Effect of salt and osmotic stresses on the expression of genes for the vacuolar H+-pyrophosphatase, H+-ATPase subunit A, and Na+/H+ antiporter from barley

Fukuda, Atsunori; Chiba, Kazuhiro; Maeda, Mineko; Nakamura, Atsuko; Maeshima, Masayoshi; Tanaka, Yoshiyuki

doi:10.1093/jxb/erh070

Cited by 159 publications

(92 citation statements)

References 47 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Recently, mRNA from a tonoplast H + -PPase gene was found to increase in the roots for a short time and there was no detectable increase in the level of transcript in the leaves under salt stress in barley (Fukuda et al, 2004). Combining TsVP expression patterns in T. halophila in the present report, it is concluded that the changes of H + -PPase activity were different in different tissues of different species under salt stress conditions.…”

Section: Effects Of Hsupporting

confidence: 58%

Cloning of an H+-PPase gene from Thellungiella halophila and its heterologous expression to improve tobacco salt tolerance

Gao

Duan

et al. 2006

Journal of Experimental Botany

137

View full text Add to dashboard Cite

An H 1 -pyrophosphatase (PPase) gene named TsVP involved in basic biochemical and physiological mechanisms was cloned from Thellungiella halophila. The deduced translation product has similar characteristics to H 1 -PPases from other species, such as Arabidopsis and rice, in terms of bioinformation. The heterologous expression of TsVP in the yeast mutant ena1 suppressed Na 1 hypersensitivity and demonstrated the function of TsVP as an H 1 -PPase. Transgenic tobacco overexpressing TsVP had 60% greater dry weight than wild-type tobacco at 300 mM NaCl and higher viability of mesophyll protoplasts under salt shock stress conditions. TsVP and AVP1, another H 1 -PPase from Arabidopsis, were heterologously expressed separately in both the yeast mutant ena1 and tobacco. The salt tolerance of TsVP or AVP1 yeast transformants and transgenic tobacco were improved to almost the same level. The TsVP transgenic tobacco lines TL3 and TL5 with the highest H 1 -PPase hydrolytic activity were studied further. These transgenic tobacco plants accumulated 25% more solutes than wild-type plants without NaCl stress and 20-32% more Na 1 under salt stress conditions. Although transgenic tobacco lines TL3 and TL5 accumulated more Na 1 in leaf tissues, the malondialdehyde content and cell membrane damage were less than those of the wild type under salt stress conditions. Presumably, compartmentalization of Na 1 in vacuoles reduces its toxic effects on plant cells. This result supports the hypothesis that overexpression of H 1 -PPase causes the accumulation of Na 1 in vacuoles instead of in the cytoplasm and avoids the toxicity of excessive Na 1 in plant cells.

show abstract

Section: Effects Of Hsupporting

confidence: 58%

Cloning of an H+-PPase gene from Thellungiella halophila and its heterologous expression to improve tobacco salt tolerance

Gao

Duan

et al. 2006

Journal of Experimental Botany

137

View full text Add to dashboard Cite

show abstract

“…The bacterial H þ -PPase appears therefore to be transcriptionally induced in response to a variety of conditions that constrain cell bioenergetics (54). On the other hand, algal and plant H þ -PPases are induced under anoxia, chilling and salt stresses (55,56), and overexpression of the vacuolar H þ -PPase isoform AVP1 in the model plant Arabidopsis has been claimed to confer increased saline and drought tolerance (57).…”

Section: Structural and Functional Featuresmentioning

confidence: 99%

H+‐PPases: yesterday, today and tomorrow

et al. 2007

View full text Add to dashboard Cite

SummarySuggestions by Calvin about a role of inorganic pyrophosphate (PPi) in early photosynthesis and by Lipmann that PPi may have been the original energy-rich phosphate donor in biological energy conversion, were followed in the mid-1960s by experimental results with isolated chromatophore membranes from the purple photosynthetic bacterium Rhodospirillum rubrum. PPi was shown to be hydrolysed in an uncoupler stimulated reaction by a membranebound inorganic pyrophosphatase (PPase), to be formed at the expense of light energy in photophosphorylation and to be utilized as an energy donor for various energy-requiring reactions, as a first known alternative to ATP. This direct link between PPi and photosynthesis led to increasing attention concerning the role of PPi in both early and present biological energy transfer. In the 1970s, the PPase was shown to be a proton pump and to be present also in higher plants. In the 1990s, sequences of H þ -PPase genes were obtained from plants, protists, bacteria and archaea and two classes of H þ -PPases differing in K þ sensitivity were established. Over 200 H þ -PPase sequences have now been determined. Recent biochemical and biophysical results have led to new progress and questions regarding the H þ -PPase family, as well as the families of soluble PPases and the inorganic polyphosphatases, which hydrolyse inorganic linear high-molecular-weight polyphosphates (HMWpolyP). Here we will focus attention on the H þ -PPases, their evolution and putative active site motifs, response to monovalent cations, genetic regulation and some very recent results, based on new methods for obtaining large quantities of purified protein, about their tertiary and quaternary structures. IUBMB Life, 59: 76-83, 2007

show abstract

“…NHX-type antiporter genes orthologous to ScNHX1 have been reported to exist in various higher plants, including salt-tolerant glycophytes and halophytes (Fukuda et al 2004b;Pardo et al 2006). Five additional NHX-type antiporter genes (AtNHX2 through 6) were identified in A. thaliana and categorized into two subgroups (AtNHX1 through 4 and AtNHX5 and 6; Yokoi et al 2002).…”

Section: Introductionmentioning

confidence: 99%

Molecular and functional analyses of rice NHX-type Na+/H+ antiporter genes

Fukuda

Nakamura

Hara

et al. 2010

Planta

203

146

View full text Add to dashboard Cite

We previously cloned a vacuolar Na+/H+ antiporter gene (OsNHX1) from rice (Oryza sativa). Here we identified four additional NHX-type antiporter genes in rice (OsNHX2 through OsNHX5) and performed molecular and functional analyses of those genes. The exon-intron structure of the OsNHX genes and the phylogenetic tree of the OsNHX proteins suggest that the OsNHX proteins are categorized into two subgroups (OsNHX1 through OsNHX4 and OsNHX5). OsNHX1, OsNHX2, OsNHX3, and OsNHX5 can suppress the Na+, Li+, and hygromycin sensitivity of yeast nhx1 mutants and their sensitivity to a high K+ concentration. The expression of OsNHX1, OsNHX2, OsNHX3, and OsNHX5 is regulated differently in rice tissues and is increased by salt stress, hyperosmotic stress, and ABA. When we studied the expression of β-glucuronidase (GUS) driven by either the OsNHX1 or the OsNHX5 promoter, we observed activity in the stele, the emerging part of lateral roots, the vascular bundle, the water pore, and the basal part of seedling shoots with both promoters. In addition, each promoter had a unique expression pattern. OsNHX1 promoter-GUS activity only was localized to the guard cells and trichome, whereas OsNHX5 promoter-GUS activity only was localized to the root tip and pollen grains. Our results suggest that the members of this gene family play important roles in the compartmentalization into vacuoles of the Na+ and K+ that accumulate in the cytoplasm and that the differential regulation of antiporter gene expression in different rice tissues may be an important factor determining salt tolerance in rice.

show abstract

Effect of salt and osmotic stresses on the expression of genes for the vacuolar H+-pyrophosphatase, H+-ATPase subunit A, and Na+/H+ antiporter from barley

Cited by 159 publications

References 47 publications

Cloning of an H+-PPase gene from Thellungiella halophila and its heterologous expression to improve tobacco salt tolerance

Cloning of an H+-PPase gene from Thellungiella halophila and its heterologous expression to improve tobacco salt tolerance

H+‐PPases: yesterday, today and tomorrow

Molecular and functional analyses of rice NHX-type Na+/H+ antiporter genes

Contact Info

Product

Resources

About