Ammonium Ion Transport by the Amt/Rh Homologue Leamt1;1.
From: Zentrum für Molekularbiologie der Pflanzen (ZMBP), Pflanzenphysiologie, Universität Tübingen, Auf der Morgenstelle 1, 72076 Tübingen, Germany.
The Biochemical journal
- Publish Date: Jun 2006
- ISSN: 1470-8728
- Volume: 396
- Issue: 3
- Pages: 431-7
- Medium: Internet
- Language: English
- Citation (JAMA): Mayer Maria, Dynowski Marek, Ludewig Uwe, et al. Ammonium Ion Transport by the Amt/Rh Homologue Leamt1;1.. Biochem. J. Jun 2006;396:431-7
Abstract
AMT (ammonium transporter)/Rh (Rhesus) ammonium transporters/channels are identified in all domains of life and fulfil contrasting functions related either to ammonium acquisition or excretion. Based on functional and crystallographic high-resolution structural data, it was recently proposed that the bacterial AmtB (ammonium transporter B) is a gas channel for NH3 [Khademi, O’Connell, III, Remis, Robles-Colmenares, Miercke and Stroud (2004) Science 305, 1587-1594; Zheng, Kostrewa, Berneche, Winkler and Li (2004) Proc. Natl. Acad. Sci. U.S.A. 101, 17090-17095]. Key residues, proposed to be crucial for NH3 conduction, and the hydrophobic, but obstructed, pore were conserved in a homology model of LeAMT1;1 from tomato. Transport by LeAMT1;1 was affected by mutations of residues that were predicted to constitute the aromatic recruitment site for NH4+ at the external pore entrance. Despite the structural similarities, LeAMT1;1 was shown to transport only the ion; each transported 14C-methylammonium molecule carried a single positive elementary charge. Similarly, NH4+ (or H+/NH3) was transported, but NH3 conduction was excluded. It is concluded that related proteins and a similar molecular architecture can apparently support contrasting transport mechanisms.
Mesh Headings (Keywords): Animals, Cation Transport Proteins, Female, Methylamines, Mutation, Oocytes, Plant Proteins, Quaternary Ammonium Compounds, Xenopus
Check for Full Text / PubMed Unique Identifier (PMID): 16499477
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