ArticleNucleic acids research2018
ComM is a hexameric helicase that promotes branch migration during natural transformation in diverse Gram-negative species.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 59 citations in OpenAlex.
- Genomic and functional dissection of natural transformation-related genes inMicrobiology spectrum · 2026Article
- Molecular interplay between ComEC domains allows for selective degradation of the non-translocating strand during natural transformation.Nucleic acids research · 2025Article
- DprA recruits ComM to facilitate recombination during natural transformation in Gram-negative bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- SbcB facilitates natural transformation inJournal of bacteriology · 2025Article
- Naturally competent bacteria and their genetic parasites-a battle for control over horizontal gene transfer?FEMS microbiology reviews · 2025Review
- Development of SacB-based counterselection for efficient allelic exchange inMicrobiology spectrum · 2025Article
- Evolution and spread ofMicrobial genomics · 2025Article
- Structural insights into the mechanism of DNA branch migration during homologous recombination in bacteria.The EMBO journal · 2024Article
- Intragenomic conflicts with plasmids and chromosomal mobile genetic elements drive the evolution of natural transformation within species.PLoS biology · 2024Article
- Manipulation of natural transformation by AbaR-type islands promotes fixation of antibiotic resistance inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Multiple host colonization and differential expansion of multidrug-resistant ST25-Acinetobacter baumannii clades.Scientific reports · 2023Article
- DNA modifications impact natural transformation of Acinetobacter baumannii.Nucleic acids research · 2023Article
- Modularity and diversity of target selectors in Tn7 transposons.Molecular cell · 2023Article
- Vibrio cholerae biofilms use modular adhesins with glycan-targeting and nonspecific surface binding domains for colonization.Nature communications · 2023Article
- The RecA-directed recombination pathway of natural transformation initiates at chromosomal replication forks in the pneumococcus.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Subcellular localization of type IV pili regulates bacterial multicellular development.Nature communications · 2022Article
- The molecular basis of FimT-mediated DNA uptake during bacterial natural transformation.Nature communications · 2022Article
- Article
- The molecular diversity of transcriptional factor TfoX is a determinant in natural transformation inFrontiers in microbiology · 2022Article
- Motor-independent retraction of type IV pili is governed by an inherent property of the pilus filament.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
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Authors and funding
6 authors at 1 institution in 1 country.
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Abstract
Acquisition of foreign DNA by natural transformation is an important mechanism of adaptation and evolution in diverse microbial species. Here, we characterize the mechanism of ComM, a broadly conserved AAA+ protein previously implicated in homologous recombination of transforming DNA (tDNA) in naturally competent Gram-negative bacterial species. In vivo, we found that ComM was required for efficient comigration of linked genetic markers in Vibrio cholerae and Acinetobacter baylyi, which is consistent with a role in branch migration. Also, ComM was particularly important for integration of tDNA with increased sequence heterology, suggesting that its activity promotes the acquisition of novel DNA sequences. In vitro, we showed that purified ComM binds ssDNA, oligomerizes into a hexameric ring, and has bidirectional helicase and branch migration activity. Based on these data, we propose a model for tDNA integration during natural transformation. This study provides mechanistic insight into the enigmatic steps involved in tDNA integration and uncovers the function of a protein required for this conserved mechanism of horizontal gene transfer.
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