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. Author manuscript; available in PMC: 2017 Jun 19.
Published in final edited form as: J Mol Biol. 2016 Mar 22;428(12):2557–2568. doi: 10.1016/j.jmb.2016.03.008

Figure 4. ΔL1 TEAD DBD exists largely in the monomeric form.

Figure 4

Figure 4

A. Results of gel filtration chromatography show that the major peak corresponding to ΔL1 TEAD DBD elutes at volumes corresponding to monomers (red triangle). TEAD DBD elutes at 12kD (green square). Proteins used for molecular weight calibration of the Sephacryl S200 XK 16/60 column are shown as filled diamonds.
Curvefitparameters:y=-0.198ln(x)+2.6991;R2=0.9828

B. DNA binding by monomeric and multimeric fractions of TEAD DBD and ΔL1 TEAD DBD. Fractions from size exclusion chromatography that correspond to monomeric TEAD DBD (a), monomeric ΔL1 TEAD DBD, multimeric TEAD DBD (c), and multimeric ΔL1 TEAD DBD (d) were used for EMSA. Arrowhead indicates free DNA at 2 fmol/lane. Protein concentrations: lane 1: 0; lanes 2–8 & 9–15: 0.3, 1, 3, 10, 30, 100, 300 nM.

C. SDS-PAGE of the four samples used for EMSA and molecular weight markers (M) (Bio-Rad, Kaleidoscope). (kD): Molecular weights of markers in kilodaltons.