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Signalling‐dependent interactions between the kinase‐coupling protein CheW and chemoreceptors in living cells
Author(s) -
Pedetta Andrea,
Parkinson John S.,
Studdert Claudia A.
Publication year - 2014
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12727
Subject(s) - biology , periplasmic space , chemoreceptor , histidine kinase , microbiology and biotechnology , transmembrane protein , cytoplasm , chemotaxis , phosphorylation , protein kinase a , receptor , signal transduction , ligand (biochemistry) , effector , biophysics , biochemistry , histidine , amino acid , escherichia coli , gene
Summary Chemical signals sensed on the periplasmic side of bacterial cells by transmembrane chemoreceptors are transmitted to the flagellar motors via the histidine kinase CheA , which controls the phosphorylation level of the effector protein CheY . Chemoreceptor arrays comprise remarkably stable supramolecular structures in which thousands of chemoreceptors are networked through interactions between their cytoplasmic tips, CheA , and the small coupling protein CheW . To explore the conformational changes that occur within this protein assembly during signalling, we used in vivo cross‐linking methods to detect close interactions between the coupling protein CheW and the serine receptor Tsr in intact E scherichia coli cells. We identified two signal‐sensitive contacts between CheW and the cytoplasmic tip of Tsr . Our results suggest that ligand binding triggers changes in the receptor that alter its signalling contacts with CheW (and/or CheA ).