Time-reversal symmetry breaking in the chemosensory array reveals a general mechanism for dissipation-enhanced cooperative sensing.

ABSTRACT: The Escherichia coli chemoreceptors form an extensive array that achieves cooperative and adaptive sensing of extracellular signals. The receptors control the activity of histidine kinase CheA, which drives a nonequilibrium phosphorylation-dephosphorylation reaction cycle for response regulator CheY. Cooperativity and dissipation are both important aspects of chemotaxis signaling, yet their consequences have only been studied separately. Recent single-cell FRET measurements revealed that kinase activity of the array spontaneously switches between active and inactive states, with asymmetric switching times that signify time-reversal symmetry breaking in the underlying dynamics. Here, we present a nonequilibrium lattice model of the chemosensory array, which demonstrates that the observed as

SUBMITTER: Hathcock D 

PROVIDER: S-EPMC11480488 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature