ArticleFrontiers in plant science2018
Bioinformatic and Functional Analysis of a Key Determinant Underlying the Substrate Selectivity of the Al Transporter, Nrat1.
Article in Frontiers in plant science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 31 citations in OpenAlex.
- Aluminum resistance in plants: A critical review focusing on STOP1.Plant communications · 2025Review
- Systematic Investigation of Aluminum Stress-Related Genes and Their Critical Roles in Plants.International journal of molecular sciences · 2024Review
- Dissecting the Roles of Phosphorus Use Efficiency, Organic Acid Anions, and Aluminum-Responsive Genes under Aluminum Toxicity and Phosphorus Deficiency in Ryegrass Plants.Plants (Basel, Switzerland) · 2024Article
- Engineering rice Nramp5 modifies cadmium and manganese uptake selectivity using yeast assay system.Frontiers in plant science · 2024Article
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- PP2C.D phosphatase SAL1 positively regulates aluminum resistance via restriction of aluminum uptake in rice.Plant physiology · 2023Article
- Article
- Article
- PcNRAMP1 Enhances Cadmium Uptake and Accumulation inInternational journal of molecular sciences · 2022Article
- Research Advances in the Mutual Mechanisms Regulating Response of Plant Roots to Phosphate Deficiency and Aluminum Toxicity.International journal of molecular sciences · 2022Review
- Aluminum in plant: Benefits, toxicity and tolerance mechanisms.Frontiers in plant science · 2022Review
- Molecular Mechanism of Nramp-Family Transition Metal Transport.Journal of molecular biology · 2021Review
- New insights into the response of maize to fluctuations in the light environment.Molecular genetics and genomics : MGG · 2021Article
- Molecular Mechanisms for Coping with Al Toxicity in Plants.International journal of molecular sciences · 2019Review
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nrat1 is a member of the natural resistance-associated macrophage protein (Nramp) family of metal ion transporters in all organisms. Different from other Nramp members capable of transporting divalent metals, Nrat1 specifically transports trivalent aluminum (Al) ion. However, molecular mechanism underlying the Al transport selectivity of Nrat1 remains unknown. Here, we performed structure-function analyses of Nrat1 and other Nramp members to gain insights into the determinants of ion selectivity. A phylogenetic analysis showed that plant Nramp transporters could be divided into five groups. OsNrat1 was found in one of the individual clades and clustered with SbNrat1 and ZmNrat1 on the evolutionary tree. Structural modeling revealed that Nrat1 transporters adopted a common LeuT fold shared by many Nramp-family transporters that likely employed an identical transport mechanism. Sequence alignment and evolutionary conservation analysis of amino acids identified a metal-permeation pathway of Nrat1 centered at the metal binding site. The metal binding site of Nrat1 was characterized by two conserved sequence motifs, i.e., the Asp-Pro-Ser-Asn motif (motif A) and the Ala-Ile-Ile-Thr motif (motif B). Replacement of the Ala-Met-Val-Met motif B of the OsNramp3 manganese (Mn) transporter to that of Nrat1 resulted in a partial gain of Al transport activity and a total loss of Mn in yeast. Conversely, substitution of the motif B of OsNrat1 with that of OsNramp3 altered the Al transport activity. These observations indicated the metal binding site, particularly the motif B, as a key determinant of Al selectivity of Nrat1.
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