ArticleNature communications2025
Bacterial Hachiman complex executes DNA cleavage for antiphage defense.
Article in Nature communications, 2025. 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.
- Molecular control of bacterial immunity.Nature structural & molecular biology · 2026Review
- Bacterial Defense and Phage Counterdefense: Unraveling the Molecular Basis of Phage Resistance.ACS omega · 2026Review
- Anti-phage defense systems in bacteria: molecular mechanisms and their role in shaping phage therapy strategies.Molecular biology reports · 2026Review
- An expanded realm of anti-CRISPR-associated proteins and regulatory mechanisms.Nucleic acids research · 2026Article
- Antiviral defence is a conserved function of diverse bacterial DNA glycosylases.Nature microbiology · 2026Article
- The antiphage mechanism of a widespread trypsin-MBL defense module.Nature chemical biology · 2026Article
- Phage-encoded factor stimulates DNA degradation by the Hna anti-phage defense system.Nature communications · 2026Article
- Structural insights into the assembly and function of Retron Ec78 PtuAB.Communications biology · 2026Article
- Nuclease-NTPase antiphage defence systems use conserved molecular features to control bacterial immunity.Nature microbiology · 2026Article
- Periplasmic gatekeeping of phage DNA entry by an rSAM enzyme matured effector with HxS repeats.Nature communications · 2026Article
- Modulation of Hachiman defence by a type II toxin-antitoxin system via balancing trade-off between the fitness cost and antiphage activity.Engineering microbiology · 2026Article
- Bacterial defense systems: Mechanisms, homology to eukaryotic immune systems, and applications.Zoological research · 2026Review
- A methylome-derived mbioRxiv : the preprint server for biology · 2026Article
- Recurrent acquisition of nuclease-protease pairs in antiviral immunity.Science (New York, N.Y.) · 2026Article
- Lactococcal mobile genetic elements harbour a diverse phage defensome rich in restriction-modification systems.Nucleic acids research · 2025Article
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Authors and funding
12 authors.
Funding
Abstract
Bacteria have developed a variety of immune systems to combat phage infections. The Hachiman system is a novel prokaryotic antiphage defense system comprising HamA and HamB proteins, which contains the DUF1837 and helicase domains, respectively. However, the defense mechanism remains only partially understood. Here, we present the cryo-electron microscopy (cryo-EM) structure of the Hachiman defense system featuring a fusion of Cap4 nuclease domain within HamA. Further structure analysis indicates that the DUF1837 domain on HamA resembles the PD-(D/E)XK nuclease but lacks active sites. Bioinformatics analysis reveals that catalytically inactive DUF1837 domains often recruit other functional domains to fulfill anti-phage defense. HamA interacts with HamB to form a heterodimer HamAB to mediate ATP hydrolysis and execute DNA cleavage, thus implementing antiphage defense. Our findings elucidate the structural basis of the Hachiman defense complex, highlighting the critical roles of the helicase and nuclease in prokaryotic immunity.
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