ArticleJournal of bacteriology2007
Mutational analysis of the flagellar protein FliG: sites of interaction with FliM and implications for organization of the switch complex.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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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.
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Who cites it
55 citing papers in PubMed.
- Role of FlhF and its domains in the assembly of a polar flagellum inJournal of bacteriology · 2025Article
- Regulatory Role of a Hydrophobic Core in the FliG C-Terminal Domain in the Rotary Direction of a Flagellar Motor.Biomolecules · 2025Article
- Changes in the hydrophobic network of the FliGiScience · 2023Article
- Structure and Assembly of theInternational journal of molecular sciences · 2023Article
- Article
- The Bacterial Flagellar Motor: Insights Into Torque Generation, Rotational Switching, and Mechanosensing.Frontiers in microbiology · 2022Review
- Structural basis of bacterial flagellar motor rotation and switching.Trends in microbiology · 2021Review
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- The flagellar motor ofeLife · 2020Article
- The Architectural Dynamics of the Bacterial Flagellar Motor Switch.Biomolecules · 2020Review
- New Twists and Turns in Bacterial Locomotion and Signal Transduction.Journal of bacteriology · 2019Review
- Organization of the Flagellar Switch Complex of Bacillus subtilis.Journal of bacteriology · 2019Article
- Directional Switching Mechanism of the Bacterial Flagellar Motor.Computational and structural biotechnology journal · 2019Review
- Rotational direction of flagellar motor from the conformation of FliG middle domain in marine Vibrio.Scientific reports · 2018Article
- Bacterial flagellar switching: a molecular mechanism directed by the logic of an electric motor.Journal of molecular modeling · 2018Article
- Three SpoA-domain proteins interact in the creation of the flagellar type III secretion system inThe Journal of biological chemistry · 2018Article
- Characterization of C-ring component assembly in flagellar motors from amino acid coevolution.Royal Society open science · 2018Article
- Crystal structure of the FliF-FliG complex fromThe Journal of biological chemistry · 2018Article
- Architecture of the Flagellar Switch Complex of Escherichia coli: Conformational Plasticity of FliG and Implications for Adaptive Remodeling.Journal of molecular biology · 2017Article
- Domain-swap polymerization drives the self-assembly of the bacterial flagellar motor.Nature structural & molecular biology · 2016Article
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4 authors.
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Abstract
The switch complex at the base of the bacterial flagellum is essential for flagellar assembly, rotation, and switching. In Escherichia coli and Salmonella, the complex contains about 26 copies of FliG, 34 copies of FliM, and more then 100 copies of FliN, together forming the basal body C ring. FliG is involved most directly in motor rotation and is located in the upper (membrane-proximal) part of the C ring. A crystal structure of the middle and C-terminal parts of FliG shows two globular domains connected by an alpha-helix and a short extended segment. The middle domain of FliG has a conserved surface patch formed by the residues EHPQ(125-128) and R(160) (the EHPQR motif), and the C-terminal domain has a conserved surface hydrophobic patch. To examine the functional importance of these and other surface features of FliG, we made mutations in residues distributed over the protein surface and measured the effects on flagellar assembly and function. Mutations preventing flagellar assembly occurred mainly in the vicinity of the EHPQR motif and the hydrophobic patch. Mutations causing aberrant clockwise or counterclockwise motor bias occurred in these same regions and in the waist between the upper and lower parts of the C-terminal domain. Pull-down assays with glutathione S-transferase-FliM showed that FliG interacts with FliM through both the EHPQR motif and the hydrophobic patch. We propose a model for the organization of FliG and FliM subunits that accounts for the FliG-FliM interactions identified here and for the different copy numbers of FliG and FliM in the flagellum.
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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.