ArticleJournal of bacteriology2015
Interaction of the C-terminal tail of FliF with FliG from the Na+-driven flagellar motor of Vibrio alginolyticus.
Article in Journal of bacteriology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 36 citations in OpenAlex.
- Changes in the hydrophobic network of the FliGiScience · 2023Article
- Ring formation byBiophysics and physicobiology · 2023Article
- The Vibrio Polar Flagellum: Structure and Regulation.Advances in experimental medicine and biology · 2023Article
- Structural insights into the mechanism of archaellar rotational switching.Nature communications · 2022Article
- Role of the N- and C-terminal regions of FliF, the MS ring component inJournal of bacteriology · 2021Article
- Construction and Loss of Bacterial Flagellar Filaments.Biomolecules · 2020Review
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- The flagellar motor ofeLife · 2020Article
- Assembly mechanism of a supramolecular MS-ring complex to initiate bacterial flagellar biogenesis inJournal of bacteriology · 2020Article
- The Architectural Dynamics of the Bacterial Flagellar Motor Switch.Biomolecules · 2020Review
- Rotational direction of flagellar motor from the conformation of FliG middle domain in marine Vibrio.Scientific reports · 2018Article
- Co-Folding of a FliF-FliG Split Domain Forms the Basis of the MS:C Ring Interface within the Bacterial Flagellar Motor.Structure (London, England : 1993) · 2017Article
- An Extended Cyclic Di-GMP Network in the Predatory Bacterium Bdellovibrio bacteriovorus.Journal of bacteriology · 2016Article
- Domain-based biophysical characterization of the structural and thermal stability of FliG, an essential rotor component of the NaBiophysics and physicobiology · 2016Article
- Article
- Flagellar region 3b supports strong expression of integrated DNA and the highest chromosomal integration efficiency of the Escherichia coli flagellar regions.Microbial biotechnology · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rotation of the polar flagellum of Vibrio alginolyticus is driven by a Na(+)-type flagellar motor. FliG, one of the essential rotor proteins located at the upper rim of the C ring, binds to the membrane-embedded MS ring. The MS ring is composed of a single membrane protein, FliF, and serves as a foundation for flagellar assembly. Unexpectedly, about half of the Vibrio FliF protein produced at high levels in Escherichia coli was found in the soluble fraction. Soluble FliF purifies as an oligomer of ∼700 kDa, as judged by analytical size exclusion chromatography. By using fluorescence correlation spectroscopy, an interaction between a soluble FliF multimer and FliG was detected. This binding was weakened by a series of deletions at the C-terminal end of FliF and was nearly eliminated by a 24-residue deletion or a point mutation at a highly conserved tryptophan residue (W575). Mutations in FliF that caused a defect in FliF-FliG binding abolish flagellation and therefore confer a nonmotile phenotype. As data from in vitro binding assays using the soluble FliF multimer correlate with data from in vivo functional analyses, we conclude that the C-terminal region of the soluble form of FliF retains the ability to bind FliG. Our study confirms that the C-terminal tail of FliF provides the binding site for FliG and is thus required for flagellation in Vibrio, as reported for other species. This is the first report of detection of the FliF-FliG interaction in the Na(+)-driven flagellar motor, both in vivo and in vitro.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.