Abstract

The phosphoenolpyruvate: glycose phosphotransferase system, or PTS, comprises a complex array of interacting cytoplasmic and membrane proteins with diverse functions in the bacterial cell. The system mediates concomitant phosphorylation and translocation of PTS sugar substrates across the cytoplasmic membrane, is involved in chemotaxis toward PTS sugars, regulates adenylate cyclase, and regulates permeases that take up certain non-PTS sugars and other solutes (as in diauxic growth). The PTS is widely distributed among obligate and facultative anaerobes, and we have recently shown that it is ubiquitously distributed among common marine bacteria. Thus, the PTS has broad ecological and medical implications, and is also an excellent model of how cytoplasmic proteins regulate the functions of membrane proteins by cycles of phosphorylation/dephosphorylation. We shall continue to study the following problems: (a) Precisely what is the mechanism by which the PTS translocates its substrates across the membrane? (b) The transport function of the PTS is under stringent metabolic control. What mechanisms are involved in this metabolic regulation? (c) What are the mechanisms that control genetic regulation of the pts operons? (d) A functional gene called pel is required for lambda DNA penetration of the inner bacterial membrane: pel was though to encode the PTS membrane protein II-BMan. Cloning studies show, however, that pel encodes a novel protein, Pel, and that Pel is required for both DNA penetration and for mannose phosphorylation. What is the role of Pel in these functions? (e) How does the PTS regulate the E. coli lactose permease and adenylate cyclase? (f) Is the PTS a primordial solute transport system that was modified during evolution to many different transport systems? A combination of biochemical, physico-chemical, and molecular biology methods will be used in attempts to answer these questions.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
1R01GM038759-01
Application #
3563682
Study Section
Microbial Physiology and Genetics Subcommittee 2 (MBC)
Project Start
1987-09-01
Project End
1992-08-31
Budget Start
1987-09-01
Budget End
1988-08-31
Support Year
1
Fiscal Year
1987
Total Cost
Indirect Cost

  Institution

Name
Johns Hopkins University
Department
Type
DUNS #
045911138
City
Baltimore
State
MD
Country
United States
Zip Code
21218

  Publications

Xu, Jianhua; Chen, Jiejin; Toptygin, Dmitri et al. (2009) Femtosecond fluorescence spectra of tryptophan in human gamma-crystallin mutants: site-dependent ultrafast quenching. J Am Chem Soc 131:16751-7
Xu, Jianhua; Toptygin, Dmitri; Graver, Karen J et al. (2006) Ultrafast fluorescence dynamics of tryptophan in the proteins monellin and IIAGlc. J Am Chem Soc 128:1214-21
Patel, Himatkumar V; Vyas, Kavita A; Mattoo, Roshan L et al. (2006) Properties of the C-terminal domain of enzyme I of the Escherichia coli phosphotransferase system. J Biol Chem 281:17579-87
Patel, Himatkumar V; Vyas, Kavita A; Savtchenko, Regina et al. (2006) The monomer/dimer transition of enzyme I of the Escherichia coli phosphotransferase system. J Biol Chem 281:17570-8
Meadow, Norman D; Mattoo, Roshan L; Savtchenko, Regina S et al. (2005) Transient state kinetics of Enzyme I of the phosphoenolpyruvate:glycose phosphotransferase system of Escherichia coli: equilibrium and second-order rate constants for the phosphotransfer reactions with phosphoenolpyruvate and HPr. Biochemistry 44:12790-6
Meibom, Karin L; Li, Xibing B; Nielsen, Alex T et al. (2004) The Vibrio cholerae chitin utilization program. Proc Natl Acad Sci U S A 101:2524-9
Patel, Himatkumar V; Vyas, Kavita A; Li, Xibing et al. (2004) Subcellular distribution of enzyme I of the Escherichia coli phosphoenolpyruvate:glycose phosphotransferase system depends on growth conditions. Proc Natl Acad Sci U S A 101:17486-91
Holtman, C K; Pawlyk, A C; Meadow, N D et al. (2001) Reverse genetics of Escherichia coli glycerol kinase allosteric regulation and glucose control of glycerol utilization in vivo. J Bacteriol 183:3336-44
Holtman, C K; Pawlyk, A C; Meadow, N et al. (2001) IIA(Glc) allosteric control of Escherichia coli glycerol kinase: binding site cooperative transitions and cation-promoted association by Zinc(II). Biochemistry 40:14302-8
Keyhani, N O; Wang, L X; Lee, Y C et al. (2000) The chitin disaccharide, N,N'-diacetylchitobiose, is catabolized by Escherichia coli and is transported/phosphorylated by the phosphoenolpyruvate:glycose phosphotransferase system. J Biol Chem 275:33084-90

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