Hydrogen exchange differences between chemoreceptor signaling complexes localize to functionally important subdomains.

ABSTRACT: The goal of understanding mechanisms of transmembrane signaling, one of many key life processes mediated by membrane proteins, has motivated numerous studies of bacterial chemotaxis receptors. Ligand binding to the receptor causes a piston motion of an α helix in the periplasmic and transmembrane domains, but it is unclear how the signal is then propagated through the cytoplasmic domain to control the activity of the associated kinase CheA. Recent proposals suggest that signaling in the cytoplasmic domain involves opposing changes in dynamics in different subdomains. However, it has been difficult to measure dynamics within the functional system, consisting of extended arrays of receptor complexes with two other proteins, CheA and CheW. We have combined hydrogen exchange mass spectrometry

SUBMITTER: Koshy SS 

PROVIDER: S-EPMC4270382 | biostudies-literature | 2014 Dec

REPOSITORIES: biostudies-literature