Conserved aspartate residues and phosphorylation in signal transduction by the chemotaxis protein CheY. 1990

R B Bourret, and J F Hess, and M I Simon
Division of Biology, California Institute of Technology, Pasadena 91125.

The CheY protein is phosphorylated by CheA and dephosphorylated by CheZ as part of the chemotactic signal transduction pathway in Escherichia coli. Phosphorylation of CheY has been proposed to occur on an aspartate residue. Each of the eight aspartate residues of CheY was replaced by using site-directed mutagenesis. Substitutions at Asp-12, Asp-13, or Asp-57 resulted in loss of chemotaxis. Most of the mutant CheY proteins were still phosphorylated by CheA but exhibited modified biochemical properties, including reduced ability to accept phosphate from CheA, altered phosphate group stability, and/or resistance to CheZ-mediated dephosphorylation. The properties of CheY proteins bearing a substitution at position 57 were most aberrant, consistent with the hypothesis that Asp-57 is the normal site of acyl phosphate formation. Evidence for an alternate site of phosphorylation in the Asp-57 mutants is presented. Phosphorylated CheY is believed to cause tumbling behavior. However, a dominant mutant CheY protein that was not phosphorylated in vitro caused tumbling in vivo in the absence of CheA. This phenotype suggests that the role of phosphorylation in the wild-type CheY protein is to stabilize a transient conformational change that can generate tumbling behavior.

UI MeSH Term Description Entries
D007700 Kinetics The rate dynamics in chemical or physical systems.
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
D008954 Models, Biological Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment. Biological Model,Biological Models,Model, Biological,Models, Biologic,Biologic Model,Biologic Models,Model, Biologic
D009154 Mutation Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations. Mutations
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
D002630 Chemotactic Factors Chemical substances that attract or repel cells. The concept denotes especially those factors released as a result of tissue injury, microbial invasion, or immunologic activity, that attract LEUKOCYTES; MACROPHAGES; or other cells to the site of infection or insult. Chemoattractant,Chemotactic Factor,Chemotaxin,Chemotaxins,Cytotaxinogens,Cytotaxins,Macrophage Chemotactic Factor,Chemoattractants,Chemotactic Factors, Macrophage,Macrophage Chemotactic Factors,Chemotactic Factor, Macrophage,Factor, Chemotactic,Factor, Macrophage Chemotactic
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

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