Tamarix hispida ThEIL1 improves salt tolerance by adjusting osmotic potential and increasing reactive oxygen species scavenging capability.

The ETHYLENE INSENSITIVE 3-LIKE (EIL) transcription factor (TF) family plays a key role in the ethylene signal transduction pathway. However, it is still unknown how EIL proteins mediate salt tolerance in Tamarix hispida. Here, we cloned and functionally characterized the TF ThEIL1 from T. hispida. ThEIL1 is a nuclear protein possessing transcriptional activation activity. In addition to binding to the PERE motif (GGATTCAA), a novel EIL protein-DNA interaction was identified, in which ThEIL1 binds to GCC-box (AGCCGCC). Gain- and loss-of-function analysis in T. hispida showed that ThEIL1 regulates the expression of trehalose-6-phosphate synthase (TPS), pyrroline-5-carboxylate synthetase (P5CS), and trehalose-6-phosphate phosphatase (TPP) to mediate the biosynthesis of proline and trehalose, respectively, thereby elevating osmotic potential. Additionally, ThEIL1 controls the activities of peroxidase (POD) and superoxide dismutase (SOD) by regulating the expression of genes encoding SODs and PODs , leading to increased reactive oxygen species scavenging capability. Moreover, overexpression of ThEIL1 in Arabidopsis significantly increased root length and fresh weight under salt treatment conditions. Furthermore, the physiological traits of T. hispida were consistent with those of Arabidopsis stably overexpressing ThEIL1. Thus, ThEIL1 serves as a TF that mediates salt tolerance by elevating osmotic potential and improving ROS scavenging capability. • ThEIL1 confers salt tolerance to Tamarix hispida and Arabidopsis. • ThEIL1 binds to GCC-box (AGCCGCC) to regulate gene expression. • Overexpression of ThEIL1 increases proline and trehalose contents. • ThEIL1 expression improves ROS scavenging capability. [ABSTRACT FROM AUTHOR]