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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45551

Title: Comparative phosphoproteomic analysis of microsomal fractions of Arabidopsis thaliana and Oryza sativa subjected to high salinity.
Authors: Ing-Feng Chang;Jue-Liang Hsu;Pang-Hung Hsu;Wei-An Sheng;Shiuan-Jeng Lai;Cindy Lee;Chun-Wei Chen;Jen-Chieh Hsu;Shu-Ying Wang;Lan-Yu Wang;Ching-Chuan Chen
Contributors: 國立臺灣海洋大學:生命科學系
Date: 2012
Issue Date: 2018-03-26T06:30:02Z
Publisher: Plant Science
Abstract: Abstract: 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 TiO2 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 TiO2 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.
Relation: 185-6
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45551
Appears in Collections:[生命科學系] 期刊論文

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