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Arabidopsis sodium dependent and independent phenotypes triggered by H⁺-PPase up-regulation are SOS1 dependent.

Plant science : an international journal of experimental plant biology (2011-12-27)
Soledad F Undurraga, Mirella P Santos, Julio Paez-Valencia, Haibing Yang, Peter K Hepler, Arnoldo R Facanha, Kendal D Hirschi, Roberto A Gaxiola
RESUMEN

Coordinate regulation of transporters at both the plasma membrane and vacuole contribute to plant cell's ability to adapt to a changing environment and play a key role in the maintenance of the chemiosmotic circuits required for cellular growth. The plasma membrane (PM) Na⁺/H⁺ antiporter (SOS1) is involved in salt tolerance, presumably in sodium extrusion; the vacuolar type I H⁺-PPase AVP1 is involved in vacuolar sodium sequestration, but its overexpression has also been shown to alter the abundance and activity of the PM H⁺-ATPase. Here we investigate the relationship between these transporters utilizing loss-of-function mutants of SOS1 (sos1) and increased expression of AVP1 (AVP1OX). Heightened expression of AVP1 enhances pyrophosphate-dependent proton pump activity, salt tolerance, ion vacuolar sequestration, K⁺ uptake capacity, root hair development, osmotic responses, and PM ATPase hydrolytic and proton pumping activities. In sos1 lines overexpressing AVP1, these phenotypes are negatively affected demonstrating that sos1 is epistatic to AVP1. Enhanced AVP1 protein levels require SOS1 and this regulation appears to be post-translational.

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Sigma-Aldrich
Pyrophosphatase, Inorganic from baker′s yeast (S. cerevisiae), powder, ≥500 units/mg protein (E1%/280)
Sigma-Aldrich
Pyrophosphatase, Inorganic from Escherichia coli, recombinant, expressed in E. coli, lyophilized powder, ≥90%, ≥800 units/mg protein