Figure 3
Figure 3. Gfi1 interacts with Triad1. (A) Schematic representation of Gfi1 and Gfi1B. The Triad1-interacting part of Gfi1B found in yeast 2-hybrid (indicated with the solid-line Y2H) contains the 6 zinc fingers that are 97% identical to Gfi1. (B) Like Gfi1B, full-length and the 6–zinc finger domain of Gfi1 also interacts with His-Triad1. No interaction was detected with the Δzinc finger domain of Gfi1. (C) GFP-Triad1 or GFP was cotransfected with Flag-Gfi1 in COS cells. α-Flag staining of whole-cell extract (wce) showed equal expression of Gfi1. α-Flag staining of the α-GFP immunoprecipitates showed that Gfi1 interacts with Triad1 but not with GFP alone. α-GFP staining (α-GFP sc-8334; Santa Cruz Biotechnology) of the immunoprecipitated proteins showed successful immunoprecipitation.

Gfi1 interacts with Triad1. (A) Schematic representation of Gfi1 and Gfi1B. The Triad1-interacting part of Gfi1B found in yeast 2-hybrid (indicated with the solid-line Y2H) contains the 6 zinc fingers that are 97% identical to Gfi1. (B) Like Gfi1B, full-length and the 6–zinc finger domain of Gfi1 also interacts with His-Triad1. No interaction was detected with the Δzinc finger domain of Gfi1. (C) GFP-Triad1 or GFP was cotransfected with Flag-Gfi1 in COS cells. α-Flag staining of whole-cell extract (wce) showed equal expression of Gfi1. α-Flag staining of the α-GFP immunoprecipitates showed that Gfi1 interacts with Triad1 but not with GFP alone. α-GFP staining (α-GFP sc-8334; Santa Cruz Biotechnology) of the immunoprecipitated proteins showed successful immunoprecipitation.

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