Abstract
Microcin 140, a novel antibiotic of low molecular weight, rapidly depletes the ATP pool of sensitive E. coli strains. This effect seems to be caused by a stimulation of the ATPase since it is not observed either in a mutant strain that lacks activity of this enzyme or in the presence of the ATPase inhibitor dicyclohexylcarbodiimide. Under these conditions the microcin does not affect the incorporation of labelled glucose into macromolecules. Microcin 140 also produces a strong inhibition of the transport of proline and phenylalanine, which is known to be coupled to the proton gradient across the bacterial membrane. There-fore, the stimulation of the bacterial ATPase can be a consequence of collapsing the proton gradient maintained by this enzyme through a proton pumping activity. These results point to a similar mechanism of action for both microcin 140 and colicin K, despite their great difference in molecular size (C.A. Plate et al., J. Biol. Chem, 249: 6138–6143, 1974).
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