Fig. 4: Modeling of CBP and HSF2 interaction.

a Amino acid sequence of the KIX-binding motifs located in the HSF2 HR-A/B region. Blue rectangle, conserved KIX-binding motif sequences (“ΦXXΦΦ”). Purple boxes, positions of the very conserved and major acetylated lysine residues; K82 (blue) is located in the DBD, K128, K135, and K197 (red) are located in the HR-A/B and K209/K210 (black) is located downstream the HR-A/B. b In silico model structure of the CBP KIX domain and the HSF2 HR-A/B domain interaction. Representation of the HSF2 HR-A/B domains In the HSF2 trimer, as a triple-coiled coil (in blue). The KIX recognition motifs of HSF2 are indicated in red. Representation of the KIX domain of CBP, a triple helical globular domain (in green). The c-Myb surface of the KIX domain is indicated in red. c In silico model. Magnification of the HSF2 and CBP interaction domains shown in b showing the tyrosine residue Y650 (pale blue) within the c-Myb surface of the CBP KIX domain in contact with the KIX recognition motifs of the HSF2 HR-A/B domain. d In silico model representation of the position of the four residues of HSF2 KIX recognition motifs and of Y650 of the CBP KIX domain that have been analyzed by in silico mutation. e In silico Y650A mutation disrupts interaction between the HSF2 KIX motifs and the CBP KIX domain (Firedock analysis). f Representative immunoblots of immunoprecipitated CBP KIX domain (IP GST) after in vitro interaction experiments between wild-type or mutated CBP KIX-GST and SNAP-HSF2 recombinant proteins produced in bacteria and reticulocyte lysates showing Y650A mutation disrupts interaction between the HSF2 KIX motifs and the CBP KIX domain (n = 3). lc IgG light chain. The left and right immunoblots correspond to two independent experiments. Source data are provided as a Source Data file.