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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1973 Feb;70(2):456–458. doi: 10.1073/pnas.70.2.456

Illicit Transport: The Oligopeptide Permease

Bruce N Ames *, Giovanna Ferro-Luzzi Ames *, Janis Dillaha Young †, Dorinne Tsuchiya †, Jean Lecocq †
PMCID: PMC433281  PMID: 4568730

Abstract

The oligopeptide permease of Escherichia coli has been characterized by Payne, Gilvarg, and their colleagues. We have confirmed its existence in Salmonella typhimurium, and have isolated a series of mutants lacking the permease. We use this transport system for smuggling a histidine biosynthetic intermediate, histidinol phosphate ester, into the bacteria as its glycylglycyl derivative, Gly-Gly-histidinol phosphate. Free histidinol phosphate ester is not transported into Salmonella. Several amino-acid analogues are shown to be much more inhibitory to Salmonella when presented to the bacteria in the form of tripeptides than as the free amino acids. The implications of this work for practical purposes are discussed. The synthesis of Gly-Gly-histidinol phosphate is described.

Keywords: histidinol phosphate transport, amino-acid analogue transport, Salmonella

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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