ArticlePloS one2015
The bactofilin cytoskeleton protein BacM of Myxococcus xanthus forms an extended β-sheet structure likely mediated by hydrophobic interactions.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 60 citations in OpenAlex.
- Bactofilins are essential spatial organizers of peptidoglycan insertion in the Lyme disease spirocheteJournal of bacteriology · 2026Article
- Article
- Polymerization and flanking domains of the bactofilin BacA collectively regulate stalk formation in Asticcacaulis biprosthecum.PLoS genetics · 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
- A dynamic bactofilin cytoskeleton cooperates with an M23 endopeptidase to control bacterial morphogenesis.eLife · 2024Article
- Catching a Walker in the Act-DNA Partitioning by ParA Family of Proteins.Frontiers in microbiology · 2022Review
- A Dynamic, Ring-Forming Bactofilin Critical for Maintaining Cell Size in the Obligate Intracellular Bacterium Chlamydia trachomatis.Infection and immunity · 2021Article
- A predatory myxobacterium controls cucumber Fusarium wilt by regulating the soil microbial community.Microbiome · 2020Article
- The structure of bactofilin filaments reveals their mode of membrane binding and lack of polarity.Nature microbiology · 2019Article
- Article
- The Helicobacter pylori cell shape promoting protein Csd5 interacts with the cell wall, MurF, and the bacterial cytoskeleton.Molecular microbiology · 2018Article
- Bactofilin-mediated organization of the ParABS chromosome segregation system in Myxococcus xanthus.Nature communications · 2017Article
- Structure of the Bacterial Cytoskeleton Protein Bactofilin by NMR Chemical Shifts and Sequence Variation.Biophysical journal · 2016Article
- Atomic-resolution structure of cytoskeletal bactofilin by solid-state NMR.Science advances · 2015Article
- Cytoskeletal Proteins in Caulobacter crescentus: Spatial Orchestrators of Cell Cycle Progression, Development, and Cell Shape.Sub-cellular biochemistryReview
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
Abstract
Bactofilins are novel cytoskeleton proteins that are widespread in Gram-negative bacteria. Myxococcus xanthus, an important predatory soil bacterium, possesses four bactofilins of which one, BacM (Mxan_7475) plays an important role in cell shape maintenance. Electron and fluorescence light microscopy, as well as studies using over-expressed, purified BacM, indicate that this protein polymerizes in vivo and in vitro into ~3 nm wide filaments that further associate into higher ordered fibers of about 10 nm. Here we use a multipronged approach combining secondary structure determination, molecular modeling, biochemistry, and genetics to identify and characterize critical molecular elements that enable BacM to polymerize. Our results indicate that the bactofilin-determining domain DUF583 folds into an extended β-sheet structure, and we hypothesize a left-handed β-helix with polymerization into 3 nm filaments primarily via patches of hydrophobic amino acid residues. These patches form the interface allowing head-to-tail polymerization during filament formation. Biochemical analyses of these processes show that folding and polymerization occur across a wide variety of conditions and even in the presence of chaotropic agents such as one molar urea. Together, these data suggest that bactofilins are comprised of a structure unique to cytoskeleton proteins, which enables robust polymerization.
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.