Abstract
Bacteriocins are bactericidal proteins that are produced by bacteria. They usually kill only bacterial cells that are closely related to the producing bacteria. The narrow host range is determined by the sophisticated uptake mechanisms that these proteins use to enter susceptible bacterial cells. Bacteriocins range in size from rather small toxic peptides to relatively large protein structures of 60–70 kDa. The relatively small bactericidal peptides include microcins and lantibiotics (De Vos et al., 1995), most of which are apparently exported by the producing cell via ABC transporters. This chapter will focus on the larger bacteriocins, especially on colicins and cloacin DF13, and on their mechanism of export. These bacteriocins are the best studied bacteriocins with respect to production, export, uptake and mode of action. These relatively large proteins are produced by Escherichia coli strains and by related gram-negative organisms. The mechanism by which these colicins are translo cated across both the inner membrane and the outer membrane to reach their extra-cellular destination is totally different from all other mechanisms studied so far. This process appears to be semi-specific and is often referred to as quasi-lysis. The exact mechanism is not known, but it has been applied for the production of heterologous proteins by E. coli. In this chapter, the mechanism of export of colicins and of cloacin DF13, and the biotechnological applications of this mechanism of export will be described.
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Oudega, B. (2003). Export of Bacteriocins. In: Oudega, B. (eds) Protein Secretion Pathways in Bacteria. Springer, Dordrecht. https://doi.org/10.1007/978-94-010-0095-6_12
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DOI: https://doi.org/10.1007/978-94-010-0095-6_12
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