Bacteriocin release protein triggers dimerization of outer membrane phospholipase A in vivo.
Bacteriocin release protein is known to activate outer membrane phospholipase A (OMPLA), which results in the release of colicin from Escherichia coli. In vivo chemical cross-linking experiments revealed that the activation coincides with dimerization of OMPLA. Permeabilization of the cell envelope and dimerization were characterized by a lag time of 2 h.
D000469:Alkaline Phosphatase / Q000378:metabolism; D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000096:biosynthesis / Q000502:physiology*; D002463:Cell Membrane Permeability; D015500:Chloramphenicol O-Acetyltransferase / Q000378:metabolism; D003432:Cross-Linking Reagents; D003600:Cytosol / Q000201:enzymology / Q000378:metabolism; D019281:Dimerization; D004789:Enzyme Activation; D004926:Escherichia coli / Q000166:cytology / Q000201:enzymology / Q000378:metabolism*; D008074:Lipoproteins; D008954:Models, Biological; D019897:Periplasm / Q000201:enzymology / Q000378:metabolism; D010741:Phospholipases A / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D013997:Time Factors