Fig. 2

Binding of the Hox-GFP fusion proteins in Kc167 cells is mainly dependent on direct interaction with DNA. a The homeodomain sequence of Ubx protein. The Arg3, Arg5, Ile47, Gln50 and Asn51 residues, mediating DNA contacts in the major and minor groves (red in Ubx wild type) were mutated to Ala3, Ala5, Ala47, Lys50 and Ala51 (grey in Ubx mutant), abolishing the ability to bind DNA. The Ubx motif sequence logo is from the JASPAR database (MA0094.2). b Comparison of the binding profiles (with fragment pileup signal normalized per million reads) of wild type and mutant Ubx (Experiment 2), with the mutant showing a strong reduction in binding. c Venn diagram showing the overlap of binding peaks (q-value 1e−10) between Ubx wild type and mutant. About 66 % of Ubx wild type peaks do not overlap with Ubx mutant peaks