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Proteomics Dissection of Cold Responsive Proteins Based on PEG Fractionation in Arabidopsis

文献类型: 外文期刊

作者: Li Shanyu 2 ; Liu Xiangguo 3 ; Wang Shang 1 ; Hao Dongyun 3 ; Xi Jinghui 1 ;

作者机构: 1.Jilin Univ, Coll Plant Sci, Changchun 130062, Peoples R China

2.Jilin Univ, Hosp 1, Changchun 130021, Peoples R China

3.Jilin Acad Agr Sci, Biotechnol Res Ctr, Changchun 130124, Peoples R China

关键词: Arabidopsis thaliana;Cold stress;Proteome;Protein fractionation

期刊名称:CHEMICAL RESEARCH IN CHINESE UNIVERSITIES ( 影响因子:1.307; 五年影响因子:0.979 )

ISSN: 1005-9040

年卷期: 2014 年 30 卷 2 期

页码:

收录情况: SCI

摘要: Proteome profiling was performed on Arabidopsis plant exposed to cold stress at 4 degrees C for 24 h in an attempt to explore the mechanisms of plant climate adaptation. The polyethylene glycol(PEG) fractionation protocol developed in this lab was used to identify as many differentially expressed low-abundance proteins as possible. In comparison with those of the biological controls, 67 protein spots with at least two-fold difference in expression were identified for the plant exposed to cold temperatures; and from these spots, 50 proteins were successfully identified by matrix-assisted laser desorption/ionization time of flight mass spectrometry(MALDI-TOF MS). Bioinformatics studies on these proteins show that 57.8% of these proteins were localized in the chloroplast. Of these proteins, 8 ones have functions in photosynthesis, including glycine hydroxymethyltransferase, Rubisco large subunit, Rubisco activase, PSBO2, fructose-1,6-bisphosphate aldolase, NADP-dependent malate dehydrogenase, sedoheptulose bisphosphatase and photosystem II reaction center PsbP family protein, suggesting that photosynthesis is greatly affected by cold stress. The identified proteins were validated by quantitative real-time polymerase chain reaction(qPCR). Taken together, our results suggest that the chloroplast might also act as a cold stress sensor and that photosynthesis-related proteins may play important roles in cold acclimation for Arabidopsis.

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