American Society of Hematology

Fig. 3.

$Fig. 3. Alterations in the DNA binding and heterodimerization activities of the Runt domain of FPD/AML RUNX1 mutations. / (A) Partial RUNX1 proteins (as indicated) were subjected to EMSA in the presence (+) and absence (−) of PEBP2β/CBFβ. WT indicates wild-type RUNX1. The position of the RUNX1 and RUNX1/CBFβ complexes with the DNA are indicated. (B) Affinity assay of the indicated partial RUNX1 proteins with PEBP2β/CBFβ. M indicates molecular weight marker as indicated both to the left and right; β, PEBP2β/CBFβ; A, input RUNX1 protein; W, unbound proteins in washed fractions; E, bound proteins eluted at 250 mM imidazole. The bands marked with arrows indicate the β subunits associated with RUNX1 proteins.$

Alterations in the DNA binding and heterodimerization activities of the Runt domain of FPD/AML RUNX1 mutations.

(A) Partial RUNX1 proteins (as indicated) were subjected to EMSA in the presence (+) and absence (−) of PEBP2β/CBFβ. WT indicates wild-type RUNX1. The position of the RUNX1 and RUNX1/CBFβ complexes with the DNA are indicated. (B) Affinity assay of the indicated partial RUNX1 proteins with PEBP2β/CBFβ. M indicates molecular weight marker as indicated both to the left and right; β, PEBP2β/CBFβ; A, input RUNX1 protein; W, unbound proteins in washed fractions; E, bound proteins eluted at 250 mM imidazole. The bands marked with arrows indicate the β subunits associated with RUNX1 proteins.

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