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蛋白磷酸酶 2C 族 A 型 TaPP2CA 与钙依赖性蛋白激酶 TaCDPK5/TaCDPK9-1 相互作用,后者磷酸化来自小麦(Triticum aestivum L.)的 TabZIP60 转录因子。

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.).

机构信息

College of Life Sciences, Northwest Normal University, Lanzhou, Gansu 730070, China.

College of Life Sciences, Northwest Normal University, Lanzhou, Gansu 730070, China.

出版信息

Plant Sci. 2022 Aug;321:111304. doi: 10.1016/j.plantsci.2022.111304. Epub 2022 May 6.

DOI:10.1016/j.plantsci.2022.111304
PMID:35696905
Abstract

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 Ca channel blocker LaCl. 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 Ca-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.

摘要

先前,我们发现 ABF/AREB(ABRE 结合因子/ABA 响应元件结合蛋白)bZIP 转录因子(TF)亚家族中的 TabZIP60 参与了盐胁迫反应。然而,TabZIP60 的调控机制尚不清楚。在本研究中,我们鉴定了两个钙依赖性蛋白激酶(CDPK)基因,TaCDPK5/TaCDPK9-1,它们被聚类到第Ⅰ组,并且受盐、脱落酸(ABA)和聚乙二醇(PEG)处理诱导。RT-qPCR 结果表明,盐诱导的 TabZIP60 的表达水平被 Ca 通道阻滞剂 LaCl 显著抑制。TaCDPK5/TaCDPK9-1 参与了 TabZIP60 蛋白在体内和体外的相互作用。并且 TaCDPK5/TaCDPK9-1 可以以 Ca 依赖性方式自我磷酸化和磷酸化 TabZIP60 蛋白。突变分析表明,TabZIP60 的丝氨酸-110 是 TaCDPK5/TaCDPK9-1-TabZIP60 相互作用所必需的,并且是 TaCDPK5/TaCDPK9-1 激酶的磷酸化位点。酵母双杂交试验结果表明 TaCDPK5/TaCDPK9-1 分别与小麦蛋白磷酸酶 2C 家族 A TaPP2CA116/TaPP2CA121 互作。这些发现表明,由 TaPP2CA116/TaPP2CA121 和 TaCDPK5/TaCDPK9-1 控制的 TabZIP60 的磷酸化状态可能在小麦的盐胁迫过程中发挥关键作用。

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