ArticleProceedings of the National Academy of Sciences of the United States of America2015
MinD-like ATPase FlhG effects location and number of bacterial flagella during C-ring assembly.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. 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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Who cites it
55 citing papers in PubMed.
- The last bacterial common ancestor encoded a complex flagellum.bioRxiv : the preprint server for biology · 2026Article
- Where and how many: evolutionary diversification of a molecular switch regulating flagellar patterns.Journal of bacteriology · 2026Review
- FlhG Cooperates With the Cell Cycle Regulator GpsB to Confine Peritrichous Flagella in B. subtilis.Molecular microbiology · 2025Article
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- Article
- MinD2 modulates cell shape and motility in the archaeonbioRxiv : the preprint server for biology · 2024Article
- Polar confinement of a macromolecular machine by an SRP-type GTPase.Nature communications · 2024Article
- Positioning of cellular components by the ParA/MinD family of ATPases.Current opinion in microbiology · 2024Review
- MinD proteins regulate CetZ1 localization inFrontiers in microbiology · 2024Article
- Structures of theProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Control of the flagellation pattern inJournal of bacteriology · 2023Article
- Multiple ParA/MinD ATPases coordinate the positioning of disparate cargos in a bacterial cell.Nature communications · 2023Article
- The Vibrio Polar Flagellum: Structure and Regulation.Advances in experimental medicine and biology · 2023Article
- The MinCDE Cell Division System Participates in the Regulation of Type III Secretion System (T3SS) Genes, Bacterial Virulence, and Motility inMicroorganisms · 2022Article
- Catching a Walker in the Act-DNA Partitioning by ParA Family of Proteins.Frontiers in microbiology · 2022Review
- Engineering Bacillus subtilis for the formation of a durable living biocomposite material.Nature communications · 2021Article
- Role of the major determinant of polar flagellation FlhG in the endoflagella-containing spirochete Leptospira.Molecular microbiology · 2021Article
- The antiactivator FleN uses an allosteric mechanism to regulate σScience advances · 2021Article
- Dissection of the ATPase active site of McdA reveals the sequential steps essential for carboxysome distribution.Molecular biology of the cell · 2021Article
- Dynamics of Bacterial Signal Recognition Particle at a Single Molecule Level.Frontiers in microbiology · 2021Article
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Authors and funding
12 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The number and location of flagella, bacterial organelles of locomotion, are species specific and appear in regular patterns that represent one of the earliest taxonomic criteria in microbiology. However, the mechanisms that reproducibly establish these patterns during each round of cell division are poorly understood. FlhG (previously YlxH) is a major determinant for a variety of flagellation patterns. Here, we show that FlhG is a structural homolog of the ATPase MinD, which serves in cell-division site determination. Like MinD, FlhG forms homodimers that are dependent on ATP and lipids. It interacts with a complex of the flagellar C-ring proteins FliM and FliY (also FliN) in the Gram-positive, peritrichous-flagellated Bacillus subtilis and the Gram-negative, polar-flagellated Shewanella putrefaciens. FlhG interacts with FliM/FliY in a nucleotide-independent manner and activates FliM/FliY to assemble with the C-ring protein FliG in vitro. FlhG-driven assembly of the FliM/FliY/FliG complex is strongly enhanced by ATP and lipids. The protein shows a highly dynamic subcellular distribution between cytoplasm and flagellar basal bodies, suggesting that FlhG effects flagellar location and number during assembly of the C-ring. We describe the molecular evolution of a MinD-like ATPase into a flagellation pattern effector and suggest that the underappreciated structural diversity of the C-ring proteins might contribute to the formation of different flagellation patterns.
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