A novel wheat S1-bZIP gene, TabZIP11-D, confers stress resistance in Arabidopsis

Most subgroup S1 basic leucine zipper (bZIP) transcription factors (TFs) play a crucial role in the abiotic stress responses. However, their functions and molecular mechanisms remain poorly characterized in wheat (Triticum aestivum L.). In this study, we identified a novel subgroup S1 bZIP gene, designated TabZIP11-D, which was transcriptionally responsive to abscisic acid (ABA), salt, and cold stresses. TabZIP11-D encodes a nuclear-localized protein that lacks transcriptional activation activity in yeast. The Ca²⁺ blocker LaCl₃ significantly suppressed the salt-induced expression of TabZIP11-D. TabZIP11-D interacted with the Ca²⁺-dependent protein kinases (TaCDPK1, TaCDPK5, TaCDPK9-1, and TaCDPK30) and the CBL-interacting protein kinase TaCIPK31. Overexpression of TabZIP11-D enhanced salt and freezing tolerance by modulating soluble sugar and proline accumulation, reducing hydrogen peroxide (H₂O₂) and malondialdehyde (MDA) contents, and regulating the expression levels of stress-responsive genes. Furthermore, TabZIP11-D formed a homodimer with itself and heterodimers with group C bZIP proteins. Modified yeast one-hybrid assays revealed that TabZIP14 and TabZIP36 significantly enhanced TabZIP11-D binding to the G-box cis-element in the promoter region of TaCBF1 gene. These findings demonstrate that TabZIP11-D heterodimerizes with TabZIP14/36 to regulate cold signaling by promoting the TaCBF1 transcription. TabZIP11-D functions as a positive regulator in the salt stress response by interacting with TaCDPK1/5/9-1/30 and TaCIPK31.