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Figure 5 | BMC Evolutionary Biology

Figure 5

From: Evolution of a novel subfamily of nuclear receptors with members that each contain two DNA binding domains

Figure 5

Protein-protein interaction of Sm2DBDα. A. Yeast two hybrid assays show that S. mansoni 2DBD-NR (Sm2DBDα) can act as a homodimer but not as a heterodimer with SmRXR1 and SmRXR2. Yeast AH109 was transformed with 1 μg of the following co-transformats: 1) pGBK-Sm2DBDα-C-F/pACT-SmRXR1, 2) pGAD-Sm2DBDα/pAs-SmRXR1-C-F, 3) pGBK-Sm2DBDα-C-F/pGAD-Sm2DBDα, 4) negative control plasmid pSV40/plamin C, 5) positive control plasmid pSV40/p53, 6) pGBK-Sm2DBDα-C-F/pACT-SmRXR2, 7) pGAD-Sm2DBDα/pAS-SmRXR2. Transformed yeast were plated on SD/-trp-leu and SD/-trp-his-leu-ade plus 3 mM 3-amino-1,2,4-triazole (3-AT). The results show that Sm2DBDα can form a homodimer but not a heterodimer with SmRXRs. B. GST pull down verified that the S. mansoni 2DBDα-E-F domain, in which the dimer interface is located, can form a homodimer in vitro.

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