TabZIP60 is involved in the regulation of ABA synthesis-mediated salt tolerance through interacting with TaCDPK30 in wheat (Triticum aestivum L.).

Abstract

TabZIP60 is found to interact with TaCDPK30 and act as a positive regulator of ABA synthesis-mediated salt tolerance in wheat. Wheat basic leucine zipper (bZIP) transcription factor (TabZIP60) was previously found to act as a positive regulator of salt resistance. However, its molecular mechanism in response to salt stress in wheat is still unclear. In this study, TabZIP60 was found to interact with wheat calcium-dependent protein kinase (TaCDPK30), which belonged to group III of CDPK family, and was induced by salt, polyethylene glycol, and abscisic acid (ABA) treatments. This mutation of serine 110 in TabZIP60 resulted in no interaction with TaCDPK30. Moreover, TaCDPK30 was involved in interactions with wheat protein phosphatase 2C clade A (TaPP2CA116/TaPP2CA121). TabZIP60-overexpressing wheat plants showed increased salt tolerance, as exhibited by better growth status, higher soluble sugar, and lower malonaldehyde contents of transgenic plants than wild-type wheat cv. Kenong 199 under salt stress. Moreover, transgenic lines showed high ABA content by upregulating ABA synthesis-related gene expression levels. TabZIP60 protein could bind and interact with the promoter of the wheat nine-cis epoxycarotenoid dioxygenase (TaNCED2) gene. Furthermore, TabZIP60 upregulated several stress response gene expression levels, which could also increase the plant's ability to resist salt stress. Thus, these results suggest that TabZIP60 could function as a regulator of ABA synthesis-mediated salt tolerance through interacting with TaCDPK30 in wheat.