ArticleBiochemistry2012
Structural insights into the interaction between the bacterial flagellar motor proteins FliF and FliG.
Article in Biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Role of FlhF and its domains in the assembly of a polar flagellum inJournal of bacteriology · 2025Article
- Article
- MotY modulates proton-driven flagellar motor output in Pseudomonas aeruginosa.BMC microbiology · 2024Article
- Article
- Bridging the N-terminal and middle domains in FliG of the flagellar rotor.Current research in structural biology · 2022Article
- Modulation of the Enzymatic Activity of the Flagellar Lytic Transglycosylase SltF by Rod Components and the Scaffolding Protein FlgJ inJournal of bacteriology · 2021Article
- Article
- Architecture and Assembly of the Bacterial Flagellar Motor Complex.Sub-cellular biochemistry · 2021Review
- Oligomerization of the FliF Domains Suggests a Coordinated Assembly of the Bacterial Flagellum MS Ring.Frontiers in microbiology · 2021Article
- The Architectural Dynamics of the Bacterial Flagellar Motor Switch.Biomolecules · 2020Review
- 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
- Crystal structure of the FliF-FliG complex fromThe Journal of biological chemistry · 2018Article
- 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
- 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
- Functional Characterization of EscK (Orf4), a Sorting Platform Component of the Enteropathogenic Escherichia coli Injectisome.Journal of bacteriology · 2017Article
- The Gearbox of the Bacterial Flagellar Motor Switch.Structure (London, England : 1993) · 2016Article
- Domain-based biophysical characterization of the structural and thermal stability of FliG, an essential rotor component of the NaBiophysics and physicobiology · 2016Article
- Article
- Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016Review
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Authors and funding
3 authors.
Funding
Abstract
The binding of the soluble cytoplasmic protein FliG to the transmembrane protein FliF is one of the first interactions in the assembly of the bacterial flagellum. Once established, this interaction is integral in keeping the flagellar cytoplasmic ring, responsible for both transmission of torque and control of the rotational direction of the flagellum, anchored to the central transmembrane ring on which the flagellum is assembled. Here we isolate and characterize the interaction between the N-terminal domain of Thermotoga maritima FliG (FliG(N)) and peptides corresponding to the conserved C-terminal portion of T. maritima FliF. Using nuclear magnetic resonance (NMR) and other techniques, we show that the last ~40 amino acids of FliF (FliF(C)) interact strongly (upper bound K(d) in the low nanomolar range) with FliG(N). The formation of this complex causes extensive conformational changes in FliG(N). We find that T. maritima FliG(N) is homodimeric in the absence of the FliF(C) peptide but forms a heterodimeric complex with the peptide, and we show that this same change in oligomeric state occurs in full-length T. maritima FliG, as well. We relate previously observed phenotypic effects of FliF(C) mutations to our direct observation of binding. Lastly, on the basis of NMR data, we propose that the primary interaction site for FliF(C) is located on a conserved hydrophobic patch centered along helix 1 of FliG(N). These results provide new detailed information about the bacterial flagellar motor and support efforts to understand the cytoplasmic ring's precise molecular structure and mechanism of rotational switching.
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