A dynamic-signaling-team model for chemotaxis receptors in Escherichia coli.
The chemotaxis system of Escherichia coli is sensitive to small relative changes in ambient chemoattractant concentrations over a broad range. Interactions among receptors are crucial to this sensitivity, as is precise adaptation, the return of chemoreceptor activity to prestimulus levels in a constant chemoeffector environment through methylation and demethylation of receptors. Signal integration and cooperativity have been attributed to strongly coupled, mixed teams of receptors, but receptors become individually methylated according to their ligand occupancy states. Here, we present a model of dynamic signaling teams that reconciles strong coupling among receptors with receptor-specific methylation. Receptor trimers of dimers couple to form a honeycomb lattice, consistent with cryo-electron microscopy (cryoEM) tomography, within which the boundaries of signaling teams change rapidly. Our model helps explain the inferred increase in signaling team size with receptor modification, and indicates that active trimers couple more strongly than inactive trimers.
Hansen
Clinton H
CH
Biophysics Program, Harvard University, Cambridge, MA 02138, USA.
Sourjik
Victor
V
Wingreen
Ned S
NS
D000465:Algorithms; D002630:Chemotactic Factors / Q000737:chemistry / Q000378:metabolism*; D002633:Chemotaxis / Q000502:physiology*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D008954:Models, Biological; D011487:Protein Conformation; D011956:Receptors, Cell Surface / Q000737:chemistry / Q000378:metabolism*; D015398:Signal Transduction / Q000502:physiology*
D002630:Chemotactic Factors; D029968:Escherichia coli Proteins; D011956:Receptors, Cell Surface