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Plant Physiology Preview Published on April 30, 2004; 10.1104/pp.103.036459
Received November 20, 2003 Phosphatase Under-Producer Mutants Have Altered Phosphorus Relations
Intercollege Program in Plant Physiology (J.L.T., J.D., J.P.L., M.J.G.), Department of Biology (M.C.T., J.D., M.J.G.), and Department of Horticulture (J.P.L., M.J.G.), Penn State University, University Park, Pennsylvania 16802 * Corresponding author; email: tomscha{at}email.unc.edu.
Phosphorus (P) acquisition and partitioning are essential for plant homeostasis. P is available for plant uptake when in its inorganic form (H2PO4
-, or Pi), but Pi is often limiting in soils. Plants secrete acid phosphatases (APases) into the apoplastic space, which may be important for obtaining Pi from organic P sources; however, the relative importance of these enzymes for plant P nutrition has yet to be determined. We demonstrate that the root-associated APase pool is increased in Arabidopsis when Pi is limiting and document five APase isoforms secreted from Arabidopsis roots. Previously, we presented the identification of the phosphatase under-producer (pup) mutants, which have decreased in vivo root APase staining when grown under low P conditions. Here, we present the characterization of one of these, pup3, and further studies with pup1. pup3 has 49%, 38%, and 37% less specific APase activity in exudates, roots, and shoots, respectively. Root-associated APase activity is decreased by 16% in pup1 and 25% in pup3, regardless of P treatment. Two APase activity isoforms are reduced in pup3 exudates, and root and shoot isoforms are also affected. One of the two exudate isoforms is recognized by a polyclonal antibody raised to an Arabidopsis purple APase recombinant protein (AtPAP12); however, AtPAP12 transcript levels are unaffected in the mutant. The pup3 mutation was mapped to 68.4
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