Open AccessQuantitative phosphoproteomic analysis provides insights into the aluminum-responsiveness of Tamba black soybean
Author(s) -
Ruizhi Han,
Yuansong Wei,
Yonghong Xie,
Lusheng Liu,
Caode Jiang,
Yang Yu
Publication year - 2020
Publication title -
plos one
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.99
H-Index - 332
ISSN - 1932-6203
DOI - 10.1371/journal.pone.0237845
Subject(s) - tandem mass tag , tandem mass spectrometry , proteomics , phosphorylation , chemistry , biochemistry , downregulation and upregulation , liquid chromatography–mass spectrometry , biology , quantitative proteomics , mass spectrometry , chromatography , gene
Aluminum (Al 3+ ) toxicity is one of the most important limitations to agricultural production worldwide. The overall response of plants to Al 3+ stress has been documented, but the contribution of protein phosphorylation to Al 3+ detoxicity and tolerance in plants is unclear. Using a combination of tandem mass tag (TMT) labeling, immobilized metal affinity chromatography (IMAC) enrichment and liquid chromatography-tandem mass spectrometry (LC-MS/MS), Al 3+ -induced phosphoproteomic changes in roots of Tamba black soybean (TBS) were investigated in this study. The Data collected in this study are available via ProteomeXchange with the identifier PXD019807. After the Al 3+ treatment, 189 proteins harboring 278 phosphosites were significantly changed (fold change > 1.2 or < 0.83, p < 0.05), with 88 upregulated, 96 downregulated and 5 up-/downregulated. Enrichment and protein interaction analyses revealed that differentially phosphorylated proteins (DPPs) under the Al 3+ treatment were mainly related to G-protein-mediated signaling, transcription and translation, transporters and carbohydrate metabolism. Particularly, DPPs associated with root growth inhibition or citric acid synthesis were identified. The results of this study provide novel insights into the molecular mechanisms of TBS post-translational modifications in response to Al 3+ stress.