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    tsr methyl-accepting chemotaxis protein Tsr [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 948884, updated on 3-Dec-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Structural signatures of Escherichia coli chemoreceptor signaling states revealed by cellular crosslinking.

    Structural signatures of Escherichia coli chemoreceptor signaling states revealed by cellular crosslinking.
    Flack CE, Parkinson JS., Free PMC Article

    07/9/2022
    The authors show that individual Tsr dimers within a trimer exhibit asymmetric flexibilities that are a function of the signaling state, highlighting the effect of their different protein interactions at the receptor tips.

    In Situ Conformational Changes of the Escherichia coli Serine Chemoreceptor in Different Signaling States.
    Yang W, Cassidy CK, Ames P, Diebolder CA, Schulten K, Luthey-Schulten Z, Parkinson JS, Briegel A., Free PMC Article

    04/25/2020
    Blue light is a universal signal for Escherichia coli chemoreceptors.

    Blue Light Is a Universal Signal for Escherichia coli Chemoreceptors.
    Perlova T, Gruebele M, Chemla YR., Free PMC Article

    04/4/2020
    this study shows that Tsr interacts with IL-8 provoking E. coli transmigration across human lung epithelial cells

    Tsr Chemoreceptor Interacts With IL-8 Provoking E. coli Transmigration Across Human Lung Epithelial Cells.
    Han B, Li M, Xu Y, Islam D, Khang J, Del Sorbo L, Lee W, Szaszi K, Zhong N, Slutsky AS, Li Y, Zhang H., Free PMC Article

    05/5/2018
    results indicate that, rather than being essential for proper receptor-receptor interaction, the "glycine hinge" residues are involved in the ability of the receptor to switch between different signaling states. Mainly, the C-helix residue G439 has a key role in shifting the equilibrium toward a kinase-activating conformation.

    Mutational Replacements at the "Glycine Hinge" of the Escherichia coli Chemoreceptor Tsr Support a Signaling Role for the C-Helix Residue.
    Pedetta A, Massazza DA, Herrera Seitz MK, Studdert CA.

    07/29/2017
    These results indicate that the E402 and R404 residues of Tsr play their most critical signaling roles at their inner locations near the trimer axis where they likely participate in stabilizing the trimer-of-dimer packing and the kinase-ON state of core signaling complexes.

    Signaling Consequences of Structural Lesions that Alter the Stability of Chemoreceptor Trimers of Dimers.
    Lai RZ, Gosink KK, Parkinson JS., Free PMC Article

    07/8/2017
    The authors suggest that the Tsr control cable transmits input signals to a four-helix HAMP bundle by modulating the intensity of structural clashes between out-of-register transmembrane helix and AS1 helix of HAMP.

    Evidence for a Helix-Clutch Mechanism of Transmembrane Signaling in a Bacterial Chemoreceptor.
    Ames P, Hunter S, Parkinson JS., Free PMC Article

    06/24/2017
    Only strains that produce TynA and FeaB converting norepinephrine to 3,4-dihydroxymandelic acid xhibited chemotaxis toward norepinephrine and 3,4-dihydroxymandelic acid is sensed by the serine chemoreceptor Tsr.

    Chemotaxis of Escherichia coli to norepinephrine (NE) requires conversion of NE to 3,4-dihydroxymandelic acid.
    Pasupuleti S, Sule N, Cohn WB, MacKenzie DS, Jayaraman A, Manson MD., Free PMC Article

    02/21/2015
    Phe396 governs conformational changes of tsr.

    A phenylalanine rotameric switch for signal-state control in bacterial chemoreceptors.
    Ortega DR, Yang C, Ames P, Baudry J, Parkinson JS, Zhulin IB., Free PMC Article

    10/11/2014
    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
    Such inversion is enabled by opposing pH sensing by the two major chemoreceptors, Tar and Tsr, such that the relative strength of the response is modulated by adaptive receptor methylation.

    Opposite responses by different chemoreceptors set a tunable preference point in Escherichia coli pH taxis.
    Yang Y, Sourjik V.

    06/1/2013
    Alterations in the symmetry of the two branches of the cytoplasmic hairpin of tsr seriously compromise chemoreceptor function.

    Functional and structural effects of seven-residue deletions on the coiled-coil cytoplasmic domain of a chemoreceptor.
    Massazza DA, Izzo SA, Gasperotti AF, Herrera Seitz MK, Studdert CA.

    04/14/2012
    Ligand specificity is determined by differentially arranged common ligand-binding residues in bacterial amino acid chemoreceptors Tsr and Tar

    Ligand specificity determined by differentially arranged common ligand-binding residues in bacterial amino acid chemoreceptors Tsr and Tar.
    Tajima H, Imada K, Sakuma M, Hattori F, Nara T, Kamo N, Homma M, Kawagishi I., Free PMC Article

    02/25/2012
    Mutant Tsr molecules with a charged amino acid or proline replacement exhibited the most severe trimer formation defects.

    Mutational analysis of N381, a key trimer contact residue in Tsr, the Escherichia coli serine chemoreceptor.
    Gosink KK, Zhao Y, Parkinson JS., Free PMC Article

    01/7/2012
    Tar molecules with the cytoplasmic methylation and kinase control domains of Tsr still sensed phenol as an attractant.

    Phenol sensing by Escherichia coli chemoreceptors: a nonclassical mechanism.
    Pham HT, Parkinson JS., Free PMC Article

    01/7/2012
    The results suggest a helix extension mechanism of Tsr transmembrane signaling in which TM2 piston motions influence HAMP stability by modulating the helicity of the control cable segment.

    Mutational analysis of the control cable that mediates transmembrane signaling in the Escherichia coli serine chemoreceptor.
    Kitanovic S, Ames P, Parkinson JS., Free PMC Article

    11/19/2011
    The findings of this study provide strong support for a three-state dynamic bundle model of HAMP domain signalling in Tsr, and possibly in other bacterial transducers as well.

    Biphasic control logic of HAMP domain signalling in the Escherichia coli serine chemoreceptor.
    Zhou Q, Ames P, Parkinson JS., Free PMC Article

    08/13/2011
    The cytoplasmic domains of Tar and Tsr receptors are close to each other near the trimer contact region at the cytoplasmic tip.

    Cross-linking evidence for motional constraints within chemoreceptor trimers of dimers.
    Massazza DA, Parkinson JS, Studdert CA., Free PMC Article

    04/16/2011
    Both LsrB and Tsr are necessary for sensing AI-2, but AI-2 uptake is not, suggesting that LsrB and Tsr interact directly in the periplasm.

    Chemotaxis to the quorum-sensing signal AI-2 requires the Tsr chemoreceptor and the periplasmic LsrB AI-2-binding protein.
    Hegde M, Englert DL, Schrock S, Cohn WB, Vogt C, Wood TK, Manson MD, Jayaraman A., Free PMC Article

    02/26/2011
    The authors propose that Tsr HAMP controls output signals by modulating destabilizing phase clashes between the AS2 helices and the adjoining kinase control helices.

    Mutational analyses of HAMP helices suggest a dynamic bundle model of input-output signalling in chemoreceptors.
    Zhou Q, Ames P, Parkinson JS., Free PMC Article

    01/21/2010
    chemoreceptors are organized as trimers of receptor dimers and display two distinct conformations that differ principally in arrangement of the HAMP domains within each trimer

    Role of HAMP domains in chemotaxis signaling by bacterial chemoreceptors.
    Khursigara CM, Wu X, Zhang P, Lefman J, Subramaniam S., Free PMC Article

    01/21/2010
    Amino acid replacements of two conserved residues at the tip of the trimer contact region of Tsr caused differing interactions with CheA and CheW.

    Different signaling roles of two conserved residues in the cytoplasmic hairpin tip of Tsr, the Escherichia coli serine chemoreceptor.
    Mowery P, Ostler JB, Parkinson JS., Free PMC Article

    01/21/2010
    The current study, utilizing a Tsr-GFP fusion protein and time-lapse fluorescence microscopy of individual cell lineages, demonstrates that Tsr accumulates approximately linearly with time at the cell poles

    Tsr-GFP accumulates linearly with time at cell poles, and can be used to differentiate 'old' versus 'new' poles, in Escherichia coli.
    Ping L, Weiner B, Kleckner N., Free PMC Article

    01/21/2010
    Most I241 lesions locked Tsr signal output in the kinase-on mode, implying that this residue is responsible mainly for stabilizing the kinase-off signaling state.

    Mutational analysis of the connector segment in the HAMP domain of Tsr, the Escherichia coli serine chemoreceptor.
    Ames P, Zhou Q, Parkinson JS., Free PMC Article

    01/21/2010
    Expansion of polyQ to 13Q in Tsr has no significant effect on chemotaxis.

    Variable length tandem repeat polyglutamine sequences in the flexible tether region of the Tsr chemotaxis receptor of Escherichia coli.
    Dzinic SH, Shukla M, Mandija I, Ram TS, Ram JL.

    01/21/2010
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