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.