Figure 1: Both CXC domains of LIN54 are required for high-affinity DNA binding. | Nature Communications

Figure 1: Both CXC domains of LIN54 are required for high-affinity DNA binding.

From: Structural basis for LIN54 recognition of CHR elements in cell cycle-regulated promoters

Figure 1

(a) FP analysis of LIN54 DBD binding to TAMRA-labelled CHR27 DNA from the CDK1 promoter. The complete DBD binds CHR27 with affinity Kd=430±80 nM, whereas the individual CXC domains (DBD-N and DBD-C) do not show binding in this assay or when titrated together. Error bars show the s.d. for three experimental replicates. (b,c) HSQC NMR spectra of 15 N-labelled 100 μM DBD-N (b) and 440 μM DBD-C (c). Each spectrum shows peak dispersion that is typical of a folded domain and the peaks change on titration of CHR13 DNA in a manner that is consistent with weak affinity binding. For clarity, only the full spectra in the absence and presence of 8 × DNA concentration are shown. The complete spectra across DNA concentrations are shown in Supplementary Fig. 1.

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