http://purl.uniprot.org/citations/15122033 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/15122033 | http://www.w3.org/2000/01/rdf-schema#comment | "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 +/-6.0 centimorgans on chromosome 5. Although P concentrations were not altered in pup1 and pup3 tissues when grown in nutrient solution in which Pi was the sole source of P, the mutants had 10% (pup1) and 17% (pup3) lower shoot P concentrations when grown in a peat-vermiculite mix in which the majority of the total P was present as organic P. Therefore, the pup defects, which include secreted APases, are functionally important for plant P nutrition."xsd:string |
http://purl.uniprot.org/citations/15122033 | http://purl.org/dc/terms/identifier | "doi:10.1104/pp.103.036459"xsd:string |
http://purl.uniprot.org/citations/15122033 | http://purl.uniprot.org/core/author | "Deikman J."xsd:string |
http://purl.uniprot.org/citations/15122033 | http://purl.uniprot.org/core/author | "Guiltinan M.J."xsd:string |
http://purl.uniprot.org/citations/15122033 | http://purl.uniprot.org/core/author | "Lynch J.P."xsd:string |
http://purl.uniprot.org/citations/15122033 | http://purl.uniprot.org/core/author | "Trull M.C."xsd:string |
http://purl.uniprot.org/citations/15122033 | http://purl.uniprot.org/core/author | "Tomscha J.L."xsd:string |
http://purl.uniprot.org/citations/15122033 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
http://purl.uniprot.org/citations/15122033 | http://purl.uniprot.org/core/name | "Plant Physiol"xsd:string |
http://purl.uniprot.org/citations/15122033 | http://purl.uniprot.org/core/pages | "334-345"xsd:string |
http://purl.uniprot.org/citations/15122033 | http://purl.uniprot.org/core/title | "Phosphatase under-producer mutants have altered phosphorus relations."xsd:string |
http://purl.uniprot.org/citations/15122033 | http://purl.uniprot.org/core/volume | "135"xsd:string |
http://purl.uniprot.org/citations/15122033 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15122033 |
http://purl.uniprot.org/citations/15122033 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15122033 |
http://purl.uniprot.org/uniprot/Q949Y3#attribution-1639FC8D67CAD3F7F5EFC916C5D74CF1 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/15122033 |
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http://purl.uniprot.org/uniprot/Q9SIV9 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15122033 |