The Arabidopsis gene AVP1 encodes a vacuolar H+-translocating inorganic pyrophosphatase (EC3.6.1.1) that functions as an electronic proton pump in the vacuolar membrane and affects growth development and stress responses in plants. This study was conducted to evaluate the molecular properties of the A. thaliana vacuolar H+-pyrophosphatase (AVP1) gene in rice. Incorporation and expression of the transgene was confirmed by PCR and quantitative real-time PCR, respectively. Expression of the AVP1 gene in transgenic rice plants (TRP1 and TRP2) resulted in significantly enhanced tolerance to 100 mM NaCl under greenhouse conditions when compared to control wild-type (WT) rice plants. Augmented AVP1 expression in the transgenic rice plants also affected total biomass and improved ion homeostasis through increased accumulation of Na+ ions in whole tissues when compared to control WT rice plants under high salinity conditions. The Fv/Fm values of transgenic rice plants were higher than those of WT rice plants, even though the values decreased over time in both WT and transgenic (TRP1 to TRP8) rice plants. Furthermore, rice grain yield and biomass of the transgenic rice plants were at least 15% higher based on the culm and root weights and panicle and spikelet numbers when compared to those of the WT rice plants during the farming season in Korea. Thus, these results suggest that ectopic AVP1 expression conferred tolerance and stress resistance to genetically modified transgenic crop plants by improving cellular ion homeostasis against salt conditions, which enhanced the rice yield and biomass under natural conditions in paddy fields.

We investigated Arctic plants to determine if they have a specific mechanism enabling them to adapt to extreme environments because they are subject to such conditions throughout their life cycles. Among the cell defense systems of the Arctic mouse-ear chickweed Cerastium arcticum, we identified a stress-responsive dehydrin gene CaDHN that belongs to the SK5 subclass and contains conserved regions with 1 S-segment at the N-terminus and 5 K-segments from the N-terminus to the C-terminus. To investigate the molecular properties of CaDHN, yeast were transformed with CaDHN. CaDHN-expressing transgenic yeast (TG) cells recovered more rapidly from challenge with exogenous stimuli, including oxidants (hydrogen peroxide, menadione, and tert-butyl hydroperoxide), high salinity, freezing and thawing, and metal (Zn2+), than wild-type (WT) cells. TG cells were sensitive to copper, cobalt, and sodium dodecyl sulfate. In addition, the cell survival of TG cells was higher than that of WT cells when cells at the mid-log and stationary stages were exposed to increased ethanol concentrations. There was a significant difference in cultures that have an ethanol content >16%. During glucose-based batch fermentation at generally used (30℃) and low (18℃) temperatures, TG cells produced a higher alcohol concentration through improved cell survival. Specifically, the final alcohol concentrations were 13.3% and 13.2% in TG cells during fermentation at 30℃ and 18℃, respectively, whereas they were 10.2% and 9.4%, respectively, in WT cells under the same fermentation conditions. An in vitro assay revealed that purified CaDHN acted as a reactive oxygen species (ROS)-scavenger by neutralizing H2O2 and a chaperone by preventing high temperature-mediated catalase inactivation. Taken together, our results show that CaDHN expression in transgenic yeast confers tolerance to various abiotic stresses by improving redox homeostasis and enhances fermentation capacity, especially at low temperatures (18℃).

Chilling stress affects growth and yield of warm-climate crops such as soybean (Glycine max L.) that is susceptible to low temperature (10-18℃). A comparative proteomic approach was employed to explore the mechanisms underlying soybean response to chilling stress. Soybean seedlings were germinated for 3-4 days and exposed to low temperature (10℃) for 3 days, and the proteins were extracted from seedling leaves. Protein separation by SDS-PAGE followed by liquid chromatography electro-spray ionization tandem mass spectrometry (LC-ESI MS/MS) was effective approach to identify proteins, based on the number of peptides reliably identified. A total of 77 proteins out of 704 proteins were identified in the presence of chilling stress. Most proteins identified had functions related to cell signaling, metabolism, energy and transport, protein biosynthesis and degradation, cytoskeleton, and were involved in regulating reactions and defending against stress. It is therefore likely that the response of soybean plant’s proteome to chilling stress is complex, and that the identification proteins may play an important role in regulating adaptation activities following challenge to chilling stress to facilitate cellular homeostasis. Furthermore, our result suggest that new ways of engineering stress-tolerant plants responding climate change by providing outline for agriculturally important chilling stress.