The bacterial two hybrid system is developed based on the activity of recombination mediated by the interaction of adenylate cyclase in Escherichia coli. It utilizes the domains and functions of two complementary fragments T25 and T18 of Bordetella pertussis adenylate cyclase (CyaA). When T25 and T18 are physically separated, they are inactive. When these two fragments fuse into the interacting peptides X and Y, the heterodimerization of these heterozygous proteins leads to functional complementarity between the T25 and T18 fragments, at which point cAMP synthesis occurs. The cyclic AMP produced by recombinant chimeric enzyme and the metabolite then activate CAP protein. The cAMP/CAP complex is a multifunctional regulatory factor of genes transcribed in Escherichia coli, thereby activating the expression of reporter genes.
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