Bacteriocins are narrow-spectrum protein antibiotics released to kill related bacteria of the same niche. Uptake of bacteriocins depends critically on the presence of an uptake receptor in the outer membrane, a translocation pore and an energy-dependent activating system of the inner membrane. Most bacteriocins act on the inner membrane as pore-forming toxins or they target cytoplasmic DNA/RNA and ribosomal synthesis respectively. Only two bacteriocins are known to become activated in the periplasmic space and to inhibit the renewal process of the peptidoglycan structure. In Escherichia coli, the Cma (colicin M) phosphatase is activated in the periplasmic space by the FkpA chaperone and subsequently degrades the C55-PP precursor unit of the peptidoglycan. Pst (pesticin) from Yersinia pestis carries a lysozyme homology domain to degrade peptidoglycan. Import of Pst is only achieved if the N-terminal translocation domain can span the outer membrane and if extensive unfolding of the protein during membrane passage is permitted. There is considerable plasticity in the import pathway since a chimaera comprising the activity domain replaced by T4 lysozyme is also translocated and active in killing those bacteria carrying the FyuA receptor.
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December 2012
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Conference Article|
November 21 2012
Structure and uptake mechanism of bacteriocins targeting peptidoglycan renewal
Kornelius Zeth
Kornelius Zeth
1
1Biozentrum, University of Basel, Klingelbergstrasse 50/70, 4053 Basel, Switzerland
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Publisher: Portland Press Ltd
Received:
July 31 2012
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© 2012 The Authors Journal
2012
Biochem Soc Trans (2012) 40 (6): 1560–1565.
Article history
Received:
July 31 2012
Citation
Kornelius Zeth; Structure and uptake mechanism of bacteriocins targeting peptidoglycan renewal. Biochem Soc Trans 1 December 2012; 40 (6): 1560–1565. doi: https://doi.org/10.1042/BST20120194
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