ArticlePeerJ2016
Structural modeling of the flagellum MS ring protein FliF reveals similarities to the type III secretion system and sporulation complex.
Article in PeerJ, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 33 citations in OpenAlex.
- Annotating microbial functions with ProkFunFind.mSystems · 2024Article
- Flagellar motor remodeling during swarming requires FliL.Molecular microbiology · 2023Article
- Control of the flagellation pattern inJournal of bacteriology · 2023Article
- Flagellar motor remodeling during swarming requires FliL.bioRxiv : the preprint server for biology · 2023Article
- FlgV forms a flagellar motor ring that is required for optimal motility of Helicobacter pylori.PloS one · 2023Article
- Pharmacologically induced weight loss is associated with distinct gut microbiome changes in obese rats.BMC microbiology · 2022Article
- Structure and Assembly of the Bacterial Flagellum.Sub-cellular biochemistry · 2022Review
- Role of the N- and C-terminal regions of FliF, the MS ring component inJournal of bacteriology · 2021Article
- Article
- Oligomerization of the FliF Domains Suggests a Coordinated Assembly of the Bacterial Flagellum MS Ring.Frontiers in microbiology · 2021Article
- Symmetry mismatch in the MS-ring of the bacterial flagellar rotor explains the structural coordination of secretion and rotation.Nature microbiology · 2020Article
- Motility, Biofilm Formation and Antimicrobial Efflux of Sessile and Planktonic Cells ofPathogens (Basel, Switzerland) · 2019Article
- A coevolution-guided model for the rotor of the bacterial flagellar motor.Scientific reports · 2018Article
- By Staying Together, Two Genes Keep the Motor Running.Structure (London, England : 1993) · 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
- A ring-shaped conduit connects the mother cell and forespore during sporulation in Bacillus subtilis.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Type Three Secretion System in Attaching and Effacing Pathogens.Frontiers in cellular and infection microbiology · 2016Review
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The flagellum is a large proteinaceous organelle found at the surface of many bacteria, whose primary role is to allow motility through the rotation of a long extracellular filament. It is an essential virulence factor in many pathogenic species, and is also a priming component in the formation of antibiotic-resistant biofilms. The flagellum consists of the export apparatus on the cytosolic side; the basal body and rotor, spanning the bacterial membrane(s) and periplasm; and the hook-filament, that protrudes away from the bacterial surface. Formation of the basal body MS ring region, constituted of multiple copies of the protein FliF, is one of the initial steps of flagellum assembly. However, the precise architecture of FliF is poorly understood. Here, I report a bioinformatics analysis of the FliF sequence from various bacterial species, suggesting that its periplasmic region is composed of three globular domains. The first two are homologous to that of the type III secretion system injectisome proteins SctJ, and the third possesses a similar fold to that of the sporulation complex component SpoIIIAG. I also describe that Chlamydia possesses an unusual FliF protein, lacking part of the SctJ homology domain and the SpoIIIAG-like domain, and fused to the rotor component FliG at its C-terminus. Finally, I have combined the sequence analysis of FliF with the EM map of the MS ring, to propose the first atomic model for the FliF oligomer, suggesting that FliF is structurally akin to a fusion of the two injectisome components SctJ and SctD. These results further define the relationship between the flagellum, injectisome and sporulation complex, and will facilitate future structural characterization of the flagellum basal body.
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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.