ArticlePloS one2014
Functional analysis of the Na+,K+/H+ antiporter PeNHX3 from the tree halophyte Populus euphratica in yeast by model-guided mutagenesis.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Lithium in plants.The New phytologist · 2025Review
- Structural and Functional Characterization of the Vacuolar-Type NaBiomolecules · 2025Article
- Genome-wide identification and drought stress-induced expression analysis of theFrontiers in genetics · 2024Article
- Structure-Guided Identification of Critical Residues in the Vacuolar Cation/Proton Antiporter NHX1 fromPlants (Basel, Switzerland) · 2023Article
- Halophytes as new model plant species for salt tolerance strategies.Frontiers in plant science · 2023Review
- New Insights into the Structure-Function Relationship of the Endosomal-Type NaInternational journal of molecular sciences · 2020Article
- Distinct Evolutionary Origins of Intron Retention Splicing Events inFrontiers in plant science · 2020Article
- Plant Endomembrane Dynamics: Studies of KPlant physiology · 2018Review
- Article
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Corrections and comments
- Erratum issued
Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Na+,K+/H+ antiporters are H+-coupled cotransporters that are crucial for cellular homeostasis. Populus euphratica, a well-known tree halophyte, contains six Na+/H+ antiporter genes (PeNHX1-6) that have been shown to function in salt tolerance. However, the catalytic mechanisms governing their ion transport remain largely unknown. Using the crystal structure of the Na+/H+ antiporter from the Escherichia coli (EcNhaA) as a template, we built the three-dimensional structure of PeNHX3 from P. euphratica. The PeNHX3 model displays the typical TM4-TM11 assembly that is critical for ion binding and translocation. The PeNHX3 structure follows the 'positive-inside' rule and exhibits a typical physicochemical property of the transporter proteins. Four conserved residues, including Tyr149, Asn187, Asp188, and Arg356, are indentified in the TM4-TM11 assembly region of PeNHX3. Mutagenesis analysis showed that these reserved residues were essential for the function of PeNHX3: Asn187 and Asp188 (forming a ND motif) controlled ion binding and translocation, and Tyr149 and Arg356 compensated helix dipoles in the TM4-TM11 assembly. PeNHX3 mediated Na+, K+ and Li+ transport in a yeast growth assay. Domain-switch analysis shows that TM11 is crucial to Li+ transport. The novel features of PeNHX3 in ion binding and translocation are discussed.
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