Overexpression of the wheat expansin gene TaEXPA2 improves oxidative stress tolerance in transgenic Arabidopsis plants

Expansins play an important role in plant stress tolerance. In a previous study, we cloned the wheat expansin gene TaEXPA2. Here, we analyze its involvement in oxidative stress tolerance. First, we observed that the expression of TaEXPA2 in wheat seedlings was upregulated during H2O2 stress. Then, we assembled a TaEXPA2 gene expression vector, transformed it to Arabidopsis, and obtained transgenic plants overexpressing TaEXPA2 (labeled OE). When exposed to H2O2, both OE and wild-type (Col) plants were damaged by oxidative stress, as indicated by decolored leaves and increased malondialdehyde (MDA) content. Damage in OE plants was less severe than in Col plants (WT), and this was accompanied by higher activity of cell wall peroxidase (POD) enzymes, including soluble POD, ionically bound POD, and covalently bound POD. The expansin activities of the OE plants were also higher than WT under oxidative stress. We further obtained the Arabidopsis mutant atexpa2 (AtEXPA2 is homologous to TaEXPA2), and found that the antioxidant ability of atexpa2 was lower than that in Col plants, accompanied by depressed activity of POD enzymes and expansins in cell walls. We transformed wheat TaEXPA2 to atexpa2 and obtained plants (labeled Rs) capable of recovering the antioxidant capacity. Oxidative stress tolerance in Rs plants was higher than that of Col plants, and the Rs plants also had higher levels of cell wall POD enzyme and expansin activity. Finally, we identified 13 POD genes in Arabidopsis thallana and analyzed their expression patterns using quantitative real-time PCR. The expression of 4 of these genes (AtPOD31, AtPOD33, AtPOD34 and AtPOD71) was significantly upregulated during exposure to H2O2. We speculate that the 4 genes upregulated by H2O2 treatment are involved in the increased activity of POD in the cell wall. We suggest that TaEXPA2 may regulate antioxidant capacity in plants by regulating the activity of cell wall peroxidase.