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Figure 10 The ToxR, E. coli dimerization system. In Vibrio cholerae, ToxR is expressed as a cytoplasmic membrane protein that acts as a transcription factor interacting with the Ctx promoter directly with its cytoplasmic domain when it is induced to dimerize by interaction with ToxS. The ToxR protein has been cloned and expressed in E. coli to study the dimerization of proteins. The extraceullular dimerization domain of ToxR is replaced with the protein of choice, in this example the immunoglobulin variable domain and expressed in E. coli. The Ctx promoter is also cloned into E. coli and the toxin gene is replaced by a reporter such as lacZ. When the immunoglobulin domains dimerize, the cytoplasmic domain of ToxR is activated and lacZ is expressed.

Figure 10 The ToxR, E. coli dimerization system. In Vibrio cholerae, ToxR is expressed as a cytoplasmic membrane protein that acts as a transcription factor interacting with the Ctx promoter directly with its cytoplasmic domain when it is induced to dimerize by interaction with ToxS. The ToxR protein has been cloned and expressed in E. coli to study the dimerization of proteins. The extraceullular dimerization domain of ToxR is replaced with the protein of choice, in this example the immunoglobulin variable domain and expressed in E. coli. The Ctx promoter is also cloned into E. coli and the toxin gene is replaced by a reporter such as lacZ. When the immunoglobulin domains dimerize, the cytoplasmic domain of ToxR is activated and lacZ is expressed.

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