Structure, function and regulation of the plant vacuolar H(+)-translocating ATPase.
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.
Ratajczak
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Darmstadt University of Technology, Institute of Botany, Schnittspahnstrasse 3-5, D-64287, Darmstadt, Germany. ratajczak@bio.tu-darmstadt.de
D004789:Enzyme Activation; D015971:Gene Expression Regulation, Enzymologic; D018506:Gene Expression Regulation, Plant; D008565:Membrane Proteins / Q000737:chemistry / Q000378:metabolism*; D010940:Plant Proteins / Q000737:chemistry / Q000378:metabolism*; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*
D008565:Membrane Proteins; D010940:Plant Proteins; D006180:Proton-Translocating ATPases