Extended Data Fig. 7: The putative interaction between a metal ion and the four cysteine residues stabilizes the structure of the CDF2DOF domain in an appropriate conformation for DNA binding. | Nature Plants

Extended Data Fig. 7: The putative interaction between a metal ion and the four cysteine residues stabilizes the structure of the CDF2DOF domain in an appropriate conformation for DNA binding.

From: PIF4 enhances DNA binding of CDF2 to co-regulate target gene expression and promote Arabidopsis hypocotyl cell elongation

Extended Data Fig. 7

The putative interaction between a metal ion and the four cysteine residues stabilizes the structure of the CDF2DOF domain in an appropriate conformation for DNA binding. a, Modelled structure of the CDF2DOF domain with the four cysteine residues (C140, C143, C165 and C168) highlighted. Removal of the metal ion by adding a divalent metal chelator destabilizes the structure. b, Size-exclusion chromatography analysis of CDF2DOF WT protein. The CDF2DOF domain is fused with an MBP tag at the N terminus. The x-axis and y-axis indicate the elution volume and the protein absorption at 280 nm, respectively. c, Gel-shift analysis of the interactions between CDF2DOF WT, Mu1 proteins and DNA in various concentrations of EDTA. Size-exclusion chromatography analysis in b and EMSA assays in c were performed twice with similar results.

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