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Changes in the periplasmic linker and in the expression level affect the activity of ToxR and λ‐ToxR fusion proteins in Escherichia coli
Author(s) -
Jappelli Roberto,
Brenner Sydney
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00125-2
Subject(s) - periplasmic space , escherichia coli , fusion protein , transmembrane protein , repressor , biochemistry , biology , plasmid , bacteriophage , chemistry , dna , gene , recombinant dna , gene expression , receptor
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.