Loss of function and inhibitory effects of human CSX/NKX2.5 homeoprotein mutations associated with congenital heart disease
J. Clin. Invest. Hideko Kasahara, et al. 106:299 doi:10.1172/JCI9860 [Go to this article.]

Figure 4
DNA binding affinity of the group 3 and 4 mutant proteins versus wild-type CSX/NKX2.5. Sequence of the native –242 bp site (top) and a mutated –242 bp binding site (bottom) in the ANF promoter. EMSA of group 3 (M198 and M259) and group 4 (M25, the mutation site is marked with an asterisk) protein compared with that of the wild-type CSX/NKX2.5. Proteins were mixed with probes containing either tandemly repeated binding sites (a–d) or single binding site (e–h). Lanes showing similar monomer/dimer ratios are indicated with asterisks in the top panels (a–d). In all three mutant proteins, binding affinity as a dimer is reduced approximately 3- to 3² fold (b–d versus a), whereas they show similar DNA binding affinity as wild-type to the single binding site (f–h versus e). D, dimer; M, monomer; F, free probe.