ArticleNature structural & molecular biology2024
Molecular basis of Gabija anti-phage supramolecular assemblies.
Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 18 citations in OpenAlex.
- Biochemical Characterization of LsGajA: A Key Nuclease for Gabija Defense in Lactic Acid Bacteria.Microorganisms · 2026Article
- Structural investigation of QatB and QatC proteins in QatABCD anti-phage defense.Nature communications · 2026Article
- Nuclease-NTPase antiphage defence systems use conserved molecular features to control bacterial immunity.Nature microbiology · 2026Article
- Article
- Co-occurrence of diverse defense systems shapes complex microbe-virus relationships in deep-sea cold seeps.Nature communications · 2026Article
- Cran1, member of a new class of OLD family ATPases, functions in cell cycle progression in an archaeon.EMBO reports · 2026Article
- Structural basis for retron co-option of anti-phage ATPase-nuclease.Nature structural & molecular biology · 2026Article
- Characterization and diversity of defense systems inFrontiers in immunology · 2026Article
- Phage SSB detection by retron Eco8 msDNA unleashes nuclease-mediated immunity.Molecular cell · 2025Article
- Abundant bacterial nucleoid-associated protein H-NS limits plasmid transfer through mechanical modification of DNA.Nucleic acids research · 2025Article
- Structural basis of the RNA-mediated Retron-Eco2 oligomerization.Cell discovery · 2025Article
- Modularity of Zorya defense systems during phage inhibition.Nature communications · 2025Article
- An OLD protein teaches us new tricks: prokaryotic antiviral defense.Nature communications · 2024Article
- Structural and biochemical insights into the mechanism of the Gabija bacterial immunity system.Nature communications · 2024Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
As one of the most prevalent anti-phage defense systems in prokaryotes, Gabija consists of a Gabija protein A (GajA) and a Gabija protein B (GajB). The assembly and function of the Gabija system remain unclear. Here we present cryo-EM structures of Bacillus cereus GajA and GajAB complex, revealing tetrameric and octameric assemblies, respectively. In the center of the complex, GajA assembles into a tetramer, which recruits two sets of GajB dimer at opposite sides of the complex, resulting in a 4:4 GajAB supramolecular complex for anti-phage defense. Further biochemical analysis showed that GajA alone is sufficient to cut double-stranded DNA and plasmid DNA, which can be inhibited by ATP. Unexpectedly, the GajAB displays enhanced activity for plasmid DNA, suggesting a role of substrate selection by GajB. Together, our study defines a framework for understanding anti-phage immune defense by the GajAB complex.
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