Insights into salicylic acid responses in cucumber (Cucumis sativus L.) cotyledons based on a comparative proteomic analysis

被引:49
作者
Hao, J. H. [1 ,2 ]
Dong, C. J. [1 ,2 ]
Zhang, Z. G. [1 ,2 ]
Wang, X. L. [1 ,2 ]
Shang, Q. M. [1 ,2 ]
机构
[1] Chinese Acad Agr Sci, Inst Vegetables & Flowers, Beijing 100081, Peoples R China
[2] Minist Agr, Key Lab Hort Crop Biol & Germplasm Innovat, Beijing 100081, Peoples R China
基金
对外科技合作项目(国际科技项目); 中国国家自然科学基金;
关键词
Cucumber (Cucumis sativus L.); Proteome; Salicylic acid; Protein interaction network; NITRATE REDUCTASE-ACTIVITY; RESISTANCE RESPONSE; STRESS; PROTEINS; LEAVES; PEA; EXPRESSION; MECHANISM; TRANSPORT; HORMONE;
D O I
10.1016/j.plantsci.2012.01.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
To investigate the response of cucumber seedlings to exogenous salicylic acid (SA) and gain a better understanding of SA action mechanism, we generated a proteomic profile of cucumber (Cucumis sativus L) cotyledons treated with exogenous SA. Analysis of 1500 protein spots from each gel revealed 63 differentially expressed proteins, 59 of which were identified successfully. Of the identified proteins, 97% matched cucumber proteins using a whole cucumber protein database based on the newly completed genome established by our laboratory. The identified proteins were involved in various cellular responses and metabolic processes, including antioxidative reactions, cell defense, photosynthesis, carbohydrate metabolism, respiration and energy homeostasis, protein folding and biosynthesis. The two largest functional categories included proteins involved in antioxidative reactions (23.7%) and photosynthesis (18.6%). Furthermore, the SA-responsive protein interaction network revealed 13 key proteins, suggesting that the expression changes of these proteins could be critical for SA-induced resistance. An analysis of these changes suggested that SA-induced resistance and seedling growth might be regulated in part through pathways involving antioxidative reactions and photosynthesis. (C) 2012 Elsevier Ireland Ltd. All rights reserved.
引用
收藏
页码:69 / 82
页数:14
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