SUMMARY: Agrocin 84 inhibits a virulent strain of containing a nopaline Ti plasmid, but not the same strain lacking the Ti plasmid; this specificity was investigated. Sensitivity to agrocin 84 was correlated with its active uptake by a high-affinity transport system with a of 5.88 × 10 M. Unmetabolized agrocin 84 was transported inside the sensitive strain and was associated with the soluble fraction of ruptured bacteria and not with the outer walls or cytoplasmic membrane. Agrocin 84 bound to a protein fraction isolated from the periplasmic space of the sensitive strain; there was no equivalent binding activity in the insensitive strain. It is proposed that sensitivity to agrocin 84 is due to the presence of one or more plasmid-coded binding proteins which are associated with transport of agrocin 84 into sensitive strains.


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