数字农科院2.0

The protein phosphatase 2C clade A TaPP2CA interact with calcium-dependent protein kinases, TaCDPK5/TaCDPK9-1, that phosphorylate TabZIP60 transcription factor from wheat (Triticum aestivum L.)

文献类型： 外文期刊

作者： Lina Zhang;Liting Wang;Xue Chen;Lijuan Zhao;Xingyan Liu;Yinghong Wang;Guofan Wu;Chuan Xia;Lichao Zhang;Xiuying Kong

作者机构：

关键词： Phosphorylation;TabZIP60 TF;TaCDPK5/TaCDPK9–1;TaPP2CA116/ TaPP2CA 121;Wheat

期刊名称： Plant Science

ISSN： 0168-9452

年卷期： 2022 年 321 卷

页码：

收录情况： SCIE（2022版）

摘要： Previously we have found that TabZIP60 from the ABF/AREB (ABRE-binding factor/ABA-responsive element-binding protein) subfamily of bZIP transcription factor (TF) was involved in salt stress response. However, the regulatory mechanism of TabZIP60 is unknown. In the present study, we identified two calcium-dependent protein kinase (CDPK) genes, TaCDPK5/TaCDPK9–1, which were clustered into group Ⅰ and were induced by salt, abscisic acid (ABA), and polyethylene glycol (PEG) treatments. RT-qPCR results showed that the expression level of salt-induced TabZIP60 was drastically inhibited by Ca2+ channel blocker LaCl3. TaCDPK5/TaCDPK9–1 were involved in interaction with TabZIP60 protein in vivo and in vitro. And TaCDPK5/TaCDPK9–1 could autophosphorylate and phosphorylate TabZIP60 protein in a Ca2+-dependent way. Mutational analysis indicated that Serine-110 of TabZIP60 was essential for TaCDPK5/TaCDPK9–1-TabZIP60 interaction and was the phosphorylation site of TaCDPK5/TaCDPK9–1 kinases. Yeast two-hybrid assay results showed the interactions between TaCDPK5/TaCDPK9–1 and wheat protein phosphatase 2 C clade A TaPP2CA116/ TaPP2CA121 separately. These findings demonstrate that the phosphorylation status of TabZIP60 controlled by TaPP2CA116/ TaPP2CA121 and TaCDPK5/TaCDPK9–1 might play a crucial role in wheat during salt stress.

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