Efficient and exclusive induction of Tet repressor by the oligopeptide Tip results from co-variation of their interaction site.

ABSTRACT: Protein-protein interactions are an important element of signal transfer within and between organisms. They are mainly mediated by short oligopeptide motifs and represent a widely used alternative to small, organic molecules for conveying information. The transcription factor TetR, a regulator of tetracycline resistance in Gram-negative bacteria, is naturally induced by tetracycline or its derivatives. The oligopeptide Tip (Transcription inducing peptide) fused to either N- or C-terminus of Thioredoxin A (TrxA) has been isolated as an artificial inducer for TetR in Escherichia coli. This inducing property can be exploited to monitor the in vivo expression of a protein of interest by fusing Tip to its C-terminus. We improve the induction efficiency of Tip by adding an aromatic amino acid be

SUBMITTER: Klotzsche M 

PROVIDER: S-EPMC1919500 | biostudies-literature | 2007

REPOSITORIES: biostudies-literature