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
| Autor: | W. H. F. Goessens, Arnold J. M. Driessen, J. van Duin, Jan Wilschut |
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| Předmět: |
Lysis
Cell Membrane Permeability Peptide RNA Phages medicine.disease_cause General Biochemistry Genetics and Molecular Biology Bacteriophage Viral Proteins Bacterial Proteins medicine Escherichia coli Amino Acid Sequence Molecular Biology Peptide sequence chemistry.chemical_classification Liposome General Immunology and Microbiology biology General Neuroscience biology.organism_classification Amino acid chemistry Lytic cycle Biochemistry Liposomes Protons Research Article |
| Zdroj: | Scopus-Elsevier |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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