ArticleNature microbiology2019
The structure of bactofilin filaments reveals their mode of membrane binding and lack of polarity.
Article in Nature microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
25 citing papers in PubMed, 55 citations in OpenAlex.
- Bactofilins are essential spatial organizers of peptidoglycan insertion in the Lyme disease spirocheteJournal of bacteriology · 2026Article
- Collecting Large Datasets of Unambiguous Structural Restraints for Protein Structure Determination by 4D Proton-Detected Solid-State NMR.Chemphyschem : a European journal of chemical physics and physical chemistry · 2026Article
- Article
- Reply to Sleutel and Remaut,mBio · 2025Article
- Polymerization and flanking domains of the bactofilin BacA collectively regulate stalk formation in Asticcacaulis biprosthecum.PLoS genetics · 2025Article
- Coupling chromosome organization to genome segregation in Archaea.Nature communications · 2025Article
- Functional specialization of the subdomains of a bactofilin driving stalk morphogenesis inbioRxiv : the preprint server for biology · 2024Article
- Halofilins as emerging bactofilin families of archaeal cell shape plasticity orchestrators.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Leptospira interrogans biofilm transcriptome highlights adaption to starvation and general stress while maintaining virulence.NPJ biofilms and microbiomes · 2024Article
- The Description of Pseudoalteromonas apostichopi sp. nov., Vibrio apostichopi sp. nov., and Marinobacter apostichopi sp. nov. from the Fertilized Eggs and Larvae of Apostichopus japonicus.Current microbiology · 2024Article
- Structural insight intomBio · 2024Article
- A dynamic bactofilin cytoskeleton cooperates with an M23 endopeptidase to control bacterial morphogenesis.eLife · 2024Article
- The Unique N-Terminal Domain of Chlamydial Bactofilin Mediates Its Membrane Localization and Ring-Forming Properties.Journal of bacteriology · 2023Article
- Interacting bactofilins impact cell shape of the MreB-less multicellular Rhodomicrobium vannielii.PLoS genetics · 2023Article
- MultipleFrontiers in cellular and infection microbiology · 2023Article
- MultipleFrontiers in microbiology · 2023Article
- Distinct regions ofeLife · 2022Article
- Functional Bacterial Amyloids: Understanding Fibrillation, Regulating Biofilm Fibril Formation and Organizing Surface Assemblies.Molecules (Basel, Switzerland) · 2022Review
- Strain-dependent motility defects and suppression by a flhO mutation for B. subtilis bactofilins.BMC research notes · 2022Article
- Weaving of bacterial cellulose by the Bcs secretion systems.FEMS microbiology reviews · 2022Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Bactofilins are small β-helical proteins that form cytoskeletal filaments in a range of bacteria. Bactofilins have diverse functions, from cell stalk formation in Caulobacter crescentus to chromosome segregation and motility in Myxococcus xanthus. However, the precise molecular architecture of bactofilin filaments has remained unclear. Here, sequence analysis and electron microscopy results reveal that, in addition to being widely distributed across bacteria and archaea, bactofilins are also present in a few eukaryotic lineages such as the Oomycetes. Electron cryomicroscopy analysis demonstrated that the sole bactofilin from Thermus thermophilus (TtBac) forms constitutive filaments that polymerize through end-to-end association of the β-helical domains. Using a nanobody, we determined the near-atomic filament structure, showing that the filaments are non-polar. A polymerization-impairing mutation enabled crystallization and structure determination, while reaffirming the lack of polarity and the strength of the β-stacking interface. To confirm the generality of the lack of polarity, we performed coevolutionary analysis on a large set of sequences. Finally, we determined that the widely conserved N-terminal disordered tail of TtBac is responsible for direct binding to lipid membranes, both on liposomes and in Escherichia coli cells. Membrane binding is probably a common feature of these widespread but only recently discovered filaments of the prokaryotic cytoskeleton.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.