ArticleNature communications2022
Structure-function studies reveal ComEA contains an oligomerization domain essential for transformation in gram-positive bacteria.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Structure and biochemistry reveal substrate-modulated ComEC nuclease activity during DNA processing.Nucleic acids research · 2026Article
- Reversible DNA condensation drives natural transformation.Nature communications · 2026Article
- Development of a Tool for High-Efficiency, Markerless and Iterative Genome Editing in Shouchella clausii.Microbial biotechnology · 2026Article
- Molecular interplay between ComEC domains allows for selective degradation of the non-translocating strand during natural transformation.Nucleic acids research · 2025Article
- ComFB, a widespread family of c-di-NMP receptor proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The molecular basis for DNA-binding by competence T4P is distinct in a representative Gram-positive and Gram-negative species.PLoS pathogens · 2025Article
- Naturally competent bacteria and their genetic parasites-a battle for control over horizontal gene transfer?FEMS microbiology reviews · 2025Review
- Host-dependent alteration of the gut microbiota: the role of luminal microRNAs.Microbiome research reports · 2025Review
- Molecular mechanisms and applications of natural transformation in bacteria.Frontiers in microbiology · 2025Review
- Methods for the Design and Analysis of Analytical Ultracentrifugation Experiments.Current protocols · 2024Article
- Visualizing dynamic competence pili and DNA capture throughout the long axis ofJournal of bacteriology · 2023Article
- Characterization and quantification of adeno-associated virus capsid-loading states by multi-wavelength analytical ultracentrifugation with UltraScan.Nanomedicine (London, England) · 2023Article
- Investigation of dynamic solution interactions between NET-1 and UNC-5B by multi-wavelength analytical ultracentrifugation.European biophysics journal : EBJ · 2023Article
- A spectral decomposition quality assessment tool for multi-wavelength AUC experiments with UltraScan.European biophysics journal : EBJ · 2023Article
- Visualizing dynamic competence pili and DNA capture throughout the long axis ofbioRxiv : the preprint server for biology · 2023Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
An essential step in bacterial transformation is the uptake of DNA into the periplasm, across the thick peptidoglycan cell wall of Gram-positive bacteria, or the outer membrane and thin peptidoglycan layer of Gram-negative bacteria. ComEA, a DNA-binding protein widely conserved in transformable bacteria, is required for this uptake step. Here we determine X-ray crystal structures of ComEA from two Gram-positive species, Bacillus subtilis and Geobacillus stearothermophilus, identifying a domain that is absent in Gram-negative bacteria. X-ray crystallographic, genetic, and analytical ultracentrifugation (AUC) analyses reveal that this domain drives ComEA oligomerization, which we show is required for transformation. We use multi-wavelength AUC (MW-AUC) to characterize the interaction between DNA and the ComEA DNA-binding domain. Finally, we present a model for the interaction of the ComEA DNA-binding domain with DNA, suggesting that ComEA oligomerization may provide a pulling force that drives DNA uptake across the thick cell walls of Gram-positive bacteria.
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