Bacteriocin release proteins: mode of action, structure, and biotechnological application |
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Authors: | Fimme Jan van der Wal Joen Luirink Bauke Oudega |
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Affiliation: | Department of Molecular Microbiology, IMBW, BioCentrum Amsterdam, Faculty of Biology, De Boelelaan 1087, 1081 HV Amsterdam, The Netherlands |
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Abstract: | Abstract: The mechanisms by which Gram-negative bacteria like Escherichia coli secrete bacteriocins into the culture medium is unique and quite different from the mechanism by which other proteins are translocated across the two bacterial membranes, namely through the known branches of the general secretory pathway. The release of bacteriocins requires the expression and activity of a so-called bacteriocin release protein and the presence of the detergent-resistant phospholipase A in the outer membrane. The bacteriocin release proteins are highly expressed small lipoproteins which are synthesized with a signal peptide that remains stable and which accumulates in the cytoplasmic membrane after cleavage. The combined action of these stable, accumulated signal peptides, the lipid-modified mature bacteriocin release proteins (BRPs) and phospholipase A cause the release of bacteriocins. The structure and mode of action of these BRPs as well as their application in the release of heterologous proteins by E. coli is described in this review. |
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Keywords: | Bacteriocin release protein Escherichia coli Gram-negative bacteria Heterologous protein release Stable signal peptide Biotechnology |
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