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The Plant Cell, Vol. 14, 889-902, April 2002, Copyright © 2002,
American Society of Plant Biologists

Identification and Characterization of the Arabidopsis PHO1 Gene Involved in Phosphate Loading to the Xylem

Dirk Hamburger1,a, Enea Rezzonicoa, Jean MacDonald-Comber Petétota, Chris Somervilleb and Yves Poirier2,a

a Institut d'Écologie-Biologie et Physiologie Végétales, Bâtiment de Biologie, Université de Lausanne, CH-1015 Lausanne, Switzerland
b Carnegie Institution of Washington, 260 Panama Street, Stanford, California 94305

2 To whom correspondence should be addressed. E-mail yves.poirier{at}ie-bpv.unil.ch; fax 41-21-692-4195

The Arabidopsis mutant pho1 is deficient in the transfer of Pi from root epidermal and cortical cells to the xylem. The PHO1 gene was identified by a map-based cloning strategy. The N-terminal half of PHO1 is mainly hydrophilic, whereas the C-terminal half has six potential membrane-spanning domains. PHO1 shows no homology with any characterized solute transporter, including the family of H+-Pi cotransporters identified in plants and fungi. PHO1 shows highest homology with the Rcm1 mammalian receptor for xenotropic murine leukemia retroviruses and with the Saccharomyces cerevisiae Syg1 protein involved in the mating pheromone signal transduction pathway. PHO1 is expressed predominantly in the roots and is upregulated weakly under Pi stress. Studies with PHO1 promoter–{beta}-glucuronidase constructs reveal predominant expression of the PHO1 promoter in the stelar cells of the root and the lower part of the hypocotyl. There also is {beta}-glucuronidase staining of endodermal cells that are adjacent to the protoxylem vessels. The Arabidopsis genome contains 10 additional genes showing homology with PHO1. Thus, PHO1 defines a novel class of proteins involved in ion transport in plants.




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