Domain-switch analysis of PeNHX3 from Populus euphratica reveals the critical role of the transmembrane domain 11 in Na+ and Li+ transport.
Identifieur interne : 001152 ( Main/Corpus ); précédent : 001151; suivant : 001153Domain-switch analysis of PeNHX3 from Populus euphratica reveals the critical role of the transmembrane domain 11 in Na+ and Li+ transport.
Auteurs : Ting Pan ; Yafen Liu ; Xiaomeng Su ; Lizhe An ; Quan-Sheng QiuSource :
- Journal of plant physiology [ 1618-1328 ] ; 2017.
English descriptors
- KwdEn :
- Arabidopsis (genetics), Arabidopsis (physiology), Biological Transport (MeSH), Cation Transport Proteins (genetics), Cation Transport Proteins (metabolism), Gene Expression Regulation, Plant (MeSH), Homeostasis (MeSH), Lithium (metabolism), Plant Proteins (genetics), Plant Proteins (metabolism), Plants, Genetically Modified (genetics), Plants, Genetically Modified (physiology), Populus (genetics), Populus (physiology), Protein Domains (MeSH), Salt Tolerance (MeSH), Sodium (metabolism), Sodium-Hydrogen Exchangers (genetics), Sodium-Hydrogen Exchangers (metabolism).
- MESH :
- chemical , genetics : Cation Transport Proteins, Plant Proteins, Sodium-Hydrogen Exchangers.
- genetics : Arabidopsis, Plants, Genetically Modified, Populus.
- chemical , metabolism : Cation Transport Proteins, Lithium, Plant Proteins, Sodium, Sodium-Hydrogen Exchangers.
- physiology : Arabidopsis, Plants, Genetically Modified, Populus.
- Biological Transport, Gene Expression Regulation, Plant, Homeostasis, Protein Domains, Salt Tolerance.
Abstract
Populus euphratica, the well-known tree halophyte, tolerates the stress of high levels of salt. We previously showed that the transmembrane domain 11 (TM11) of PeNHX3, a Na+,K+/H+ antiporter from P. euphratica, was crucial for Na+ and Li+ transport in a yeast growth assay. Here, we examined the role of TM11 in catalyzing Na+ and Li+ transport in transgenic Arabidopsis. We found that PeNHX3 localized to the tonoplasts in Arabidopsis. Overexpression of PeNHX3 in Arabidopsis improved seedling growth and enhanced salt tolerance and Li+ detoxification. However, overexpression of PeNHX3 did not improve Arabidopsis growth at KCl concentrations higher than 0.1mM, suggesting a low K+ transport activity for PeNHX3 in plants. We performed in planta domain-switch analysis by replacing the C-terminal domain of AtNHX1 with a C-terminal segment of PeNHX3 containing the TM11 domain. We demonstrated that TM11 was critical for the Na+ and Li+ transport activities by PeNHX3. Taken together, PeNHX3 plays an important role in salt tolerance and Li+ detoxification in plants. TM11 controls the Na+ and Li+ transport activities of PeNHX3 in Arabidopsis.
DOI: 10.1016/j.jplph.2017.09.003
PubMed: 28946051
Links to Exploration step
pubmed:28946051Le document en format XML
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<term>Gene Expression Regulation, Plant (MeSH)</term>
<term>Homeostasis (MeSH)</term>
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<term>Populus (physiology)</term>
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<term>Sodium-Hydrogen Exchangers (metabolism)</term>
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<front><div type="abstract" xml:lang="en">Populus euphratica, the well-known tree halophyte, tolerates the stress of high levels of salt. We previously showed that the transmembrane domain 11 (TM11) of PeNHX3, a Na<sup>+</sup>
,K<sup>+</sup>
/H<sup>+</sup>
antiporter from P. euphratica, was crucial for Na<sup>+</sup>
and Li<sup>+</sup>
transport in a yeast growth assay. Here, we examined the role of TM11 in catalyzing Na<sup>+</sup>
and Li<sup>+</sup>
transport in transgenic Arabidopsis. We found that PeNHX3 localized to the tonoplasts in Arabidopsis. Overexpression of PeNHX3 in Arabidopsis improved seedling growth and enhanced salt tolerance and Li<sup>+</sup>
detoxification. However, overexpression of PeNHX3 did not improve Arabidopsis growth at KCl concentrations higher than 0.1mM, suggesting a low K<sup>+</sup>
transport activity for PeNHX3 in plants. We performed in planta domain-switch analysis by replacing the C-terminal domain of AtNHX1 with a C-terminal segment of PeNHX3 containing the TM11 domain. We demonstrated that TM11 was critical for the Na<sup>+</sup>
and Li<sup>+</sup>
transport activities by PeNHX3. Taken together, PeNHX3 plays an important role in salt tolerance and Li<sup>+</sup>
detoxification in plants. TM11 controls the Na<sup>+</sup>
and Li<sup>+</sup>
transport activities of PeNHX3 in Arabidopsis.</div>
</front>
</TEI>
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<Abstract><AbstractText>Populus euphratica, the well-known tree halophyte, tolerates the stress of high levels of salt. We previously showed that the transmembrane domain 11 (TM11) of PeNHX3, a Na<sup>+</sup>
,K<sup>+</sup>
/H<sup>+</sup>
antiporter from P. euphratica, was crucial for Na<sup>+</sup>
and Li<sup>+</sup>
transport in a yeast growth assay. Here, we examined the role of TM11 in catalyzing Na<sup>+</sup>
and Li<sup>+</sup>
transport in transgenic Arabidopsis. We found that PeNHX3 localized to the tonoplasts in Arabidopsis. Overexpression of PeNHX3 in Arabidopsis improved seedling growth and enhanced salt tolerance and Li<sup>+</sup>
detoxification. However, overexpression of PeNHX3 did not improve Arabidopsis growth at KCl concentrations higher than 0.1mM, suggesting a low K<sup>+</sup>
transport activity for PeNHX3 in plants. We performed in planta domain-switch analysis by replacing the C-terminal domain of AtNHX1 with a C-terminal segment of PeNHX3 containing the TM11 domain. We demonstrated that TM11 was critical for the Na<sup>+</sup>
and Li<sup>+</sup>
transport activities by PeNHX3. Taken together, PeNHX3 plays an important role in salt tolerance and Li<sup>+</sup>
detoxification in plants. TM11 controls the Na<sup>+</sup>
and Li<sup>+</sup>
transport activities of PeNHX3 in Arabidopsis.</AbstractText>
<CopyrightInformation>Copyright © 2017 Elsevier GmbH. All rights reserved.</CopyrightInformation>
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