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. 1988 Mar;7(3):867–873. doi: 10.1002/j.1460-2075.1988.tb02886.x

A synthetic peptide corresponding to the C-terminal 25 residues of phage MS2 coded lysis protein dissipates the protonmotive force in Escherichia coli membrane vesicles by generating hydrophilic pores.

W H Goessens 1, A J Driessen 1, J Wilschut 1, J van Duin 1
PMCID: PMC454404  PMID: 2840287

Abstract

The RNA phage MS2 encodes a protein, 75 amino acids long, that is necessary and sufficient for lysis of the host cell. DNA deletion analysis has shown that the lytic activity is confined to the C-terminal half of the protein. We have examined the effects of a synthetic peptide, covering the C-terminal 25 amino acids of the lysis protein, on the electrochemical potential, generated in Escherichia coli membrane vesicles and in liposomes reconstituted with cytochrome c oxidase. In all cases the peptide dissipates the electrochemical potential. The peptide also induces the release of carboxyfluorescein (376 daltons), but not of inuline (5500 daltons), from protein-free liposomes. The phenomena are observed at a lipid to peptide molar ratio of approximately 100:1. The possible connection between the dissipation of the proton-motive force and bacteriolysis is discussed.

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Selected References

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