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.