| Author |
Pi, Erxu Qu, Liqun Hu, Jianwen Huang, Yingying Qiu, Lijuan Lu, Hongfei Jiang, Bo Liu, Cong Peng, Tingting Zhao, Ying Wang, Huizhong Tsai, Sau-Na Ngai, Saiming Du, Liqun |
| Description |
Author Affiliation: Pi E ( From the College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, Zhejiang, 310036, PR China); Qu L ( From the College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, Zhejiang, 310036, PR China); Hu J ( §Shanghai Applied Protein Technology Co. Ltd, Shanghai, 200233, PR China); Huang Y ( From the College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, Zhejiang, 310036, PR China); Qiu L ( ¶The National Key Facility for Crop Gene Resources and Genetic Improvement (NFCRI), Institute of Crop Science, Chinese Academy of Agricultural Sciences, Beijing, P.R. China); Lu H ( âCollege of Life Science, Zhejiang Sci-Tech University, Hangzhou, 310018, PR China); Jiang B ( **College of Biology and Food Engineering, Changshu Institute of Technology, Changshu 215500, PR China); Liu C ( From the College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, Zhejiang, 310036, PR China); Peng T ( From the College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, Zhejiang, 310036, PR China); Zhao Y ( From the College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, Zhejiang, 310036, PR China); Wang H ( From the College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, Zhejiang, 310036, PR China); Tsai SN ( Centre for Soybean Research of Partner State Key Laboratory of Agrobiotechnology and School of Life Sciences, The Chinese University of Hong Kong, Hong Kong.); Ngai S ( Centre for Soybean Research of Partner State Key Laboratory of Agrobiotechnology and School of Life Sciences, The Chinese University of Hong Kong, Hong Kong pierzaixian001@aliyun.com liqundu@hznu.edu.cn smngai@cuhk.edu.hk.); Du L ( From the College of Life and Environmental Sciences, Hangzhou Normal University, Hangzhou, Zhejiang, 310036, PR China) |
| Abstract |
Understanding molecular mechanisms underlying plant salinity tolerance provides valuable knowledgebase for effective crop improvement through genetic engineering. Current proteomic technologies, which support reliable and high-throughput analyses, have been broadly used for exploring sophisticated molecular networks in plants. In the current study, we compared phosphoproteomic and proteomic changes in roots of different soybean seedlings of a salt-tolerant cultivar (Wenfeng07) and a salt-sensitive cultivar (Union85140) induced by salt stress. The root samples of Wenfeng07 and Union85140 at three-trifoliate stage were collected at 0 h, 0.5 h, 1 h, 4 h, 12 h, 24 h, and 48 h after been treated with 150 mm NaCl. LC-MS/MS based phosphoproteomic analysis of these samples identified a total of 2692 phosphoproteins and 5509 phosphorylation sites. Of these, 2344 phosphoproteins containing 3744 phosphorylation sites were quantitatively analyzed. Our results showed that 1163 phosphorylation sites were differentially phosphorylated in the two compared cultivars. Among them, 10 MYB/MYB transcription factor like proteins were identified with fluctuating phosphorylation modifications at different time points, indicating that their crucial roles in regulating flavonol accumulation might be mediated by phosphorylated modifications. In addition, the protein expression profiles of these two cultivars were compared using LC MS/MS based shotgun proteomic analysis, and expression pattern of all the 89 differentially expressed proteins were independently confirmed by qRT-PCR. Interestingly, the enzymes involved in chalcone metabolic pathway exhibited positive correlations with salt tolerance. We confirmed the functional relevance of chalcone synthase, chalcone isomerase, and cytochrome P450 monooxygenase genes using soybean composites and Arabidopsis thaliana mutants, and found that their salt tolerance were positively regulated by chalcone synthase, but was negatively regulated by chalcone isomerase and cytochrome P450 monooxygenase. A novel salt tolerance pathway involving chalcone metabolism, mostly mediated by phosphorylated MYB transcription factors, was proposed based on our findings. (The mass spectrometry raw data are available via ProteomeXchange with identifier PXD002856). |
