Previous Article | Next Article ![]()
Applied and Environmental Microbiology, September 1998, p. 3147-3152, Vol. 64, No. 9
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.
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Cloning and Expression of the Listeria
monocytogenes Scott A ptsH and ptsI Genes,
Coding for HPr and Enzyme I, Respectively, of the
Phosphotransferase System

*
Corresponding author. Mailing address: Department
of Food Science and Technology, University of Nebraska-Lincoln,
Lincoln, NE 68583-0919. Phone: (402) 472-2820. Fax: (402)
472-1693. E-mail: bhutkins{at}foodsci.unl.edu.
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:
Copyright © 2009 by the American Society for Microbiology. For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»