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  • Title: Expression in Escherichia coli of the carboxy terminal domain of the BLAR sensory-transducer protein of Bacillus licheniformis as a water-soluble Mr 26,000 penicillin-binding protein.
    Author: Joris B, Ledent P, Kobayashi T, Lampen JO, Ghuysen JM.
    Journal: FEMS Microbiol Lett; 1990 Jun 15; 58(1):107-13. PubMed ID: 2204571.
    Abstract:
    A cloning vector has been constructed which allows production and export by Escherichia coli of the Met346-Arg601 carboxy terminal domain of the 601 amino acid BLAR sensory-transducer involved in beta-lactamase inducibility in Bacillus licheniformis. The polypeptide, referred to as BLAR-CTD, accumulates in the periplasm of E. coli in the form of a water-soluble, Mr 26,000 penicillin-binding protein. These data and homology searches suggest that BLAR has a membrane topology similar to that of other sensory-transducers involved in chemotaxis.
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