Ludewig, Uwe ; Wilken, Stephanie ; Wu, Binghua ; Jost, Wolfgang ; Obrdlik, Petr ; El Bakkoury, Mohamed ; Marini, Anne-Marie ; André, Bruno ; Hamacher, Tanja ; Boles, Eckhard ; Wirén, Nicolaus von ; Frommer, Wolf B. (2003)
Homo- and hetero-oligomerization of ammonium transporter-1 NH4 uniporters.
In: The Journal of biological chemistry, 278 (46)
Artikel, Bibliographie
Kurzbeschreibung (Abstract)
In most organisms, high affinity ammonium uptake is catalyzed by members of the ammonium transporter family (AMT/MEP/Rh). A single point mutation (G458D) in the cytosolic C terminus of the plasma membrane transporter LeAMT1;1 from tomato leads to loss of function, although mutant and wild type proteins show similar localization when expressed in yeast or plant protoplasts. Co-expression of LeAMT1;1 and mutant in Xenopus oocytes inhibited ammonium transport in a dominant negative manner, suggesting homo-oligomerization. In vivo interaction between LeAMT1;1 proteins was confirmed by the split ubiquitin yeast two-hybrid system. LeAMT1;1 is isolated from root membranes as a high molecular mass oligomer, converted to a approximately 35-kDa polypeptide by denaturation. To investigate interactions with the LeAMT1;2 paralog, co-localizing with LeAMT1;1 in root hairs, LeAMT1;2 was characterized as a lower affinity NH4+ uniporter. Co-expression of wild types with the respective G458D/G465D mutants inhibited ammonium transport in a dominant negative manner, supporting the formation of heteromeric complexes in oocytes. Thus, in yeast, oocytes, and plants, ammonium transporters are able to oligomerize, which may be relevant for regulation of ammonium uptake.
| Typ des Eintrags: | Artikel |
|---|---|
| Erschienen: | 2003 |
| Autor(en): | Ludewig, Uwe ; Wilken, Stephanie ; Wu, Binghua ; Jost, Wolfgang ; Obrdlik, Petr ; El Bakkoury, Mohamed ; Marini, Anne-Marie ; André, Bruno ; Hamacher, Tanja ; Boles, Eckhard ; Wirén, Nicolaus von ; Frommer, Wolf B. |
| Art des Eintrags: | Bibliographie |
| Titel: | Homo- and hetero-oligomerization of ammonium transporter-1 NH4 uniporters. |
| Sprache: | Englisch |
| Publikationsjahr: | 2003 |
| Titel der Zeitschrift, Zeitung oder Schriftenreihe: | The Journal of biological chemistry |
| Jahrgang/Volume einer Zeitschrift: | 278 |
| (Heft-)Nummer: | 46 |
| Kurzbeschreibung (Abstract): | In most organisms, high affinity ammonium uptake is catalyzed by members of the ammonium transporter family (AMT/MEP/Rh). A single point mutation (G458D) in the cytosolic C terminus of the plasma membrane transporter LeAMT1;1 from tomato leads to loss of function, although mutant and wild type proteins show similar localization when expressed in yeast or plant protoplasts. Co-expression of LeAMT1;1 and mutant in Xenopus oocytes inhibited ammonium transport in a dominant negative manner, suggesting homo-oligomerization. In vivo interaction between LeAMT1;1 proteins was confirmed by the split ubiquitin yeast two-hybrid system. LeAMT1;1 is isolated from root membranes as a high molecular mass oligomer, converted to a approximately 35-kDa polypeptide by denaturation. To investigate interactions with the LeAMT1;2 paralog, co-localizing with LeAMT1;1 in root hairs, LeAMT1;2 was characterized as a lower affinity NH4+ uniporter. Co-expression of wild types with the respective G458D/G465D mutants inhibited ammonium transport in a dominant negative manner, supporting the formation of heteromeric complexes in oocytes. Thus, in yeast, oocytes, and plants, ammonium transporters are able to oligomerize, which may be relevant for regulation of ammonium uptake. |
| Fachbereich(e)/-gebiet(e): | 10 Fachbereich Biologie ?? fb10_botanik ?? 10 Fachbereich Biologie > Pflanzenernährung und Biomasse |
| Hinterlegungsdatum: | 17 Mär 2010 15:47 |
| Letzte Änderung: | 28 Feb 2022 12:42 |
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