The stable bacteriocin release protein signal peptide, expressed as a separate entity, functions in the release of cloacin DF13 |
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Authors: | Fimme J van der Wal Corinne M ten Hagen Bauke Oudega Joen Luirink |
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Institution: | Department of Molecular Microbiology, IMBW, BioCentrum Amsterdam, Faculty of Biology, Vrije Universiteit, De Boelelaan 1087, 1081 HV Amsterdam, the Netherlands |
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Abstract: | Abstract The pCloDF1S encoded bacteriocin release protein (BRP) plays a role in the release of the bacteriocin cloacin DF13. The BRP signal peptide is stable after cleavage, and accumulates in the cytoplasmic membrane. A BRP which is correctly targeted by the unstable murein lipoprotein signal peptide (Lpp-BRP) is not capable of inducing the release of cloacin DF13. To investigate the role of the stable BRP signal peptide in the release of cloacin DF13, the stable BRP signal peptide and the Lpp-BRP were expressed in trans in cells also producing cloacin DF13. Expression and release experiments indicate that the stable signal peptide can complement the Lpp-BRP in the release of cloacin DF13. |
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Keywords: | Bacteriocin release Escherichia coli Signal peptide Precursor processing Lipoprotein Outer membrane |
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