Quantitative proteome analysis reveals changes of membrane transport proteins in Sedum plumbizincicola under cadmium stress

文献类型： 外文期刊

第一作者： Zhu, Yue

作者： Zhu, Yue;Qiu, Wenmin;Li, Yuhong;Han, Xiaojiao;Zhuo, Renying;Zhu, Yue;Zhu, Yue;Qiu, Wenmin;Li, Yuhong;Han, Xiaojiao;Zhuo, Renying;Tan, Jinjuan;Deng, Zhiping;Wu, Longhua;Jiang, Yugen;Wu, Chao

作者机构：

关键词： Integrative membrane protein; Cadmium tolerance and accumulation; Sedum plumbizincicola; TMT labeling Based quantification proteome; Transporter

期刊名称：CHEMOSPHERE （ 影响因子：8.943； 五年影响因子：8.52 ）

ISSN： 0045-6535

年卷期： 2022 年 287 卷

页码：

收录情况： SCI

摘要： Sedum plumbizincicola is an herbaceous species tolerant of excessive cadmium accumulation in above-ground tissues. The implications of membrane proteins, especially integrative membrane proteins, in Cd detoxification of plants have received attention in recent years, but a comprehensive profiling of Cd-responsive membrane proteins from Cd hyperaccumulator plants is lacking. In this study, the membrane proteins of root, stem, and leaf tissues of S. plumbizincicola seedlings treated with Cd solution for 0, 1 or 4 days were analyzed by Tandem Mass Tag (TMT) labeling-based proteome quantification (Data are available via ProteomeXchange with identifier PXD025302). Total 3353 proteins with predicted transmembrane helices were identified and quantified in at least one tissue group. 1667 proteins were defined as DAPs (differentially abundant proteins) using fold change >1.5 with p-values <0.05. The number of DAPs involved in metabolism, transport protein, and signal transduction was significantly increased after exposure to Cd, suggesting that the synthesis and decomposition of organic compounds and the transport of ions were actively involved in the Cd tolerance process. The number of up-regulated transport proteins increased significantly from 1-day exposure to 4-day exposure, from 5 to 112, 16 to 42, 18 to 44, in root, stem, and leaf, respectively. Total 352 Cd-regulated transport proteins were identified, including ABC transporters, ion transport proteins, aquaporins, proton pumps, and organic transport proteins. Heterologous expression of SpABCB28, SpMTP5, SpNRAMP5, and SpHMA2 in yeast and subcellular localization showed the Cd-specific transport activity. The results will enhance our understanding of the molecular mecha-nism of Cd hypertolerance and hyperaccumulation in S. plumbizincicola and will be benefit for future genetic engineering in phytoremediation.

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