ArticleJournal of bacteriology2000
Role of FliJ in flagellar protein export in Salmonella.
Article in Journal of bacteriology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed.
- Uncoupling substrate delivery from export gate activation reveals distinct roles of the flagellar ATPase complex.Frontiers in microbiology · 2026Article
- "The structure of the Type III secretion system export gate with CdsO, an ATPase lever arm".PLoS pathogens · 2020Article
- Questing functions and structures of hypothetical proteins from Campylobacter jejuni: a computer-aided approach.Bioscience reports · 2020Article
- Flagellar Basal Body Structural Proteins FlhB, FliM, and FliY Are Required for Flagellar-Associated Protein Expression inFrontiers in microbiology · 2018Article
- Evolution of DDB1-binding WD40 (DWD) in the viridiplantae.PloS one · 2018Article
- Mechanism of type-III protein secretion: Regulation of FlhA conformation by a functionally critical charged-residue cluster.Molecular microbiology · 2017Article
- Article
- Involvement of the flagellar assembly pathway in Vibrio alginolyticus adhesion under environmental stresses.Frontiers in cellular and infection microbiology · 2015Article
- ATPase-independent type-III protein secretion in Salmonella enterica.PLoS genetics · 2014Article
- Flagellar biosynthesis exerts temporal regulation of secretion of specific Campylobacter jejuni colonization and virulence determinants.Molecular microbiology · 2014Article
- Article
- EscO, a functional and structural analog of the flagellar FliJ protein, is a positive regulator of EscN ATPase activity of the enteropathogenic Escherichia coli injectisome.Journal of bacteriology · 2014Article
- Interaction between FliJ and FlhA, components of the bacterial flagellar type III export apparatus.Journal of bacteriology · 2013Article
- Article
- Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.Microbiology and molecular biology reviews : MMBR · 2012Review
- Complete Genome of Ignavibacterium album, a Metabolically Versatile, Flagellated, Facultative Anaerobe from the Phylum Chlorobi.Frontiers in microbiology · 2012Article
- An energy transduction mechanism used in bacterial flagellar type III protein export.Nature communications · 2011Article
- Common architecture of the flagellar type III protein export apparatus and F- and V-type ATPases.Nature structural & molecular biology · 2011Article
- Flagellated but not hyperfimbriated Salmonella enterica serovar Typhimurium attaches to and forms biofilms on cholesterol-coated surfaces.Journal of bacteriology · 2010Article
- The HP0256 gene product is involved in motility and cell envelope architecture of Helicobacter pylori.BMC microbiology · 2010Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
We isolated and characterized spontaneous mutants with defects in the 147-amino-acid Salmonella protein FliJ, which is a cytoplasmic component of the type III flagellar export apparatus. These mutants, including ones with null mutations, have the ability to form swarms on motility agar plates after prolonged incubation at 30 degrees C; i.e., they display a leaky motile phenotype. One mutant, SJW277, which formed significantly bigger swarms than the others, encoded only the N-terminal 73 amino acids of FliJ, one-half of the protein. At 30 degrees C, overproduction of this mutant protein improved, to wild-type levels, both motility and the ability to export both rod/hook-type (FlgD; hook capping protein) and filament-type (FliC; flagellin) substrates. At 42 degrees C, however, export was inhibited, indicating that the mutant FliJ protein was temperature sensitive. Taking advantage of this, we performed temperature upshift experiments, which demonstrated that FliJ is directly required for the export of FliC. Co-overproduction of FliJ and either of two export substrates, FliE or FlgG, hindered their aggregation in the cytoplasm. We conclude that FliJ is a general component of the flagellar export apparatus and has a chaperone-like activity for both rod/hook-type and filament-type substrates.
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