Lookup NU author(s): Christopher Birchall,
Dr Phillip Aldridge
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
The assembly of the bacterial flagellum is exquisitely controlled. Flagellar biosynthesis is underpinned by a specialized type III secretion system that allows export of proteins from the cytoplasm to the nascent structure. Bacillus subtilis regulates flagellar assembly using both conserved and species-specific mechanisms. Here, we show that YvyG is essential for flagellar filament assembly. We define YvyG as an orthologue of the Salmonella enterica serovar Typhimurium type III secretion system chaperone, FlgN, which is required for the export of the hook-filament junction proteins, FlgK and FlgL. Deletion of flgN (yvyG) results in a nonmotile phenotype that is attributable to a decrease in hag translation and a complete lack of filament polymerization. Analyses indicate that a flgK-flgL double mutant strain phenocopies deletion of flgN and that overexpression of flgK-flgL cannot complement the motility defect of a Delta flgN strain. Furthermore, in contrast to previous work suggesting that phosphorylation of FlgN alters its subcellular localization, we show that mutation of the identified tyrosine and arginine FlgN phosphorylation sites has no effect on motility. These data emphasize that flagellar biosynthesis is differentially regulated in B. subtilis from classically studied Gram-negative flagellar systems and questions the biological relevance of some posttranslational modifications identified by global proteomic approaches.
Author(s): Cairns LS, Marlow VL, Kiley TB, Birchall C, Ostrowski A, Aldridge PD, Stanley-Wall NR
Publication type: Article
Publication status: Published
Journal: Journal of Bacteriology
Print publication date: 01/06/2014
Online publication date: 04/04/2014
Acceptance date: 01/04/2014
Date deposited: 16/10/2014
ISSN (print): 0021-9193
ISSN (electronic): 1098-5530
Publisher: American Society for Microbiology
Altmetrics provided by Altmetric