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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 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.
The limited work done to evaluate the role of V-ATPases in drought stress has provided conflicting results.
These isoforms may be required to provide unique functions or regulatory constraints within the varied micro-compartments requiring V-ATPases [ 26 27 34 39 43 ] . In addition, different isoforms may be responsible for targeting to varied subcellular compartments [ 10 26 28 36 41 44 47 ] . Furthermore, it is possible that gene family members may behave in a differential manner with respect to environmental stress [ 36 ] .
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.
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