Sun,XD (reprint author),Chinese Acad Sci,Kunming Inst Bot,Key Lab Plant Div & Biogeog East Asia,Kunming,Peoples R China.
Stipa purpurea, an endemic forage species on the Tibetan Plateau, is highly resistant to cold and drought, but the mechanisms underlying its responses to drought stress remain elusive. An understanding of such mechanisms may be useful for developing cultivars that are adaptable to water deficit. In this study, we analyzed the physiological and proteomic responses of S. purpurea under increasing drought stress. Seedlings of S. purpurea were subjected to a drought gradient in a controlled experiment, and proteins showing changes in abundance under these conditions were identified by two-dimensional electrophoresis followed by mass spectrometry analysis. A western blotting analysis was conducted to confirm the increased abundance of a heat-shock protein, NCED2, and a dehydrin in S. purpurea seedlings under drought conditions. We detected carbonylated proteins to identify oxidation-sensitive proteins in S. purpurea seedlings, and found that ribulose-1, 5-bisphosphate carboxylase oxygenase (RuBisCO) was one of the oxidation-sensitive proteins under drought. Together, these results indicated drought stress might inhibit photosynthesis in S. purpurea by oxidizing RuBisCO, but the plants were able to maintain photosynthetic efficiency by a compensatory upregulation of unoxidized RuBisCO and other photosynthesis-related proteins. Further analyses confirmed that increased abundance of antioxidant enzymes could balance the redox status of the plants to mitigate drought induced oxidative damage.
1.Chinese Acad Sci, Kunming Inst Bot, Key Lab Plant Div & Biogeog East Asia, Kunming, Peoples R China 2.Chinese Acad Sci, Kunming Inst Bot, Plant Germplasm & Genom Ctr, Kunming, Peoples R China 3.Chinese Acad Sci, Kunming Inst Bot, Inst Tibetan Plateau Res Kunming, Kunming, Peoples R China 4.Chinese Acad Sci, Key Lab Tibetan Environm Changes & Land Surface P, Inst Tibetan Plateau Res, Beijing, Peoples R China 5.Univ Chinese Acad Sci, Beijing, Peoples R China