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Plant and Cell Physiology Advance Access published online on March 7, 2005
Plant and Cell Physiology, doi:10.1093/pcp/pci081
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Plant and Cell Physiology 2005 © The Japanese Society of Plant Physiologists (JSPP); all rights reserved.
Received June 11, 2004
Accepted February 25, 2005

Regular Paper

A Putative Function of the Arabidopsis Fe-Phytosiderophore Transporter Homolog AtYSL2 in Fe and Zn Homeostasis

Gabriel Schaaf 1, Adam Schikora 2, Jennifer Häberle 1, Grégory Vert 2, Uwe Ludewig 3, Jean-Francois Briat 2, Catherine Curie 2, and Nicolaus von Wirén 1*

1 Institut für Pflanzenernährung, Universität Hohenheim, D-70593 Stuttgart, Germany
2 Biochimie et Physiologie Moléculaire des Plantes, Centre National de la Recherche Scientifique (Unité Mixte de Recherche 5004)/Institut National de la Recherche Agronomique/Agro-M/Université Montpellier II, 2 place Viala, F-34060 Montpellier cedex 1, France
3 ZMBP-Pflanzenphysiologie, Universität Tübingen, Auf der Morgenstelle 1, D-72076 Tübingen, Germany

* To whom correspondence should be addressed.
Nicolaus von Wirén, E-mail: vonwiren{at}uni-hohenheim.de


  Abstract

Although Arabidopsis thaliana does not produce phytosiderophores under Fe deficiency, it contains eight homologs to the metal-phytosiderophore/metal-nicotianamine transporter ZmYS1 from maize. This study aimed at investigating whether one of the closest Arabidopsis homologs to ZmYS1, AtYSL2, is involved in metal-chelate transport. Northern analysis revealed high expression levels of AtYSL2 in Fe-sufficient or Fe-resupplied roots, while under Fe deficiency transcript levels decreased. Quantitative RT-PCR and analysis of transgenic plants expressing an AtYSL2 promoter::{beta}-glucuronidase gene further allowed the detection of a down-regulated AtYSL2 gene expression under Zn and Fe deficiency. In contrast to ZmYS1, AtYSL2 did not mediate metal-phytosiderophore or metal-nicotianamine transport in yeast mutants defective in Cu or Fe uptake, nor did AtYSL2 mediate Fe(II)-, Fe(III)- or Ni(II)-NA-inducible currents when assayed by two-electrode voltage clamp in Xenopus oocytes. Moreover, truncation of the N-terminus to remove putative phosphorylation sites that might trigger autoinhibition did not confer functionality to AtYSL2. A direct growth comparison of yeast cells transformed with AtYSL2 in two different yeast expression vectors showed that transformation with empty pFL61 repressed growth even under non-limiting Fe supply. We therefore conclude that the yeast complementation assay employed by DiDonato et al. (2004) does not allow the identification of AtYSL2 as a Fe-NA transporter. Transgenic plants expressing an AtYSL2 promoter::{beta}-glucuronidase gene reported expression in root endodermis and pericycle cells facing the meta xylem tubes. Taken together, our investigations support an involvement of AtYSL2 in Fe and Zn homeostasis, although functionality or substrate specificity are likely to differ between AtYSL2 and ZmYS1.


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