title: Colicin N and its thermolytic fragment induce phospholipid vesicle fusion.
abstract: Colicin N, a bacteriocin encoded on a plasmid belonging to the pore-forming class of colicins, induces phospholipid vesicle fusion at acidic pH as demonstrated by fluorescence resonance energy transfer. Its C-terminal thermolytic fragment has properties very similar to the native molecule. The fusion is protein concentration-dependent and is regulated by (a) group(s) with a pK of approximately 4.6. The physiological relevance of this characteristic common to all colicins tested so far is discussed.
authors.affiliation: European Molecular Biology Laboratory, Heidelberg, FRG.
authors.forename: D
authors.initials: D
authors.lastname: Massotte
authors.forename: F
authors.initials: F
authors.lastname: Pattus
mesh_terms: D003087:Colicins / Q000494:pharmacology*; D004926:Escherichia coli; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D008561:Membrane Fusion; D008563:Membrane Lipids; D009391:Nephelometry and Turbidimetry; D010446:Peptide Fragments / Q000494:pharmacology; D010743:Phospholipids; D013050:Spectrometry, Fluorescence
chemical_list: D003087:Colicins; D008563:Membrane Lipids; D010446:Peptide Fragments; D010743:Phospholipids