Disappearance of specific proteins from the membranes of colicin-treated cells.
Two colicins that affect energy metabolism in Escherichia coli (colicins K and E1) are shown to cause loss of specific membrane proteins from treated cells. Disappearance of these proteins after treatment with colicin K occurs at low multiplicities and is independent of ATPase (EC 3.6.1.4) and phospholipase A (EC 3.1.1.4) activities. The uncouplers carbonyl cyanide m-chlorophenylhydrazone and dinitrophenol do not alter the pattern of membrane proteins.
D000251:Adenosine Triphosphatases / Q000378:metabolism; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D003087:Colicins / Q000494:pharmacology*; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D008565:Membrane Proteins / Q000378:metabolism*; D010740:Phospholipases / Q000378:metabolism; D013045:Species Specificity
D003087:Colicins; D008565:Membrane Proteins; D010740:Phospholipases; D000251:Adenosine Triphosphatases