ArticlePloS one2013
Function of FlhB, a membrane protein implicated in the bacterial flagellar type III secretion system.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Sulfur disproportionation occurs globally across anoxic habitats and has multiple mechanisms of independent evolutionary origin.The ISME journal · 2026Review
- The two-component system CpxA/CpxR regulates pathogenesis and stress adaptability in the poplar canker bacterium Lonsdalea populi.Molecular plant pathology · 2024Article
- Molecular characterization and in-depth genome analysis of Enterobacter sp. S-16.Functional & integrative genomics · 2023Article
- Article
- A Proline-Rich Element in the Type III Secretion Protein FlhB Contributes to Flagellar Biogenesis in the Beta- and Gamma-Proteobacteria.Frontiers in microbiology · 2020Article
- Flagellar Basal Body Structural Proteins FlhB, FliM, and FliY Are Required for Flagellar-Associated Protein Expression inFrontiers in microbiology · 2018Article
- Pseudomonas fluorescens Filamentous Hemagglutinin, an Iron-Regulated Protein, Is an Important Virulence Factor that Modulates Bacterial Pathogenicity.Frontiers in microbiology · 2016Article
- One-Step PCR Detection ofFrontiers in microbiology · 2016Article
- Type III Secretion System Translocon Component EseB Forms Filaments on and Mediates Autoaggregation of and Biofilm Formation by Edwardsiella tarda.Applied and environmental microbiology · 2015Article
- Weak Interactions between Salmonella enterica FlhB and Other Flagellar Export Apparatus Proteins Govern Type III Secretion Dynamics.PloS one · 2015Article
- Building a flagellum outside the bacterial cell.Trends in microbiology · 2014Review
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The membrane protein FlhB is a highly conserved component of the flagellar secretion system, and it plays an active role in the regulation of protein export. In this study conserved properties of FlhB that are important for its function were investigated. Replacing the flhB gene (or part of the gene) in Salmonella typhimurium with the flhB gene of the distantly related bacterium Aquifex aeolicus greatly reduces motility. However, motility can be restored to some extent by spontaneous mutations in the part of flhB gene coding for the cytoplasmic domain of Aquifex FlhB. Structural analysis suggests that these mutations destabilize the structure. The secondary structure and stability of the mutated cytoplasmic fragments of FlhB have been studied by circular dichroism spectroscopy. The results suggest that conformational flexibility could be important for FlhB function. An extragenic suppressor mutation in the fliS gene, which decreases the affinity of FliS to FliC, partially restores motility of the FlhB substitution mutants.
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