ArticleNucleic acids research2023
Structural and functional investigation of GajB protein in Gabija anti-phage defense.
Article in Nucleic acids research, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Biochemical Characterization of LsGajA: A Key Nuclease for Gabija Defense in Lactic Acid Bacteria.Microorganisms · 2026Article
- Cran1, member of a new class of OLD family ATPases, functions in cell cycle progression in an archaeon.EMBO reports · 2026Article
- Abundant bacterial nucleoid-associated protein H-NS limits plasmid transfer through mechanical modification of DNA.Nucleic acids research · 2025Article
- A DNA nicking Class 1 OLD family nuclease mediates phage defense in Vibrio cholerae and is countered by a phage-encoded inhibitor.Nucleic acids research · 2025Article
- AmBio · 2024Article
- AbioRxiv : the preprint server for biology · 2024Article
- Article
- An OLD protein teaches us new tricks: prokaryotic antiviral defense.Nature communications · 2024Article
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Authors and funding
6 authors.
Funding
Abstract
Bacteriophages (phages) are viruses that infect bacteria and archaea. To fend off invading phages, the hosts have evolved a variety of anti-phage defense mechanisms. Gabija is one of the most abundant prokaryotic antiviral systems and consists of two proteins, GajA and GajB. GajA has been characterized experimentally as a sequence-specific DNA endonuclease. Although GajB was previously predicted to be a UvrD-like helicase, its function is unclear. Here, we report the results of structural and functional analyses of GajB. The crystal structure of GajB revealed a UvrD-like domain architecture, including two RecA-like core and two accessory subdomains. However, local structural elements that are important for the helicase function of UvrD are not conserved in GajB. In functional assays, GajB did not unwind or bind various types of DNA substrates. We demonstrated that GajB interacts with GajA to form a heterooctameric Gabija complex, but GajB did not exhibit helicase activity when bound to GajA. These results advance our understanding of the molecular mechanism underlying Gabija anti-phage defense and highlight the role of GajB as a component of a multi-subunit antiviral complex in bacteria.
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