Quantitative Phosphoproteomics Analysis of Nitric Oxide-Responsive Phosphoproteins in Cotton Leaf
文献类型: 外文期刊
作者: Fan, Shuli 1 ; Meng, Yanyan 1 ; Song, Meizhen 1 ; Pang, Chaoyou 1 ; Wei, Hengling 1 ; Liu, Ji 1 ; Zhan, Xianjin 1 ; Lan, Jiayang 1 ; Feng, Changhui 1 ; Zhang, Shengxi 1 ; Yu, Shuxun 1 ;
作者机构: 1.State Key Laboratory of Cotton Biology, Institute of Cotton Research, Chinese Academy of Agricultural Sciences, Anyang, Henan Province, China
2.Key Laboratory of Cotton Biology and Breeding in the Middle Reaches of the Changjing River, Institute of Economic Crop, Hubei Academy of Agricultural Science, Wuhan, Hubei Province,China, 3 College of Agronomy, Northwest A & F University, Yangling, Shaanxi Province, China Crop, Hubei Academy of Agricultural Science, Wuhan, Hubei Province, China
3.Xianjin Zhan
4.Shuxun Yu
期刊名称:PLOS ONE ( 影响因子:3.24; 五年影响因子:3.788 )
ISSN: 1932-6203
年卷期: 2014 年 9 卷 4 期
页码:
收录情况: SCI
摘要: Knowledge of phosphorylation events and their regulation is crucial to understanding the functional biology of plant proteins, but very little is currently known about nitric oxide-responsive phosphorylation in plants. Here, we report the first large-scale, quantitative phosphoproteome analysis of cotton (Gossypium hirsutum) treated with sodium nitroprusside (nitric oxide donor) by utilizing the isobaric tag for relative and absolute quantitation (iTRAQ) method. A total of 1315 unique phosphopeptides, spanning 1528 non-redundant phosphorylation sites, were detected from 1020 cotton phosphoproteins. Among them, 183 phosphopeptides corresponding to 167 phosphoproteins were found to be differentially phosphorylated in response to sodium nitroprusside. Several of the phosphorylation sites that we identified, including RQxS, DSxE, TxxxxSP and SPxT, have not, to our knowledge, been reported to be protein kinase sites in other species. The phosphoproteins identified are involved in a wide range of cellular processes, including signal transduction, RNA metabolism, intracellular transport and so on. This study reveals unique features of the cotton phosphoproteome and provides new insight into the biochemical pathways that are regulated by nitric oxide.
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