Biogenesis of the Flagellar Switch Complex in Escherichia coli: Formation of Sub-Complexes Independently of the Basal-Body MS-Ring.

ABSTRACT: Direction switching in the flagellar motor of Escherichia coli is under the control of a complex on the rotor formed from the proteins FliG, FliM, and FliN. FliG lies at the top of the switch complex (i.e., nearest the membrane) and is arranged with its C-terminal domain (FliG_C) resting on the middle domain (FliG_M) of the neighboring subunit. This organization requires the protein to adopt an open conformation that exposes the surfaces engaging in intersubunit FliG_C/FliG_M contacts. In a recent study, Baker and coworkers [13] obtained evidence that FliG in the cytosol is monomeric and takes on a more compact conformation, with FliG_C making intramolecular contact with FliG_M of the same subunit. In the present work, we examine

SUBMITTER: Kim EA 

PROVIDER: S-EPMC5568845 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature