Changes in the periplasmic linker and in the expression level affect the activity of ToxR and λ-ToxR fusion proteins in Escherichia coli
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Add time:08/29/2019 Source:sciencedirect.com
In order to assess the potentiality of Vibrio cholerae ToxR protein and of bacteriophage λ repressor as indicators of the dimerization of periplasmic proteins in Escherichia coli, we have constructed a series of plasmids encoding transmembrane fusion proteins. The amino-terminal part, containing the DNA binding domain of either ToxR or λ repressor, is located in the cytoplasm and acts as reporter for dimerization. As models of periplasmic proteins we have used alkaline phosphatase (a dimer) and β-lactamase (a monomer). Both the expression level and the distance between the transmembrane segment and the periplasmic protein substantially affect the activity of the reporter domains.
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