PMID:3054422
| Citation |
Jackson, ME and Pratt, JM (1988) Analysis of the membrane-binding domain of penicillin-binding protein 5 of Escherichia coli. Mol. Microbiol. 2:563-8 |
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| Abstract |
Internal deletions close to the C-terminus of the Escherichia coli penicillin binding protein 5 (PBP5, DacA) have defined the C-terminal 18 residues of the protein as essential for membrane binding. This C-terminal sequence is capable of forming a strongly amphiphilic alpha-helix. In this paper we show that the PBP5 amphiphilic helix is able to anchor the periplasmic TEM-beta-lactamase to the inner membrane. In addition, we have demonstrated that mature PBP5 (lacking the N-terminal signal sequence) possesses the ability to bind to the membrane from a soluble form of the protein, showing that translocation across the membrane is unnecessary for anchoring to be established. |
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| Keywords |
Amino Acid Sequence; Bacterial Proteins; Biological Transport; Blotting, Western; Carrier Proteins/genetics; Carrier Proteins/metabolism; Electrophoresis, Polyacrylamide Gel; Escherichia coli/genetics; Escherichia coli/metabolism; Hexosyltransferases; Membrane Proteins/genetics; Membrane Proteins/metabolism; Molecular Sequence Data; Muramoylpentapeptide Carboxypeptidase/genetics; Muramoylpentapeptide Carboxypeptidase/metabolism; Mutation; Penicillin-Binding Proteins; Peptide Fragments/genetics; Peptide Fragments/metabolism; Peptidyl Transferases; Plasmids; Protein Sorting Signals/genetics; Protein Sorting Signals/metabolism; Recombinant Fusion Proteins/genetics; Recombinant Fusion Proteins/metabolism; beta-Lactamases/metabolism |
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