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. 2021 Nov 17;22(22):12400. doi: 10.3390/ijms222212400

Figure 1.

Figure 1

Two new C2H2 proteins that interact with the BTB domain of CP190. (a) Summary of the mapping of the interaction between CG31365 and CP190 proteins in pull-down and yeast two-hybrid (Y2H) assays. An uncertain interaction is shown in brackets. For Y2H, different fragments of CG31365 were fused with the GAL4 activation domain and tested for interaction with the CP190 BTB domain fused to the GAL4 DNA-binding domain (GAL4 BD). GAL4 BD serves as the negative control. The growth assay yeast plates are shown in Supplementary Materials Figure S2. (b) Mapping of the interaction between CG31365 and CP190 proteins using pull-down assays. The uncropped images are shown in the Supplementary Materials Figure S3. (c) Co-immunoprecipitation of CP190 and CG31365 tagged with FLAG in extracts from Drosophila S2 cells. Total extracts were immunoprecipitated with FLAG antibodies. The immunoprecipitates (IPs) were analyzed by Western blotting. The uncropped images are shown in Supplementary Materials Figure S1. (d) Summary of the mapping of the interaction between CG4730 and CP190 proteins in pull-down and Y2H assays. Designations are the same as in panel (a). (e) Mapping of the interaction between CG4730 and CP190 proteins using pull-down assays. The uncropped images are shown in the Supplementary Materials Figure S3. (f) Co-immunoprecipitation of CP190 and CG4730 tagged with FLAG in extracts from Drosophila S2 cells. Total extracts were immunoprecipitated with FLAG antibodies. The immunoprecipitates (IPs) were analyzed by Western blotting. The uncropped images are shown in the Supplementary Materials Figure S1.