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. 2022 Oct 18;35(1):552–573. doi: 10.1093/plcell/koac308

Figure 1.

Figure 1

VvMYB30 interacts physically with VvWRKY8. A, Y2H assay. Yeast cells co-transformed with VvMYB30 fused to the GAL4 activation domain and VvWRKY8 fused to the GAL4 binding domain were grown on selective media. AD-T/BD-53 was used as a positive control. VvMYB30-AD/BD, AD/VvWRKY8-BD, and AD-T/BD-lam were used as negative controls. B, In vitro pull-down assay. VvWRKY8 was fused with SUMO and HIS tags, and the molecular weights were almost 30 kD, VvMYB30 were fused with GST tag, and the molecular weight was almost 55 kD. VvMYB30 and GST were detected by GST tag monoclonal antibody, VvWRKY8 were detected by HIS tag monoclonal antibody. C, BiFC assay. VvWRKY8 was fused with the nYFP, VvMYB30 were fused with the cYFP, and the combinations of VvMYB30-cYFP/VvWRKY8-nYFP, VvMYB30-cYFP/nYFP, and cYFP/VvWRKY8-nYFP were expressed in N. benthamiana leaves, respectively. Scale bar: 20 μm. D, Co-IP assays in N. benthamiana leaves, the molecular weight of VvWRKY8 and VvMYB30 was almost 25 and 40 kD, respectively. α-cMYC, cMYC tag monoclonal antibody; α-FLAG, FLAG tag polyclonal antibody.