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J. Bacteriol., 01 1998, 96-99, Vol 180, No. 1
Copyright © 1998, American Society for Microbiology

Mechanistic properties of the two-component bacteriocin lactococcin G [In Process Citation]

G Moll, H Hildeng-Hauge, J Nissen-Meyer, IF Nes, WN Konings and AJ Driessen
Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Haren, The Netherlands.

Lactococcin G is a bacteriocin whose activity depends on the complementary action of two peptides, termed alpha and beta. Biologically active, synthetic lactococcin G was used to study the mode of action on sensitive cells of Lactococcus lactis. The alpha and beta peptides can bind independently to the target cell surface, but activity requires the complementary peptide. Once bound to the cell surface, the peptides cannot be displaced to the surfaces of other cells. A complex of alpha and beta peptides forms a transmembrane pore that conducts monovalent cations but not protons. Efflux of potassium ions is observed only above pH 5.0, and the rate of efflux increases steeply with the pH. The consequences of cation fluxes for the viability of the target cells are discussed.

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