ArticleJournal of molecular biology2015
Assembly states of FliM and FliG within the flagellar switch complex.
Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 40 citations in OpenAlex.
- Regulatory Role of a Hydrophobic Core in the FliG C-Terminal Domain in the Rotary Direction of a Flagellar Motor.Biomolecules · 2025Article
- CryoEM structures reveal how the bacterial flagellum rotates and switches direction.Nature microbiology · 2024Article
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- Article
- A physical mechanism underlying the torque generation of the bacterial flagellar motor.The European physical journal. E, Soft matter · 2022Article
- Modulation of the Enzymatic Activity of the Flagellar Lytic Transglycosylase SltF by Rod Components and the Scaffolding Protein FlgJ inJournal of bacteriology · 2021Article
- Mechanosensitive recruitment of stator units promotes binding of the response regulator CheY-P to the flagellar motor.Nature communications · 2021Article
- Structural Conservation and Adaptation of the Bacterial Flagella Motor.Biomolecules · 2020Review
- Symmetry mismatch in the MS-ring of the bacterial flagellar rotor explains the structural coordination of secretion and rotation.Nature microbiology · 2020Article
- The Architectural Dynamics of the Bacterial Flagellar Motor Switch.Biomolecules · 2020Review
- Structural diversity in the Mycobacteria DUF3349 superfamily.Protein science : a publication of the Protein Society · 2020Article
- Article
- A Mechanism of Modulating the Direction of Flagellar Rotation in Bacteria by Fumarate and Fumarate Reductase.Journal of molecular biology · 2019Article
- Organization of the Flagellar Switch Complex of Bacillus subtilis.Journal of bacteriology · 2019Article
- Characterization of FlgP, an Essential Protein for Flagellar Assembly inJournal of bacteriology · 2019Article
- Bacterial flagellar switching: a molecular mechanism directed by the logic of an electric motor.Journal of molecular modeling · 2018Article
- A coevolution-guided model for the rotor of the bacterial flagellar motor.Scientific reports · 2018Article
- Characterization of C-ring component assembly in flagellar motors from amino acid coevolution.Royal Society open science · 2018Article
- Production, characterization, and assessment of a stable analog of the response regulator CheY-phosphate from Thermotoga maritima.Protein science : a publication of the Protein Society · 2017Article
- Biogenesis of the Flagellar Switch Complex in Escherichia coli: Formation of Sub-Complexes Independently of the Basal-Body MS-Ring.Journal of molecular biology · 2017Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
At the base of the bacterial flagella, a cytoplasmic rotor (the C-ring) generates torque and reverses rotation sense in response to stimuli. The bulk of the C-ring forms from many copies of the proteins FliG, FliM, and FliN, which together constitute the switch complex. To help resolve outstanding issues regarding C-ring architecture, we have investigated interactions between FliM and FliG from Thermotoga maritima with X-ray crystallography and pulsed dipolar ESR spectroscopy (PDS). A new crystal structure of an 11-unit FliG:FliM complex produces a large arc with a curvature consistent with the dimensions of the C-ring. Previously determined structures along with this new structure provided a basis to test switch complex assembly models. PDS combined with mutational studies and targeted cross-linking reveal that FliM and FliG interact through their middle domains to form both parallel and antiparallel arrangements in solution. Residue substitutions at predicted interfaces disrupt higher-order complexes that are primarily mediated by contacts between the C-terminal domain of FliG and the middle domain of a neighboring FliG molecule. Spin separations among multi-labeled components fit a self-consistent model that agree well with electron microscopy images of the C-ring. An activated form of the response regulator CheY destabilizes the parallel arrangement of FliM molecules to perturb FliG alignment in a process that may reflect the onset of rotation switching. These data suggest a model of C-ring assembly in which intermolecular contacts among FliG domains provide a template for FliM assembly and cooperative transitions.
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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.