THE STABLE BACTERIOCIN RELEASE PROTEIN SIGNAL PEPTIDE, EXPRESSED AS A SEPARATE ENTITY, FUNCTIONS IN THE RELEASE OF CLOACIN DF13

被引：7

作者：

VANDERWAL, FJ ^{[1
]}

TENHAGEN, CM ^{[1
]}

OUDEGA, B ^{[1
]}

LUIRINK, J ^{[1
]}

机构：

[1] FREE UNIV AMSTERDAM,FAC BIOL,BIOCTR AMSTERDAM,IMBW,DEPT MOLEC MICROBIOL,1081 HV AMSTERDAM,NETHERLANDS

来源：

FEMS MICROBIOLOGY LETTERS | 1995年 / 131卷 / 02期

关键词：

BACTERIOCIN RELEASE; ESCHERICHIA COLI; SIGNAL PEPTIDE; PRECURSOR PROCESSING; LIPOPROTEIN; OUTER MEMBRANE;

D O I：

10.1016/0378-1097(95)00255-4

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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 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.

引用

页码：173 / 177

页数：5

共 25 条

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