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The archaeal and the vacuolar ATPase are both homologous to the bacterial F-ATPases, but the level of sequence similarity with the F-ATPases is much lower than between the V- and the A-ATPases.
Fully expanded leaves exhibited an increase only for the proteolipid mRNA, an increase of approximately three fold over non salt stressed plants [ 54 ] . Cell suspension cultures when subjected to salt stress exhibited increase in activity of both P-Type and V-Type ATPases without concomitant increase in protein levels [ 55 ] . Transcript levels of subunit E of the V-ATPase in Mesembryanthemum crystallinum were recently shown to increase in leaves but not roots of salt stressed plants with a concomitant increase in protein levels in leaves [ 56 ] . On the other hand, subunit E in Hordeum vulgare showed no effect on mRNA level in response to salt stress [ 57 ] . The effects of salt stress on V-ATPases has also been investigated in tobacco ( Nicotiana tabacum ) suspension cells.
In plant cells V-ATPases are responsible for the deacidification of the cytosol and the energization of secondary transport processes across the tonoplast, as well as in the endocytotic and secretory pathways [ 12 ] . In addition, the vacuolar type ATPase is thought to be primarily responsible for the acidification and expansion of the large central vacuole [ 12 13 14 15 ] . In plants a critical event in growth and development is the maturation and expansion of the central vacuole.
The structure of the bovine mitochondrial F 1 -ATPase has been determined by X-ray crystallography [ 30 ] . The intein insertion points in the yeasts' V-ATPase and the Thermoplasma and Pyrococcus A-ATPases correspond to the catalytic site where the ATP binds and is hydrolyzed during the catalytic cycle.
The limited work done to evaluate the role of V-ATPases in drought stress has provided conflicting results.
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