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Domain-switch analysis of PeNHX3 from Populus euphratica reveals the critical role of the transmembrane domain 11 in Na+ and Li+ transport.

Identifieur interne : 001432 ( Main/Exploration ); précédent : 001431; suivant : 001433

Domain-switch analysis of PeNHX3 from Populus euphratica reveals the critical role of the transmembrane domain 11 in Na+ and Li+ transport.

Auteurs : Ting Pan [République populaire de Chine] ; Yafen Liu [République populaire de Chine] ; Xiaomeng Su [République populaire de Chine] ; Lizhe An [République populaire de Chine] ; Quan-Sheng Qiu [République populaire de Chine]

Source :

RBID : pubmed:28946051

Descripteurs français

English descriptors

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


Affiliations:


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Le document en format XML

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<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>
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<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>
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