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Published on March 14, 2008; 10.1104/pp.108.117820

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Received February 15, 2008
Accepted March 11, 2008

Characterization of an amino acid permease from the endomycorrhizal fungus Glomus mosseae

Gilda Cappellazzo , Luisa Lanfranco *, Michael Fitz , Daniel Wipf , and Paola Bonfante

Dipartimento di Biologia Vegetale, Universita di Torino, Istituto per la Protezione delle Piante, CNR, Viale Mattioli 25, 10125, Torino, Italy; NWG Transport in der Mykorrhiza IZMB - Institut fur Zellulare und Molekulare Botanik Bonn University Bonn, Kirschallee 1 D-53115 Bonn, Germany; UMR INRA 1088/CNRS 5184/Universite de Bourgogne Plante-Microbe-Environnement, F-21000 Dijon Cedex, France

* Corresponding author; email: luisa.lanfranco{at}unito.it.

Arbuscular mycorrhizal (AM) fungi are capable of exploiting organic nitrogen (N) sources, but the molecular mechanisms that control such an uptake are still unknown.

PCR-based approaches, bioinformatic tools and a heterologous expression system have been used to characterize a sequence coding for an amino acid permease (GmosAAP1) from the AM fungus Glomus mosseae. The GmosAAP1 shows primary and secondary structures that are similar to other fungal amino acid permeases. Functional complementation and uptake experiments in a yeast mutant that was defective in the multiple amino acid uptake system demonstrated that GmosAAP1 is able to transport proline through a proton coupled, pH and energy dependent process. A competitive test showed that GmosAAP1 binds non polar and hydrophobic amino acids thus indicating a relatively specific substrate spectrum. GmosAAP1 mRNAs were detected in the extraradical fungal structures. Transcript abundance was increased upon exposure to organic N, in particular when supplied at 2 mM concentrations.

These findings suggest that GmosAAP1 plays a role in the first steps of amino acid acquisition, allowing direct amino acid uptake from the soil and extending the molecular tools thanks to which AM fungi exploit soil resources.






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