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Cold-induced changes of protein and phosphoprotein expression patterns from rice roots as revealed by multiplex proteomic analysis

文献类型： 外文期刊

作者： Chen, Jinhui 2 ; Tian, Lin 3 ; Xu, Huifang 1 ; Tian, Dagang 4 ; Luo, Yuming 1 ; Ren, Chongmiao 1 ; Yang, Liming 1 ; Shi, 1 ;

作者机构： 1.Huaiyin Normal Univ, Sch Life Sci, Jiangsu Key Lab Ecoagr Biotechnol Hongze Lake, Huaian 223300, Jiangsu, Peoples R China

2.Nanjing Forestry Univ, Minist Educ, Key Lab Forest Genet & Biotechnol, Nanjing 210037, Jiangsu, Peoples R China

3.Chinese Acad Forestry, State Key Lab Tree Genet & Breeding, Beijing 100091, Peoples R China

4.Fujian Acad Agr Sci, Inst Biotechnol, Fujian Key Lab Genet Engn Agr, Fuzhou 350003, Fujian, Peoples R China

5.Nanjing Normal Univ, Coll Life Sci, Nanjing 210046, Jiangsu, Peoples R China

关键词： Cold stress;Multiplex proteomics;Phosphoprotein;Rice roots

期刊名称：PLANT OMICS （ 影响因子：0.777； 五年影响因子：0.802 ）

ISSN： 1836-0661

年卷期： 2012 年 5 卷 2 期

页码：

收录情况： SCI

摘要： Cold stress is a critical abiotic stress that reduces crop yield and quality. The response of the rice proteome to cold stress has been documented, and differential proteomic analysis has provided valuable information on the mechanisms by which rice adapts to cold stress. A global analysis of the change in protein phosphorylation status in response to cold stress remains to be explored, however. Here, we performed a phosphoproteomic analysis of rice roots following exposure to cold stress using a two-dimensional gel electrophoresis-based multiplex proteomic approach. Differentially expressed proteins and phosphoproteins were detected and identified by matrix-assisted laser desorption ionization time of flight/time of flight mass spectrometry combined with querying rice protein databases. Nineteen protein gel spots (stained with silver) showed a twofold difference in abundance of protein spots from gels with and without cold stress; these proteins were identified to be involved in redox homeostasis, signal transduction, and metabolism. Twelve of the thirteen phosphoprotein gel spots (stained with Pro-Q Diamond) that showed a twofold abundance difference were identified, including the following nine proteins: enolase, glyceraldehyde-3-phosphate dehydrogenase, nucleoside diphosphate kinase, ascorbate peroxidase, adenosine kinase, CPK1 adapter protein 2, ATP synthase subunit alpha, methionine synthase 1, and tubulin. Phosphorylation site predictors were used to confirm that the identified proteins had putative phosphorylation sites. These results suggest that phosphorylation of some proteins in rice roots is regulated in response to cold stress.

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