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. 2019 Dec 13;9:19102. doi: 10.1038/s41598-019-55617-6

Figure 1.

Figure 1

Summary of the interactions between HIPP1 and insulator proteins in the yeast two-hybrid assay. (a) Structural scheme of HIPP1, CP190, and Su(Hw) proteins, showing their domains and the corresponding numbers of the amino acid residues: CID, CP190 interaction domain; Cr, crotonase-fold domain; BTB, BTB/POZ domain; D, aspartic acid-rich (D-rich) domain; M, centrosomal targeting domain; E, C-terminal glutamic acid-rich domain; Zf, zinc-finger domain; LZ, leucine zipper motif; CTAD, C-terminal acidic domain. The vertical arrow under the scheme of the Su(Hw) protein indicates the Su(Hw)Δ283 mutation. (b) The results of testing interactions between HIPP1 domains. (c) The results of testing HIPP1 domains for interactions with CP190 and Su(Hw) proteins. (d) The results of testing CP190 and Su(Hw) domains for interactions with HIPP1 protein. All experiments were performed in triplicate. Numbers in brackets indicate amino acid residues flanking the protein regions included in analysis. The plus signs indicate the relative strength of two-hybrid interactions (Fig. S1); the minus sign indicates the absence of the interaction; the asterisk indicates that the interaction was observed only when the DBD of GAL4 was fused to the C-terminal region of HIPP1 derivatives.