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Plant and Cell Physiology Advance Access originally published online on December 10, 2008
Plant and Cell Physiology 2009 50(1):13-25; doi:10.1093/pcp/pcn186
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© The Author 2008. Published by Oxford University Press on behalf of Japanese Society of Plant Physiologists. All rights reserved.
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and the Japanese Society of Plant Physiologists are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions@oxfordjournals.org

Special Issue - Regular Paper

AtAMT1;4, a Pollen-Specific High-Affinity Ammonium Transporter of the Plasma Membrane in Arabidopsis

Lixing Yuan1,2, Lucile Graff2, Dominique Loqué2, Soichi Kojima2, Yumiko N. Tsuchiya3, Hideki Takahashi3 and Nicolaus von Wirén2,*

1Department of Plant Nutrition, College of Resources and Environmental Sciences, China Agricultural University, Beijing 100193, PR China
2Molecular Plant Nutrition, Institute of Plant Nutrition, University of Hohenheim, D-70593 Stuttgart, Germany
3RIKEN Plant Science Center, Yokohama, 230-0045 Japan

*Corresponding author: E-mail, vonwiren{at}uni-hohenheim.de; Fax, +49-711-45923295.


  Abstract

Pollen represents an important nitrogen sink in flowers to ensure pollen viability. Since pollen cells are symplasmically isolated during maturation and germination, membrane transporters are required for nitrogen import across the pollen plasma membrane. This study describes the characterization of the ammonium transporter AtAMT1;4, a so far uncharacterized member of the Arabidopsis AMT1 family, which is suggested to be involved in transporting ammonium into pollen. The AtAMT1;4 gene encodes a functional ammonium transporter when heterologously expressed in yeast or when overexpressed in Arabidopsis roots. Concentration-dependent analysis of 15N-labeled ammonium influx into roots of AtAMT1;4-transformed plants allowed characterization of AtAMT1;4 as a high-affinity transporter with a Km of 17 µM. RNA and protein gel blot analysis showed expression of AtAMT1;4 in flowers, and promoter–gene fusions to the green fluorescent protein (GFP) further defined its exclusive expression in pollen grains and pollen tubes. The AtAMT1;4 protein appeared to be localized to the plasma membrane as indicated by protein gel blot analysis of plasma membrane-enriched membrane fractions and by visualization of GFP-tagged AtAMT1;4 protein in pollen grains and pollen tubes. However, no phenotype related to pollen function could be observed in a transposon-tagged line, in which AtAMT1;4 expression is disrupted. These results suggest that AtAMT1;4 mediates ammonium uptake across the plasma membrane of pollen to contribute to nitrogen nutrition of pollen via ammonium uptake or retrieval.

Keywords: Ammonium uptake - AMTs - Germination - Nitrogen transport - Pollen - Pollen tube

Abbreviations: AMT/MEP/Rh, ammonium transporter/methylamine permease/rhesus; CaMV, cauliflower mosaic virus; GFP, green fluorescent protein; GUS, β-glucuronidase; MeA, methylammonium; MS, Murashige and Skoog; ORF, open reading frame; V-ATPase, vauolar ATPase; VPPase, vacuolar pyrophosphatase.

(Received October 14, 2008; Accepted November 27, 2008)
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