ArticleNature communications2025
Architecture and mechanism of a dual-enzyme retron system in prokaryotic immunity.
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 7 papers.
What it found
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Who cites it
7 citing papers in PubMed.
- Higher-order assembly of a type IX retron enables exploitation for designer antimicrobials.bioRxiv : the preprint server for biology · 2026Article
- Mechanistic insights into activation of bacterial Retron-Eco8 immunity by phage protein SSB.Nature communications · 2026Article
- Structural insights into the assembly and function of Retron Ec78 PtuAB.Communications biology · 2026Article
- Structure and mechanism of antiphage retron Eco2.Nature structural & molecular biology · 2026Article
- Structural mechanism of the Retron-Eco7 anti-phage defense system.Nature communications · 2025Article
- Phage nuclease-mediated defense activation of the bacterial Retron-Eco7 toxin-antitoxin system.Nucleic acids research · 2025Article
- Non-coding RNA mediates the defense-associated reverse transcriptase (DRT) anti-phage oligomerization transition.The EMBO journal · 2025Article
Corrections and comments
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Authors and funding
16 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Retrons are bacterial genetic retroelements encoding a reverse transcriptase (RT) and a non-coding RNA (ncRNA)-multi-copy single-stranded DNA (msDNA) hybrid. Diverse effector proteins or domains are found to associate with retrons, typically forming tripartite toxin-antitoxin systems involved in anti-phage defense. Although retrons have attracted growing interest in genome editing technologies, the mechanisms underlying most retron-mediated immune systems remain poorly understood. Here, we characterize a distinct quaternary retron system, Ec78, harboring a dual-component effector complex in which the PtuA ATPase and PtuB nuclease act in concert to mediate phage clearance. The cryo-EM structure of the Ec78 complex adopts a flower-basket-like architecture, with two Ec78 retrons engaging the PtuAB effector complexes through a msDNA-insertion assembly mechanism. Shortening of msDNA in length releases the PtuAB from Ec78 retron and triggers its activation. The cryo-EM structure of the retron-unbound effector complex further reveals an arginine-lysine finger loop on the PtuB nuclease that undergoes an ordered-to-disordered transition during enzymatic activation. These findings delineate the molecular basis underlying the Ec78 system in antiviral defense and highlight the mechanistic diversity of retron systems in prokaryotic immunity.
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