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1.
J Bacteriol ; 196(12): 2216-26, 2014 Jun.
Article in English | MEDLINE | ID: mdl-24706744

ABSTRACT

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 ΔflgN 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.


Subject(s)
Bacillus subtilis/metabolism , Bacterial Proteins/metabolism , Flagella/physiology , Amino Acid Sequence , Bacillus subtilis/cytology , Bacillus subtilis/genetics , Bacterial Proteins/genetics , Gene Expression Regulation, Bacterial/physiology , Molecular Sequence Data , Movement , Mutation
2.
Front Microbiol ; 14: 1093922, 2023.
Article in English | MEDLINE | ID: mdl-37032848

ABSTRACT

Uropathogenic Escherichia coli is a major cause of urinary tract infections. Analysis of the innate immune response in immortalized urothelial cells suggests that the bacterial flagellar subunit, flagellin, is key in inducing host defenses. A panel of 48 clinical uro-associated E. coli isolates recovered from either cystitis, pyelonephritis asymptomatic bacteriuria (ABU) or UTI-associated bacteraemia infections were characterized for motility and their ability to induce an innate response in urothelial cells stably transfected with a NF-κB luciferase reporter. Thirty-two isolates (67%) were identified as motile with strains recovered from cystitis patients exhibiting an uneven motility distribution pattern; seven of the cystitis isolates were associated with a > 5-fold increase in NF-κB signaling. To explore whether the NF-κB signaling response reflected antigenic variation, flagellin was purified from 14 different isolates. Purified flagellin filaments generated comparable NF-κB signaling responses, irrespective of either the source of the isolate or H-serotype. These data argued against any variability between isolates being related to flagellin itself. Investigations also argued that neither TLR4 dependent recognition of bacterial lipopolysaccharide nor growth fitness of the isolates played key roles in leading to the variable host response. To determine the roles, if any, of flagellar abundance in inducing these variable responses, flagellar hook numbers of a range of cystitis and ABU isolates were quantified. Images suggested that up to 60% of the isolate population exhibited flagella with the numbers averaging between 1 and 2 flagella per bacterial cell. These data suggest that selective pressures exist in the urinary tract that allow uro-associated E. coli strains to maintain motility, but exploit population heterogeneity, which together function to prevent host TLR5 recognition and bacterial killing.

3.
J Bacteriol ; 193(11): 2695-707, 2011 Jun.
Article in English | MEDLINE | ID: mdl-21441504

ABSTRACT

Bacterial flagella play key roles in surface attachment and host-bacterial interactions as well as driving motility. Here, we have investigated the ability of Caulobacter crescentus to assemble its flagellar filament from six flagellins: FljJ, FljK, FljL, FljM, FljN, and FljO. Flagellin gene deletion combinations exhibited a range of phenotypes from no motility or impaired motility to full motility. Characterization of the mutant collection showed the following: (i) that there is no strict requirement for any one of the six flagellins to assemble a filament; (ii) that there is a correlation between slower swimming speeds and shorter filament lengths in ΔfljK ΔfljM mutants; (iii) that the flagellins FljM to FljO are less stable than FljJ to FljL; and (iv) that the flagellins FljK, FljL, FljM, FljN, and FljO alone are able to assemble a filament.


Subject(s)
Caulobacter crescentus/physiology , Flagella/metabolism , Flagellin/genetics , Flagellin/metabolism , Macromolecular Substances/metabolism , Caulobacter crescentus/genetics , Flagella/ultrastructure , Gene Deletion , Genes, Bacterial , Locomotion , Macromolecular Substances/ultrastructure , Microscopy, Electron
4.
Phys Rev Lett ; 105(2): 026801, 2010 Jul 09.
Article in English | MEDLINE | ID: mdl-20867723

ABSTRACT

We consider the transport of electrons passing through a mesoscopic device possessing internal dynamical quantum degrees of freedom. The mutual interaction between the system and the conduction electrons contributes to the current fluctuations, which we describe in terms of full counting statistics. We identify conditions where this discriminates coherent from incoherent internal dynamics and also identify and illustrate conditions under which the device acts to dynamically bunch transmitted or reflected electrons, thereby generating super-Poissonian noise.

5.
Genes Dev ; 20(16): 2315-26, 2006 Aug 15.
Article in English | MEDLINE | ID: mdl-16912280

ABSTRACT

The sigma(28) protein is a member of the bacterial sigma(70)-family of transcription factors that directs RNA polymerase to flagellar late (class 3) promoters. The sigma(28) protein is regulated in response to flagellar assembly by the anti-sigma(28) factor FlgM. FlgM inhibits sigma(28)-dependent transcription of genes whose products are needed late in assembly until the flagellar basal motor structure, the hook-basal body (HBB), is constructed. A second function for the sigma(28) transcription factor has been discovered: sigma(28) facilitates the secretion of FlgM through the HBB, acting as the FlgM Type III secretion chaperone. Transcription-specific mutants in sigma(28) were isolated that remained competent for FlgM-facilitated secretion separating the transcription and secretion-facilitation activities of sigma (28). Conversely, we also describe the isolation of mutants in sigma(28) that are specific for FlgM-facilitated secretion. The data demonstrate that sigma(28) is the Type III secretion chaperone for its own anti-sigma factor FlgM. Thus, a novel role for a sigma(70)-family transcription factor is described.


Subject(s)
Bacterial Proteins/metabolism , Flagella/metabolism , Molecular Chaperones/metabolism , Salmonella typhimurium/genetics , Salmonella typhimurium/metabolism , Sigma Factor/metabolism , Bacterial Proteins/genetics , DNA-Directed RNA Polymerases/metabolism , Flagella/genetics , Mutagenesis , Mutation , Polymerase Chain Reaction , Salmonella typhimurium/cytology , Sigma Factor/genetics , beta-Galactosidase/metabolism
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