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Fig. 3 | BMC Biology

Fig. 3

From: Functional role of dimerization and CP190 interacting domains of CTCF protein in Drosophila melanogaster

Fig. 3

a Domain structure of the Drosophila CP190 protein. b Mapping dCTCF and CP190 interaction modules using the yeast two-hybrid assay. c Analysis of interactions between purified recombinant GST-dCTCF-CTD and 6xHis-CP190 by GST-pull-down assay. GST-dCTCF-CTD bound to glutathione agarose beads was incubated with bacterially expressed 6xHis-CP190. After successive washes, the GST-dCTCF-CTD protein was eluted from the beads with excess glutathione. d Analysis of interactions between recombinant GST-dCTCF-CTD and CP190 from Drosophila S2 cells nuclear lysate by GST-pull-down assay. An S2 nuclear extract was incubated with recombinant GST-dCTCF-CTD bound to glutathione agarose beads. After washing and elution with excess glutathione, CP190 and GAF association was assayed by western blotting. e Immunoprecipitation of FLAG-tagged dCTCF full-length and deletion mutants with CP190 antibodies. f Mapping of CTCF-interaction region within CP190 protein using GST-pull-down assay. AD activating domain, BD binding domain, S2 Schneider 2 cells

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