A chemoreceptor conformational equilibrium controlled by signaling inputs.

ABSTRACT: In chemotaxis, motile bacteria recognize external molecules and move toward favorable concentrations. Chemoreceptors form complexes that perform transmembrane signaling, control a histidine kinase, and undergo posttranslational adaptational modifications. Chemoreceptors are thought to function by switching between two signaling states: kinase-off, favored by ligand occupancy, and kinase-on, favored by adaptational modification. Many structural and biochemical features of the two states have been identified, but little is known about the equilibrium between them and the response of that equilibrium to signaling inputs. Using single-molecule Förster resonance energy transfer, we monitored helical separations in the Escherichia coli aspartate chemoreceptor Tar for the two pairs of heli

SUBMITTER: Hoffman MC 

PROVIDER: S-EPMC12280922 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature