Illicit Transport: The Oligopeptide Permease
- 1 February 1973
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 70 (2) , 456-458
- https://doi.org/10.1073/pnas.70.2.456
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
This publication has 8 references indexed in Scilit:
- Effects of N-Methyl Peptide Bonds on Peptide Utilization by Escherichia coliJournal of General Microbiology, 1972
- Response of Escherichia coli to Ornithyl PeptidesJournal of Biological Chemistry, 1972
- Peptide Transport and Metabolism in BacteriaAnnual Review of Biochemistry, 1971
- The utilization of prolyl peptides by Escherichia coliBiochemical Journal, 1971
- The requirement for the protonated α-amino group for the transport of peptides in Escherichia coliBiochemical Journal, 1971
- Classification and Mapping of Spontaneous and Induced Mutations in The Histidine Operon of SalmonellaAdvances in Genetics, 1971
- Uptake of amino acids by Salmonella typhimuriumArchives of Biochemistry and Biophysics, 1964
- Phosphorus Assay in Column ChromatographyJournal of Biological Chemistry, 1959