Indole is produced by a large number of Gram-positive and Gram-negative bacterial species, including Escherichia coli ( 17). These observations not only enhance our understanding of indole signaling in bacteria but also provide a simple explanation for the ability of indole to signal between biological kingdoms. coli lipid membrane without the aid of any proteinaceous transporter. Furthermore, direct observation of individual liposomes shows that indole can rapidly cross an E. coli membrane under normal physiological conditions is independent of AcrEF-TolC and Mtr. We conclude that the movement of indole across the E. We have combined in vivo and in vitro approaches to examine the relative importance of protein-mediated transport and direct passage across the E. However, the evidence for their involvement is indirect, and it has been known for a long time that indole can pass directly through a lipid bilayer. A view often repeated in the literature is that in Escherichia coli the AcrEF-TolC and Mtr transporter proteins are involved in the export and import, respectively, of indole.
Indole synthesized within the producer bacterium is exported into the surroundings where its accumulation is detected by sensitive cells. In many respects indole behaves like the signaling component of a quorum-sensing system. Its role is not restricted to bacteria, and recently it has been shown to include mutually beneficial signaling between enteric bacteria and their mammalian hosts. It regulates the transition from exponential to stationary phase, it is involved in the control of plasmid stability, and it influences biofilm formation, virulence, and stress responses (including antibiotic resistance). Indole has many, diverse roles in bacterial signaling.
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