FIG 3.
CdaA-CdaR complex formation. (A) B2H analysis for studying the interactions between full-length and truncated CdaA and CdaR variants. N-CdaA and C-CdaA represent domains of the Bordetella pertussis adenylate cyclase that are fused to the N and C termini of the proteins, respectively. Δ80CdaA and Δ28CdaR are truncated proteins lacking the N-terminal 80 and 28 amino acids, respectively. Probably due to the toxic effects of the diadenylate cyclase, we have failed to combine the N-CdaA fusion proteins in E. coli (23). C-CdaR and N-CdaA fusions are most likely inactive because many of the adenylate cyclase domains are not cytosolic. (B) Model illustrating the localization of CdaR and CdaA and the interaction of the proteins in L. monocytogenes. CW, cell wall; M, membrane.