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. Author manuscript; available in PMC: 2019 Feb 6.
Published in final edited form as: Structure. 2017 Dec 28;26(2):209–224.e6. doi: 10.1016/j.str.2017.12.002

Figure 2. Y2H Mapping of the Bicc1-ANKS3-ANKS6 Interaction Network.

Figure 2.

Full-length (FL) human Bicc1, truncated KH (residues 1–414), IVS (415–872), and SAM-domain (873–974) fragments, and full-length ANKS3 and ANKS6 and their respective ANK (34–220 and 8–423, respectively) and SAM (425–488 and 773–836, respectively) domains were used as baits and preys in yeast two-hybrid (Y2H) assays. A growth control in non-selective medium without leucine (L) and tryptophan (T) is shown in the first column (L‒T‒). Interactions are revealed in triple selective medium (L‒T‒H‒) lacking histidine, supplemented with the indicated increasing amounts of 3-aminotriazole (3-AT).

(A–I) Each panel shows one bait protein fused to the DNA-binding domain of Gal4 (Gal4-BD) and the strength of its interactions with all candidate preys fused to Gal4 activation domain (Gal4-AD).

(J) Summary of protein interactions observed in Y2H assays. 3-AT resistance values determined for each interaction were used to define an interaction strength scale (box) from the weakest (thin dotted black line) to the strongest (thick solid red line).