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作 者:Pengfei Gan Chunlei Tang Yi Lu Chenrong Ren Hojjatollah Rabbani Nasab Xufeng Kun Xiaodong Wang Liangzhuang Li Zhensheng Kang Xiaojie Wang Jianfeng Wang
机构地区:[1]State Key Laboratory of Crop Stress Resistance and High-Efficiency Production,College of Plant Protection,Northwest A&F University,Yangling 712100,Shaanxi,China [2]Plant Protection Station of Xinjiang Uygur Autonomous Region,Urumqi 830049,Xinjiang,China [3]Plant Protection Research Department,Agricultural and Natural Resource Research and Education Center of Golestan,Agricultural Research,Education and Extension Organization(AREEO),Gorgan,Iran
出 处:《Stress Biology》2024年第1期321-335,共15页逆境生物学(英文)
基 金:supported by the National Natural Science Foundation of China(32161143023,32225041);the earmarked fund for CARS(CARS-03);Science and Technology Assistance Project of Xinjiang Uygur Autonomous Region(2022E02070),and Tang Scholar.
摘 要:Protein phosphorylation plays an important role in immune signaling transduction in plant resistance to pathogens.Wheat stripe rust,caused by Puccinia striiformis f.sp.tritici(Pst),severely devastates wheat production.Nonetheless,the molecular mechanism of wheat resistance to stripe rust remains limited.In this study,quantitative phosphoproteomics was employed to investigate the protein phosphorylation changes in wheat challenged by Pst.A total of 1537 and 2470 differentially accumulated phosphoproteins(DAPs)were identified from four early infection stage(6,12,18 and 24 h post-inoculation)in incompatible and compatible wheat-Pst interactions respectively.KEGG analysis revealed that Oxidative Phosphorylation,Phosphatidylinositol Signaling,and MAPK signaling processes are distinctively enriched in incompatible interaction,while Biosynthesis of secondary metabolites and RNA degradation process were significantly enriched in compatible interactions.In particular,abundant changes in phosphorylation levels of chloroplast proteins were identified,suggesting the regulatory role of photosynthesis in wheat-Pst interaction,which is further emphasized by protein-protein interaction(PPI)network analysis.Motif-x analysis identified[xxxxSPxxxx]motif,likely phosphorylation sites for defensive response-related kinases,and a new[xxxxSSxxxx]motif significantly enriched in incompatible interaction.The results shed light on the early phosphorylation events contributing to wheat resistance against Pst.Moreover,our study demonstrated that the phosphorylation levels of Nucleoside diphosphate kinase TaNAPK1 are upregulated at 12 hpi with CYR23 and at 24 hpi with CYR31.Transient silencing of TaNAPK1 was able to attenuate wheat resistance to CYR23 and CYR31.Our study provides new insights into the mechanisms underlying Pst-wheat interactions and may provide database to find potential targets for the development of new resistant varieties.
关 键 词:WHEAT Puccinia striiformis f.sp.tritici PHOSPHOPROTEOMICS
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