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Colicin N and its thermolytic fragment induce phospholipid vesicle fusion
Author(s) -
Massotte D.,
Pattus F.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81593-5
Subject(s) - colicin , bacteriocin , phospholipid , chemistry , vesicle , escherichia coli , biochemistry , biophysics , biology , membrane , gene , organic chemistry , antimicrobial
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 p K of approximately 4.6. The physiological relevance of this characteristic common to all colicins tested so far is discussed.