ArticleThe Journal of biological chemistry2011
PvAMT1;1, a highly selective ammonium transporter that functions as H+/NH4(+) symporter.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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33 citing papers in PubMed.
- Reciprocal co-regulation of nitrate and ammonium transporters is modulated by external pH in Arabidopsis.Journal of experimental botany · 2026Article
- Genome-wide analysis of the ammonium transporters gene family in Phaseolus vulgaris and its roles in response to drought and salinity stress.Scientific reports · 2025Article
- Association betweenFrontiers in medicine · 2025Article
- Functional crosstalk between nitrate and ammonium transporters in N acquisition and pH homeostasis.Frontiers in plant science · 2025Review
- Physiological, molecular, and environmental insights into plant nitrogen uptake, and metabolism under abiotic stresses.The plant genome · 2024Review
- Biological ammonium transporters from the Amt/Mep/Rh superfamily: mechanism, energetics, and technical limitations.Bioscience reports · 2024Review
- Review
- Regulation of Cytosolic pH: The Contributions of Plant Plasma Membrane HInternational journal of molecular sciences · 2021Review
- Integrated Physiological, Transcriptomic, and Metabolomic Analyses Revealed Molecular Mechanism for Salt Resistance in Soybean Roots.International journal of molecular sciences · 2021Article
- Combined Transcriptome and Proteome Analysis of Masson Pine (International journal of molecular sciences · 2020Article
- Plant nitrogen uptake and assimilation: regulation of cellular pH homeostasis.Journal of experimental botany · 2020Review
- Function and Regulation of Ammonium Transporters in Plants.International journal of molecular sciences · 2020Review
- Functional and Regulatory Characterization of Three AMTs in Maize Roots.Frontiers in plant science · 2020Article
- Functional Characterization of theFrontiers in plant science · 2020Article
- The plant defensin gene AtPDF2.1 mediates ammonium metabolism by regulating glutamine synthetase activity in Arabidopsis thaliana.BMC plant biology · 2019Article
- Complex Gene Regulation Underlying Mineral Nutrient Homeostasis in Soybean Root Response to Acidity Stress.Genes · 2019Article
- NOEnvironmental science and pollution research international · 2018Article
- Gene characterization and transcription analysis of two new ammonium transporters in pear rootstock (Pyrus betulaefolia).Journal of plant research · 2016Article
- Nitrogen Source and External Medium pH Interaction Differentially Affects Root and Shoot Metabolism in Arabidopsis.Frontiers in plant science · 2016Article
- Evolution of Electrogenic Ammonium Transporters (AMTs).Frontiers in plant science · 2016Article
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4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
One of the main forms of nitrogen assimilated by microorganisms and plants is ammonium, despite its toxicity at low millimolar concentrations. Ammonium absorption has been demonstrated to be carried out by highly selective plasma membrane-located transporters of the AMT/MEP/Rh family and characterized by the presence of a well conserved hydrophobic pore through which ammonia is proposed to move. However, uncertainties exist regarding the exact chemical species transported by these membrane proteins, which can be in the form of either hydrophobic ammonia or charged ammonium. Here, we present the characterization of PvAMT1;1 from the common bean and demonstrate that it mediates the high affinity (micromolar), rapidly saturating (1 mM) electrogenic transport of ammonium. Activity of the transporter is enhanced by low extracellular pH, and associated with this acidic pH stimulation are changes in the reversal potential and cytoplasm acidification, indicating that PvAMT1;1 functions as an H(+)/NH(4)(+) symporter. Mutation analysis of a unique histidine present in PvAMT1;1 (H125R) leads to the stimulation of ammonium transport by decreasing the K(m) value by half and by increasing the V(max) 3-fold, without affecting the pH dependence of the symporter. In contrast, mutation of the first conserved histidine within the channel modifies the properties of PvAMT1;1, increasing its K(m) and V(max) values and transforming it into a pH-independent mechanism.
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