Comparative analysis of salt-responsive phosphoproteins in maize leaves using Ti4+-IMAC enrichment and ESI-Q-TOF MS
Comparative analysis of salt-responsive phosphoproteins in maize leaves using Ti4+-IMAC enrichment and ESI-Q-TOF MS
复制标题
使用 Ti4 -IMAC 富集和 ESI-Q-TOF MS 比较分析玉米叶片中的盐响应磷蛋白
DOI：
10.1002/elps.201200381
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发表时间：
2013-02-01
期刊：
影响因子：
2.9
通讯作者：
Ren, Xueqin
中科院分区：
文献类型：
--
作者：
Hu, Yufeng;Guo, Shuangxi;Ren, Xueqin
盐胁迫是植物最常见的非生物胁迫之一。可逆的蛋白质磷酸化参与植物对盐胁迫的防御过程。在这里，我们进行了全球磷酸肽映射，通过我们合成的PVA-磷酸-Ti4+ IMAC加上随后的ESI-Q-TOF MS鉴定富集。共104个肽序列，含有139个磷酸化位点，确定从70个磷蛋白的控制叶。与此相反，124个磷酸肽含有143个磷酸化位点的92磷蛋白在盐胁迫玉米叶片中被确定。与对照组相比，47个蛋白磷酸化，25个蛋白去磷酸化，45个蛋白重叠。在72个差异磷蛋白中，35个是已知的盐胁迫反应蛋白，其余的未见文献报道。为了剖析差异磷酸化，检索差异磷蛋白的基因本体论注释。结果表明，细胞信号通路的成员，如钙调素和14-3-3蛋白的调节响应24小时盐胁迫。多个假定的盐响应磷蛋白似乎参与光合相关过程的调节。这些结果有助于理解盐诱导玉米叶片磷酸化的过程。
Salinity is one of the most common abiotic stresses encountered by plants. Reversible protein phosphorylation is involved in plant defense processes against salinity stress. Here, we performed global phosphopeptide mapping through enrichment by our synthesized PVA-phosphate-Ti4+ IMAC coupled with subsequent identification by ESI-Q-TOF MS. A total of 104 peptide sequences containing 139 phosphorylation sites were determined from 70 phosphoproteins of the control leaves. In contrast, 124 phosphopeptides containing 143 phosphorylated sites from 92 phosphoproteins were identified in salt-stressed maize leaves. Compared with the control, 47 proteins were phosphorylated, 25 were dephosphorylated, and 45 overlapped. Among the 72 differential phosphoproteins, 35 were known salt stress response proteins and the rest had not been reported in the literature. To dissect the differential phosphorylation, gene ontology annotations were retrieved for the differential phosphoproteins. The results revealed that cell signaling pathway members such as calmodulin and 14-3-3 proteins were regulated in response to 24-h salt stress. Multiple putative salt-responsive phosphoproteins seem to be involved in the regulation of photosynthesis-related processes. These results may help to understand the salt-inducible phosphorylation processes of maize leaves.