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. 2007 Feb 15;26(5):1444–1455. doi: 10.1038/sj.emboj.7601577

Figure 2.

Figure 2

B. abortus PleC, DivJ and PdhS interact with DivK through their C-terminal domain. (A) Yeast two-hybrid assay showing physical interactions between the B. abortus response regulator DivK and the histidine kinases PleC, DivJ and PdhS. Activation of lacZ reporter gene was demonstrated as formation of blue colonies on plates containing X-Gal. Activation of HIS3 reporter gene was measured as growth on plates without histidine but with 3-AT. ‘*' Represents truncated forms of PleC and DivJ fused to AD, which comprised the HATPase_C domain and excluded the predicted transmembrane domains. (B) Yeast two-hybrid assay demonstrating that the N-terminal domain of PdhS is required for its dimerization, and its C-terminal domain, comprising the HATPase_C and PAS domains, is involved in the interaction with DivK. As in (A), activation of HIS3 reporter gene was measured as growth on plates without histidine but with 3-AT. AD and BD represent the activation and binding domains of Gal4, respectively. At least three independent experiments were performed for each yeast two-hybrid assay.