Signaling-Related Mobility Changes in Bacterial Chemotaxis Receptors Revealed by Solid-State NMR.

ABSTRACT: Bacteria employ remarkable membrane-bound nanoarrays to sense their environment and direct their swimming. Arrays consist of chemotaxis receptor trimers of dimers that are bridged at their membrane-distal tips by rings of two cytoplasmic proteins, a kinase CheA and a coupling protein CheW. It is not clear how ligand binding to the periplasmic domain of the receptor deactivates the CheA kinase bound to the cytoplasmic tip ∼300 Å away, but the mechanism is thought to involve changes in dynamics within the cytoplasmic domain. To test these proposals, we applied solid-state NMR mobility-filtered experiments to functional complexes of the receptor cytoplasmic fragment (U-¹³C,¹⁵N-CF), CheA, and CheW. Assembly of these proteins into native-like, homogeneous arrays is mediate

SUBMITTER: Kashefi M 

PROVIDER: S-EPMC5613836 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature