van der Wal F J, ten Hagen C M, Oudega B, Luirink J
Department of Molecular Microbiology, Vrije Universiteit, Amsterdam, The Netherlands.
FEMS Microbiol Lett. 1995 Sep 1;131(2):173-7. doi: 10.1111/j.1574-6968.1995.tb07773.x.
The pCloDF13 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 murecin 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 DF 13.
