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    cheA chemotaxis protein CheA [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 946401, updated on 17-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Engineered chemotaxis core signaling units indicate a constrained kinase-off state.

    Engineered chemotaxis core signaling units indicate a constrained kinase-off state.
    Muok AR, Chua TK, Srivastava M, Yang W, Maschmann Z, Borbat PP, Chong J, Zhang S, Freed JH, Briegel A, Crane BR., Free PMC Article

    11/13/2021
    ATP Binding as a Key Target for Control of the Chemotaxis Kinase.

    ATP Binding as a Key Target for Control of the Chemotaxis Kinase.
    Jun SY, Pan W, Hazelbauer GL., Free PMC Article

    02/20/2021
    Strategies for identifying dynamic regions in protein complexes: Flexibility changes accompany methylation in chemotaxis receptor signaling states.

    Strategies for identifying dynamic regions in protein complexes: Flexibility changes accompany methylation in chemotaxis receptor signaling states.
    Malik N, Wahlbeck KA, Thompson LK., Free PMC Article

    12/5/2020
    CheW truncated variants are able to drive chemotaxis behavior through activation and control of the CheA kinase. CheA control and networking activities reside in separate domains of CheW protein.

    Truncated, Non-networking Versions of the Coupling Protein CheW Retain Chemoreceptor Control of Kinase CheA.
    Pedetta A, Studdert CA.

    07/4/2020
    It has been concluded that the dipped conformation of the CheA.P4 domain is critical to the kinase-active state in core signaling units.

    Identification of a Kinase-Active CheA Conformation in Escherichia coli Chemoreceptor Signaling Complexes.
    Piñas GE, Parkinson JS., Free PMC Article

    06/13/2020
    Conformational shifts in a chemoreceptor helical hairpin control kinase signaling in Escherichia coli.

    Conformational shifts in a chemoreceptor helical hairpin control kinase signaling in Escherichia coli.
    Gao Q, Cheng A, Parkinson JS., Free PMC Article

    03/28/2020
    A model for signal transmission in chemotaxis signaling complexes in which the CheW-receptor interface plays the key role in conveying signaling-related conformational changes from receptors to the CheA kinase.

    Noncritical Signaling Role of a Kinase-Receptor Interaction Surface in the Escherichia coli Chemosensory Core Complex.
    Piñas GE, DeSantis MD, Parkinson JS., Free PMC Article

    04/27/2019
    the interdomain linker is an active module that has the ability to impose regulatory effects on CheA activity

    Regulatory Role of an Interdomain Linker in the Bacterial Chemotaxis Histidine Kinase CheA.
    Ding X, He Q, Shen F, Dahlquist FW, Wang X., Free PMC Article

    02/23/2019
    Signaling complexes control CheA by altering its apparent rate constant of autophosphorylation.

    Signaling complexes control the chemotaxis kinase by altering its apparent rate constant of autophosphorylation.
    Pan W, Dahlquist FW, Hazelbauer GL., Free PMC Article

    08/26/2017
    Oxidized Aer activates CheA, whereas ASQ Aer reversibly inhibits CheA.

    Bacterial Energy Sensor Aer Modulates the Activity of the Chemotaxis Kinase CheA Based on the Redox State of the Flavin Cofactor.
    Samanta D, Widom J, Borbat PP, Freed JH, Crane BR., Free PMC Article

    05/27/2017
    the Tar(FO) modules demonstrate that trimerized signaling tips self-associate, bind CheA and CheW, and facilitate conversion of CheA to an active conformation.

    Preformed Soluble Chemoreceptor Trimers That Mimic Cellular Assembly States and Activate CheA Autophosphorylation.
    Greenswag AR, Li X, Borbat PP, Samanta D, Watts KJ, Freed JH, Crane BR., Free PMC Article

    08/22/2015
    Co-overexpression of Tsr, CheA, and CheW yields hexagonal Arrays.

    New insights into bacterial chemoreceptor array structure and assembly from electron cryotomography.
    Briegel A, Wong ML, Hodges HL, Oikonomou CM, Piasta KN, Harris MJ, Fowler DJ, Thompson LK, Falke JJ, Kiessling LL, Jensen GJ., Free PMC Article

    06/21/2014
    Differences were observed, however, in a keel-like density that we identify here as CheA kinase domains P1 and P2, the phosphorylation site domain and the binding domain for response regulator target proteins.

    The mobility of two kinase domains in the Escherichia coli chemoreceptor array varies with signalling state.
    Briegel A, Ames P, Gumbart JC, Oikonomou CM, Parkinson JS, Jensen GJ., Free PMC Article

    03/15/2014
    Thus, these P1 phosphorylation domain mutants appear to define interaction determinants for P1-P4 docking during the CheA autophosphorylation reaction.

    Mutational analysis of the P1 phosphorylation domain in Escherichia coli CheA, the signaling kinase for chemotaxis.
    Nishiyama S, Garzón A, Parkinson JS., Free PMC Article

    03/1/2014
    analysis of CheA and CheW protein architecture and their role in bacterial chemotaxis

    Bacterial chemoreceptor arrays are hexagonally packed trimers of receptor dimers networked by rings of kinase and coupling proteins.
    Briegel A, Li X, Bilwes AM, Hughes KT, Jensen GJ, Crane BR., Free PMC Article

    05/5/2012
    The exchange of CheA and CheW at receptor clusters shows a modest dependency on the receptor modification.

    Effects of receptor modification and temperature on dynamics of sensory complexes in Escherichia coli chemotaxis.
    Schulmeister S, Grosse K, Sourjik V., Free PMC Article

    01/14/2012
    F214A substitution in P2 of CheA caused 1,000-fold reduction in CheA-CheY binding affinity.

    Identification of an anchor residue for CheA-CheY interactions in the chemotaxis system of Escherichia coli.
    Thakor H, Nicholas S, Porter IM, Hand N, Stewart RC., Free PMC Article

    10/1/2011
    The 2[to]2[to]1 organization is the core structural and functional unit of chemotaxis signaling complexes and hexagonal arrays characteristic of signaling complexes may be built from this unit.

    Core unit of chemotaxis signaling complexes.
    Li M, Hazelbauer GL., Free PMC Article

    08/27/2011
    crystal of CheA belonged to space group P1, with unit-cell parameters a = 59.271, b = 67.674, c = 82.815 A, alpha = 77.568, beta = 86.073, gamma = 64.436 degrees . The asymmetric unit may contain up to ten dimeric units of P3 four-helix bundles

    Crystallization and preliminary X-ray crystallographic analysis of Escherichia coli CheA P3 dimerization domain.
    Park SY, Ham SW, Kim KY, Crane BR., Free PMC Article

    08/20/2011
    Specific CheA-short (CheA(S)) residues, L123 and L126, were identified as critical for CheZ binding. In the CheA(S) 'P1-CheZ nuclear magnetic resonance structure, these residues form an interaction surface on alpha-helix E in the 'P1 domain.

    The CheZ binding interface of CheAS is located in alpha-helix E.
    O'Connor C, Matsumura P, Campos A., Free PMC Article

    01/21/2010
    Results describe the ranges and kinetics of domain motions in the free CheA dimer.

    Thermal domain motions of CheA kinase in solution: Disulfide trapping reveals the motional constraints leading to trans-autophosphorylation.
    Gloor SL, Falke JJ., Free PMC Article

    01/21/2010
    N-terminus verified by Edman degradation on mature peptide

    Tandem translation starts in the cheA locus of Escherichia coli.
    Kofoid EC, Parkinson JS., Free PMC Article

    11/5/2007
    The fluorescence properties of CheA carrying a Phe455Trp replacement can be used to monitor ATP-binding events and a conformational change at the CheA protein histidine kinase active site.

    Analysis of ATP binding to CheA containing tryptophan substitutions near the active site.
    Stewart RC.

    01/21/2010
    chemotaxis in E. coli requires the presence of chemoreceptor arrays and that the formation of these arrays requires the scaffolding interactions of the signaling molecules CheA and CheW

    Direct visualization of Escherichia coli chemotaxis receptor arrays using cryo-electron microscopy.
    Zhang P, Khursigara CM, Hartnell LM, Subramaniam S., Free PMC Article

    01/21/2010
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