Engineering drought -resistant crop plants is a critically important objective. Overexpression of the vacuolar H ؉ -pyrophosphatase (H ؉ -PPase) AVP1 in the model plant Arabidopsis thaliana results in enhanced performance under soil water deficits. Recent work demonstrates that AVP1 plays an important role in root development through the facilitation of auxin fluxes. With the objective of improving crop performance, we expressed AVP1 in a commercial cultivar of tomato. This approach resulted in (i) greater pyrophosphate-driven cation transport into root vacuolar fractions, (ii) increased root biomass, and (iii) enhanced recovery of plants from an episode of soil water deficit stress. More robust root systems allowed transgenic tomato plants to take up greater amounts of water during the imposed water deficit stress, resulting in a more favorable plant water status and less injury. This study documents a general strategy for improving drought resistance of crops.root development ͉ biotechnology ͉ water deficit stress ͉ tomato

The vacuolar sequestration of metals is an important metal tolerance mechanism in plants. The Arabidopsis thaliana vacuolar transporters CAX1 and CAX2 were originally identified in a Saccharomyces cerevisiae suppression screen as Ca2+/H+ antiporters. CAX2 has a low affinity for Ca2+ but can transport other metals including Mn2+ and Cd2+. Here we demonstrate that unlike cax1 mutants, CAX2 insertional mutants caused no discernable morphological phenotypes or alterations in Ca2+/H+ antiport activity. However, cax2 lines exhibited a reduction in vacuolar Mn2+/H+ antiport and, like cax1 mutants, reduced V-type H+ -ATPase (V-ATPase) activity. Analysis of a CAX2 promoter beta-glucoronidase (GUS) reporter gene fusion confirmed that CAX2 was expressed throughout the plant and strongly expressed in flower tissue, vascular tissue and in the apical meristem of young plants. Heterologous expression in yeast identified an N-terminal regulatory region in CAX2, suggesting that Arabidopsis contains multiple cation/H+ antiporters with shared regulatory features. Furthermore, despite significant variations in morphological and biochemical phenotypes, cax1 and cax2 lines both significantly alter V-ATPase activity, hinting at coordinate regulation among transporters driven by H+ gradients and the V-ATPase.