Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR.

ABSTRACT: Bacteria utilize thermotaxis signal transduction proteins, including CheA, and CheY, to switch the direction of the cell movement. However, the thermally responsive machinery enabling warm-seeking behavior has not been identified. Here we examined the effects of temperature on the structure and dynamics of the full-length CheA and CheY complex, by NMR. Our studies revealed that the CheA-CheY complex exists in equilibrium between multiple states, including one state that is preferable for the autophosphorylation of CheA, and another state that is preferable for the phosphotransfer from CheA to CheY. With increasing temperature, the equilibrium shifts toward the latter state. The temperature-dependent population shift of the dynamic domain arrangement of the CheA-CheY complex induced changes

SUBMITTER: Minato Y 

PROVIDER: S-EPMC5705603 | biostudies-literature | 2017 Nov

REPOSITORIES: biostudies-literature