ArticleNucleic acids research2024
Structural basis for the concerted antiphage activity in the SIR2-HerA system.
Article in Nucleic acids research, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Type III Druantia two-component antiphage defense depends on the DruH-DruE interaction for inhibiting viral DNA circularization and replication.Cell insight · 2026Article
- Classification of Sir2-HerA systems reveals a multilayered regulatory cascade gating the type III antiphage activity.Nucleic acids research · 2026Article
- From Biocontrol to Synthesis: Innovative Progress ofInternational journal of molecular sciences · 2025Review
- Structural remodeling activates bacterial anti-phage immunity: insights from HerA-DUF4297.Frontiers in cellular and infection microbiology · 2025Review
- Mechanistic basis for the allosteric activation of NADase activity in the Sir2-HerA antiphage defense system.Nature communications · 2024Article
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Authors and funding
10 authors.
Funding
Abstract
Recently, a novel two-gene bacterial defense system against phages, encoding a SIR2 NADase and a HerA ATPase/helicase, has been identified. However, the molecular mechanism of the bacterial SIR2-HerA immune system remains unclear. Here, we determine the cryo-EM structures of SIR2, HerA and their complex from Paenibacillus sp. 453MF in different functional states. The SIR2 proteins oligomerize into a dodecameric ring-shaped structure consisting of two layers of interlocked hexamers, in which each subunit exhibits an auto-inhibited conformation. Distinct from the canonical AAA+ proteins, HerA hexamer alone in this antiphage system adopts a split spiral arrangement, which is stabilized by a unique C-terminal extension. SIR2 and HerA proteins assemble into a ∼1.1 MDa torch-shaped complex to fight against phage infection. Importantly, disruption of the interactions between SIR2 and HerA largely abolishes the antiphage activity. Interestingly, binding alters the oligomer state of SIR2, switching from a dodecamer to a tetradecamer state. The formation of the SIR2-HerA binary complex activates NADase and nuclease activities in SIR2 and ATPase and helicase activities in HerA. Together, our study not only provides a structural basis for the functional communications between SIR2 and HerA proteins, but also unravels a novel concerted antiviral mechanism through NAD+ degradation, ATP hydrolysis, and DNA cleavage.
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