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Investigation of transphosphorylation between chemotaxis proteins and the phosphoenolpyruvate:sugar phosphotransferase system. 1995

M S Johnson, and E H Rowsell, and B L Taylor
Department of Microbiology and Molecular Genetics, Loma Linda University, CA 92350, USA.

Transphosphorylation between the chemotaxis proteins and phosphoenolpyruvate:sugar phosphotransferase system (PTS) from Escherichia coli was investigated by incubating the CheA, CheW and CheY proteins of the chemotaxis cascade, and Enzyme I, HPr and Enzyme IImtl of the PTS with [gamma-32P]ATP or [32P]phosphoenolpyruvate in the presence and absence of cell extract. In the absence of cell extract, ATP phosphorylated CheA, but in the presence of cell extract, Enzyme I was also phosphorylated. Phosphoenolpyruvate phosphorylated only PTS components. The transphosphorylation of Enzyme I by ATP did not require chemotaxis proteins, and likely occurred through acetate kinase. Regardless of phosphorylation state, the HPr protein did not inhibit the rate of ATP-dependent phosphorylation of the CheA or the CheY protein. It is concluded that chemotaxis to PTS substrates is not mediated by transphosphorylation between the PTS and chemotaxis systems.

UI MeSH Term Description Entries
D008565 Membrane Proteins Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors. Cell Membrane Protein,Cell Membrane Proteins,Cell Surface Protein,Cell Surface Proteins,Integral Membrane Proteins,Membrane-Associated Protein,Surface Protein,Surface Proteins,Integral Membrane Protein,Membrane Protein,Membrane-Associated Proteins,Membrane Associated Protein,Membrane Associated Proteins,Membrane Protein, Cell,Membrane Protein, Integral,Membrane Proteins, Integral,Protein, Cell Membrane,Protein, Cell Surface,Protein, Integral Membrane,Protein, Membrane,Protein, Membrane-Associated,Protein, Surface,Proteins, Cell Membrane,Proteins, Cell Surface,Proteins, Integral Membrane,Proteins, Membrane,Proteins, Membrane-Associated,Proteins, Surface,Surface Protein, Cell
D010731 Phosphoenolpyruvate Sugar Phosphotransferase System The bacterial sugar phosphotransferase system (PTS) that catalyzes the transfer of the phosphoryl group from phosphoenolpyruvate to its sugar substrates (the PTS sugars) concomitant with the translocation of these sugars across the bacterial membrane. The phosphorylation of a given sugar requires four proteins, two general proteins, Enzyme I and HPr and a pair of sugar-specific proteins designated as the Enzyme II complex. The PTS has also been implicated in the induction of synthesis of some catabolic enzyme systems required for the utilization of sugars that are not substrates of the PTS as well as the regulation of the activity of ADENYLYL CYCLASES. EC 2.7.1.-. Phosphoenolpyruvate Hexose Phosphotransferases,Phosphoenolpyruvate-Glycose Phosphotransferase System,Hexose Phosphotransferases, Phosphoenolpyruvate,Phosphoenolpyruvate Glycose Phosphotransferase System,Phosphotransferase System, Phosphoenolpyruvate-Glycose,Phosphotransferases, Phosphoenolpyruvate Hexose,System, Phosphoenolpyruvate-Glycose Phosphotransferase
D010766 Phosphorylation The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety. Phosphorylations
D002633 Chemotaxis The movement of cells or organisms toward or away from a substance in response to its concentration gradient. Haptotaxis
D004926 Escherichia coli A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc. Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D000071677 Histidine Kinase A member of the transferase superfamily of proteins. In the activated state, protein-histidine kinase autophosphorylates at a histidine residue, subsequently transferring high-energy phosphoryl groups to an aspartate residue of the response-regulator domain, which results in a conformational shift in the effector domain. Histidine kinases mediate signal transduction in a wide range of processes involving cellular adaptation to environmental stress. Histidine Protein Kinase,Histone H4 Histidine Kinase,Protein Histidine Pros-Kinase,Protein Kinase (Histidine), Pros-Kinase,Protein-Histidine Kinase,Protein-Histidine Pros-Kinase,Protein-Histidine Tele-Kinase,Sensor Histidine Kinase,Histidine Kinase, Sensor,Histidine Pros-Kinase, Protein,Kinase, Histidine,Kinase, Histidine Protein,Kinase, Protein-Histidine,Kinase, Sensor Histidine,Pros-Kinase, Protein Histidine,Pros-Kinase, Protein-Histidine,Protein Histidine Kinase,Protein Histidine Pros Kinase,Protein Histidine Tele Kinase,Protein Kinase, Histidine,Tele-Kinase, Protein-Histidine
D000072236 Methyl-Accepting Chemotaxis Proteins Transmembrane sensor receptor proteins that are central components of the chemotactic systems of a number of motile bacterial species which include ESCHERICHIA COLI and SALMONELLA TYPHIMURIUM. Methyl-accepting chemotaxis proteins derive their name from a sensory adaptation process which involves methylation at several glutamyl residues in their cytoplasmic domain. Methyl-accepting chemotaxis proteins trigger chemotactic responses across spatial chemical gradients, causing organisms to move either toward favorable stimuli or away from toxic ones. Methyl-Accepting Chemotaxis Protein,MACP-I,MACP-II,Methyl Accepting Chemotaxis Protein 1,Methyl Accepting Chemotaxis Protein 2,Methyl Accepting Chemotaxis Protein 3,Methyl-Accepting Chemotaxis Protein I,Methyl-Accepting Chemotaxis Protein II,Methyl-Accepting Chemotaxis Protein III,Chemotaxis Protein, Methyl-Accepting,Chemotaxis Proteins, Methyl-Accepting,Methyl Accepting Chemotaxis Protein,Methyl Accepting Chemotaxis Protein I,Methyl Accepting Chemotaxis Protein II,Methyl Accepting Chemotaxis Protein III,Methyl Accepting Chemotaxis Proteins,Protein, Methyl-Accepting Chemotaxis,Proteins, Methyl-Accepting Chemotaxis
D001426 Bacterial Proteins Proteins found in any species of bacterium. Bacterial Gene Products,Bacterial Gene Proteins,Gene Products, Bacterial,Bacterial Gene Product,Bacterial Gene Protein,Bacterial Protein,Gene Product, Bacterial,Gene Protein, Bacterial,Gene Proteins, Bacterial,Protein, Bacterial,Proteins, Bacterial
D012486 Salmonella typhimurium A serotype of Salmonella enterica that is a frequent agent of Salmonella gastroenteritis in humans. It also causes PARATYPHOID FEVER. Salmonella typhimurium LT2
D029968 Escherichia coli Proteins Proteins obtained from ESCHERICHIA COLI. E coli Proteins

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