From: Signaling through Enzyme-Linked Cell-Surface Receptors

Figure 15-69The two-component signaling pathway that enables chemotaxis receptors to control the flagellar motor during bacterial chemotaxis
The histidine kinase CheA is stably bound to the receptor via the adaptor protein CheW. The binding of a repellent increases the activity of the receptor, which stimulates CheA to phosphorylate itself on histidine. CheA quickly transfers its covalently bound, high-energy phosphate directly to CheY to generate CheY-phosphate, which then diffuses away, binds to the flagellar motor, and causes the motor to rotate clockwise, which results in tumbling. The binding of an attractant has the opposite effect: it decreases the activity of the receptor and therefore decreases the phosphorylation of CheA and CheY, which results in counterclockwise flagellar rotation and smooth swimming. CheZ accelerates the autodephosphorylation of CheY-phosphate, thereby inactivating it. Each of the phosphorylated intermediates decays in about 10 seconds, enabling the bacterium to respond very quickly to changes in its environment (see Figure 15-10).
- Figure 15-69, The two-component signaling pathway that enables chemotaxis recept...Figure 15-69, The two-component signaling pathway that enables chemotaxis receptors to control the flagellar motor during bacterial chemotaxis - Molecular Biology of the CellBookself
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