Dataset Information

Cloning and characterization of a novel vacuolar Na+/H+ antiporter gene (Dgnhx1) from chrysanthemum.

ABSTRACT: Plant vacuolar Na(+)/H(+) antiporter genes play significant roles in salt tolerance. However, the roles of the chrysanthemum vacuolar Na(+)/H(+) antiporter genes in salt stress response remain obscure. In this study, we isolated and characterized a novel vacuolar Na(+)/H(+) antiporter gene DgNHX1 from chrysanthemum. The DgNHX1 sequence contained 1920 bp with a complete open reading frame of 1533 bp encoding a putative protein of 510 amino acids with a predicted protein molecular weight of 56.3 kDa. DgNHX1 was predicted containing nine transmembrane domains. Its expression in the chrysanthemum was up-regulated by salt stress, but not by abscisic acid (ABA). To assess roles of DgNHX1 in plant salt stress responses, we performed gain-of-function experiment. The DgNHX1-overexpression tobacco plants showed significant salt tolerance than the wild type (WT). The transgenic lines exhibited more accumulation of Na(+) and K(+) under salt stress. These findings suggest that DgNHX1 plays a positive regulatory role in salt stress response.

SUBMITTER: Liu QL

PROVIDER: S-EPMC3869812 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Cloning and characterization of a novel vacuolar Na+/H+ antiporter gene (Dgnhx1) from chrysanthemum.

Liu Qing-Lin QL Xu Ke-Dong KD Zhong Ming M Pan Yuan-Zhi YZ Jiang Bei-Bei BB Liu Guang-Li GL Jia Yin Y

PloS one 20131220 12

Plant vacuolar Na(+)/H(+) antiporter genes play significant roles in salt tolerance. However, the roles of the chrysanthemum vacuolar Na(+)/H(+) antiporter genes in salt stress response remain obscure. In this study, we isolated and characterized a novel vacuolar Na(+)/H(+) antiporter gene DgNHX1 from chrysanthemum. The DgNHX1 sequence contained 1920 bp with a complete open reading frame of 1533 bp encoding a putative protein of 510 amino acids with a predicted protein molecular weight of 56.3 k ...[more]

PMID: 24376735

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Project description:Na+/H+ antiporters are integral membrane proteins that are present in almost every cell and in every kingdom of life. They are essential for the regulation of intracellular pH-value, Na+-concentration and cell volume. These secondary active transporters exchange sodium ions against protons via an alternating access mechanism, which is not understood in full detail. Na+/H+ antiporters show distinct species-specific transport characteristics and regulatory properties that correlate with respective physiological functions. Here we present the characterization of the Na+/H+ antiporter NhaA from Salmonella enterica serovar Thyphimurium LT2, the causing agent of food-born human gastroenteritis and typhoid like infections. The recombinant antiporter was functional in vivo and in vitro. Expression of its gene complemented the Na+-sensitive phenotype of an E. coli strain that lacks the main Na+/H+ antiporters. Purified to homogeneity, the antiporter was a dimer in solution as accurately determined by size-exclusion chromatography combined with multi-angle laser-light scattering and refractive index monitoring. The purified antiporter was fully capable of electrogenic Na+(Li+)/H+-antiport when reconstituted in proteoliposomes and assayed by solid-supported membrane-based electrophysiological measurements. Transport activity was inhibited by 2-aminoperimidine. The recorded negative currents were in agreement with a 1Na+(Li+)/2H+ stoichiometry. Transport activity was low at pH 7 and up-regulation above this pH value was accompanied by a nearly 10-fold decrease of KmNa (16 mM at pH 8.5) supporting a competitive substrate binding mechanism. K+ does not affect Na+ affinity or transport of substrate cations, indicating that selectivity of the antiport arises from the substrate binding step. In contrast to homologous E. coli NhaA, transport activity remains high at pH values above 8.5. The antiporter from S. Typhimurium is a promising candidate for combined structural and functional studies to contribute to the elucidation of the mechanism of pH-dependent Na+/H+ antiporters and to provide insights in the molecular basis of species-specific growth and survival strategies.

Dataset Information

Cloning and characterization of a novel vacuolar Na+/H+ antiporter gene (Dgnhx1) from chrysanthemum.

Publications

Cloning and characterization of a novel vacuolar Na+/H+ antiporter gene (Dgnhx1) from chrysanthemum.

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