Three SpoA-domain proteins interact in the creation of the flagellar type III secretion system in Helicobacter pylori.

ABSTRACT: Bacterial flagella are rotary nanomachines that contribute to bacterial fitness in many settings, including host colonization. The flagellar motor relies on the multiprotein flagellar motor-switch complex to govern flagellum formation and rotational direction. Different bacteria exhibit great diversity in their flagellar motors. One such variation is exemplified by the motor-switch apparatus of the gastric pathogen Helicobacter pylori, which carries an extra switch protein, FliY, along with the more typical FliG, FliM, and FliN proteins. All switch proteins are needed for normal flagellation and motility in H. pylori, but the molecular mechanism of their assembly is unknown. To fill this gap, we examined the interactions among these proteins. We found that the C-terminal SpoA

SUBMITTER: Lam KH 

PROVIDER: S-EPMC6130963 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature