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• W1551207815 abstract "Research Article1 March 1988free access 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 W. H. Goessens Department of Biochemistry, University of Leiden, The Netherlands. Search for more papers by this author A. J. Driessen A. J. Driessen Department of Biochemistry, University of Leiden, The Netherlands. Search for more papers by this author J. Wilschut J. Wilschut Department of Biochemistry, University of Leiden, The Netherlands. Search for more papers by this author J. van Duin J. van Duin Department of Biochemistry, University of Leiden, The Netherlands. Search for more papers by this author W. H. Goessens W. H. Goessens Department of Biochemistry, University of Leiden, The Netherlands. Search for more papers by this author A. J. Driessen A. J. Driessen Department of Biochemistry, University of Leiden, The Netherlands. Search for more papers by this author J. Wilschut J. Wilschut Department of Biochemistry, University of Leiden, The Netherlands. Search for more papers by this author J. van Duin J. van Duin Department of Biochemistry, University of Leiden, The Netherlands. Search for more papers by this author Author Information W. H. Goessens1, A. J. Driessen1, J. Wilschut1 and J. Duin1 1Department of Biochemistry, University of Leiden, The Netherlands. The EMBO Journal (1988)7:867-873https://doi.org/10.1002/j.1460-2075.1988.tb02886.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info 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. Previous ArticleNext Article Volume 7Issue 31 March 1988In this issue RelatedDetailsLoading ..." @default.
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• W1551207815 title "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." @default.
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• W1551207815 doi "https://doi.org/10.1002/j.1460-2075.1988.tb02886.x" @default.
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