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

Journal

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1465, Issue 1-2, Pages 17-36

Publisher

ELSEVIER
DOI: 10.1016/S0005-2736(00)00129-2

Keywords

ATP hydrolysis; gene expression; holoenzyme structure; proton transport; subunit composition; V-ATPase

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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, (C) 2000 Elsevier Science B.V. All rights reserved.

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