house-keeping' and as a stress response enzyme. It has been shown that transcript and protein amount of the V-ATPase are regulated depending on metabolic conditions indicating that the expression of V-ATPase subunit is highly regulated. Moreover, there is increasing evidence that modulation of the holoenzyme structure might influence V-ATPase activity.

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