The Two-Peptide (Class-IIb) Bacteriocins: Genetics, Biosynthesis, Structure, and Mode of Action

  • Jon Nissen-Meyer
  • Camilla Oppegård
  • Per Rogne
  • Helen Sophie Haugen
  • Per Eugen Kristiansen


The two-peptide (class-IIb) bacteriocins consist of two different peptides, both of which are required to obtain high antimicrobial activity. These bacteriocins kill target-cells by inducing membrane-leakage and they seem to display some specificity with respect to the molecules they transfer across membranes. The genes encoding the two peptides of two-peptide bacteriocins are next to each other on the same operon. In the same or a nearby operon are genes encoding (i) the immunity protein that protects the bacteriocin-producer from its own bacteriocin, (ii) a dedicated ABC-transporter that exports the bacteriocin from cells and cleaves off the N-terminal bacteriocin leader sequence, and (iii) an accessory protein whose exact function has not been fully clarified. Some two-peptide bacteriocins appear to be produced constitutively, whereas the production of other two-peptide bacteriocins is regulated through a three-component regulatory system that consists of a peptide pheromone, a membrane-associated histidine protein kinase, and response regulators. It has recently been proposed that the two peptides of (some) two-peptide bacteriocins may form a membrane-penetrating helix-helix structure involving helix-helix interacting GxxxG-motifs present in all currently characterized two-peptide bacteriocins. It has also been suggested that the helix-helix structure interacts with an integrated membrane (transport) protein, thus inducing a conformational change in the protein, which in turn causes membrane-leakage. This proposed mode-of-action is similar to that of the pediocin-like (class-IIa) bacteriocins and lactococcin A, which bind to a part of the mannose phosphotransferase permease that is embedded in the cell membrane, thereby altering the conformation of the ­permease in a manner that causes membrane-leakage and cell death.


Circular Dichroism Transmembrane Helix Bacteriocin Production Helix Structure Immunity Protein 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  • Jon Nissen-Meyer
    • 1
  • Camilla Oppegård
  • Per Rogne
  • Helen Sophie Haugen
  • Per Eugen Kristiansen
  1. 1.Department of Molecular BiosciencesUniversity of OsloOsloNorway

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