A novel superfamily of transporters for allantoin and other oxo derivatives of nitrogen heterocyclic compounds in Arabidopsis

• Verfasst von: Desimone, Marcelo [VerfasserIn]
• Verfasst von: Catoni, Elisabetta [VerfasserIn]
• Verfasst von: Ludewig, Uwe [VerfasserIn]
• Verfasst von: Hilpert, Melanie [VerfasserIn]
• Verfasst von: Schneider, Anja [VerfasserIn]
• Verfasst von: Kunze, Reinhard [VerfasserIn]
• Verfasst von: Tegeder, Mechthild [VerfasserIn]
• Verfasst von: Frommer, Wolf Bernd [VerfasserIn]
• Verfasst von: Schumacher, Karin [VerfasserIn]
• Titel: A novel superfamily of transporters for allantoin and other oxo derivatives of nitrogen heterocyclic compounds in Arabidopsis
• Verf.angabe: Marcelo Desimone, Elisabetta Catoni, Uwe Ludewig, Melanie Hilpert, Anja Schneider, Reinhard Kunze, Mechthild Tegeder, Wolf Bernd Frommer, and Karin Schumacher
• E-Jahr: 2002
• Jahr: 01 April 2002
• Umfang: 10 S.
• Fussnoten: Gesehen am 07.10.2021
• Titel Quelle: Enthalten in: The plant cell
• Ort Quelle: Rockville, Md. : Soc., 1989
• Jahr Quelle: 2002
• Band/Heft Quelle: 14(2002), 4 vom: Apr., Seite 847-856
• ISSN Quelle: 1532-298X
• DOI: doi:10.1105/tpc.010458
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1772781517

Abstract

A wide spectrum of soil heterocyclic nitrogen compounds are potential nutrients for plants. Here, it is shown that Arabidopsis plants are able to use allantoin as sole nitrogen source. By functional complementation of a yeast mutant defective in allantoin uptake, an Arabidopsis transporter, AtUPS1 (Arabidopsis thaliana ureide permease 1), was identified. AtUPS1 belongs to a novel superfamily of plant membrane proteins with five open reading frames in Arabidopsis (identity, 64 to 82%). UPS proteins have 10 putative transmembrane domains with a large cytosolic central domain containing a “Walker A” motif. Transport of 14C-labeled allantoin by AtUPS1 in yeast exhibited saturation kinetics (K m ∼ 52 μM), was dependent on Glc and a proton gradient, and was stimulated by acidic pH. AtUPS1 transports uric acid and xanthine, besides allantoin, but not adenine. Protons are cosubstrates in allantoin transport by AtUPS1, as demonstrated by expression in Xenopus laevis oocytes. In plants, AtUPS1 gene expression was dependent on the nitrogen source. Therefore, AtUPS1 presumably is involved in the uptake of allantoin and other purine degradation products when primary sources are limiting.