Comparative phosphoproteomic analysis of microsomal fractions of Arabidopsis thaliana and Oryza sativa subjected to high salinity

in Sciences Citation Index(SCI), 科學引文索引資料庫(SCI)
標題Comparative phosphoproteomic analysis of microsomal fractions of Arabidopsis thaliana and Oryza sativa subjected to high salinity
出版類型SCI(Sciences Citation Index)
出版年度2012
AuthorsIng-Feng Chang, 張英?, Liao Ming-Huei 徐睿良, Pang-Hung Hsu 許邦弘, Wei-An Sheng 盛維安, Shiuan-Jeng Lai 賴軒正, Cindy Lee 李欣蒂, Chun-Wei Chen 陳俊偉, Jen-Chieh Hsu 許仁傑, Shu-Ying Wang 王舒瑩, Lan-Yu Wang 王蘭玉, & Ching-Chuan Chen 陳景川
開始頁131
頁數11
出版日期2012 / 4
其他編號NSC 98-2113-M-020 -002 -MY2
中文摘要

Plants respond to salt stress by initiating phosphorylation cascades in their cells. Many key phosphorylation events take place at membranes. Microsomal fractions from 400 mM salt-treated Arabidopsis suspension plants were isolated, followed by trypsin shaving, enrichment using Zirconium ion-charged or TiO(2) magnetic beads, and tandem mass spectrometry analyses for site mapping. A total of 27 phosphorylation sites from 20 Arabidopsis proteins including photosystem II reaction center protein H PsbH were identified. In addition to Arabidopsis, microsomal fractions from shoots of 200 mM salt-treated rice was carried out, followed by trypsin digestion using shaving or tube-gel, and enrichment using Zirconium ion-charged or TiO(2) magnetic beads. This yielded identification of 13 phosphorylation sites from 8 proteins including photosystem II reaction center protein H PsbH. Label-free quantitative analysis suggests that the phosphorylation sites of PsbH were regulated by salt stress in Arabidopsis and rice. Sequence alignment of PsbH phosphorylation sites indicates that Thr-2 and Thr-4 are evolutionarily conserved in plants. Four conserved phosphorylation motifs were predicted, and these suggest that a specific unknown kinase or phosphatase is involved in high-salt stress responses in plants.

期刊名稱Plant Science
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