Applied and Environmental Microbiology, September 1998, p. 3147-3152, Vol. 64, No. 9
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

School of Biological Sciences,1 and Department of Food Science and Technology,2 University of Nebraska-Lincoln, Lincoln, Nebraska 68583-0919
Received 2 March 1998/Accepted 14 June 1998
The phosphoenolpyruvate (PEP)-dependent phosphotransferase system (PTS) utilizes high-energy phosphate present in PEP to drive the uptake of several different carbohydrates in bacteria. In order to examine the role of the PTS in the physiology of Listeria monocytogenes, we identified the ptsH and ptsI genes encoding the HPr and enzyme I proteins, respectively, of the PTS. Nucleotide sequence analysis indicated that the predicted proteins are nearly 70% similar to HPr and enzyme I proteins from other organisms. Purified L. monocytogenes HPr overexpressed in Escherichia coli was also capable of complementing an HPr defect in heterologous extracts of Staphylococcus aureus ptsH mutants. Additional studies of the transcriptional organization and control indicated that the ptsH and ptsI genes are organized into a transcription unit that is under the control of a consensus-like promoter and that expression of these genes is mediated by glucose availability and pH or by by-products of glucose metabolism.
Paper no. 12177 in the Journal Series of the Nebraska Agricultural
Experiment Station, Lincoln.
Present address: Department of Food Science, North Carolina State
University, Raleigh, NC 27695-7624.
This article has been cited by other articles:
| J. Bacteriol. | Microbiol. Mol. Biol. Rev. | Eukaryot. Cell | All ASM Journals |
|---|