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TitleProtein-primed homopolymer synthesis by an antiviral reverse transcriptase.
Journal, issue, pagesNature, Vol. 643, Issue 8074, Page 1352-1362, Year 2025
Publish dateMay 28, 2025
AuthorsStephen Tang / Rimantė Žedaveinytė / Nathaniel Burman / Shishir Pandey / Josephine L Ramirez / Louie M Kulber / Tanner Wiegand / Royce A Wilkinson / Yanzhe Ma / Dennis J Zhang / George D Lampe / Mirela Berisa / Marko Jovanovic / Blake Wiedenheft / Samuel H Sternberg /
PubMed AbstractBacteria defend themselves from viral predation using diverse immune systems, many of which target foreign DNA for degradation. Defence-associated reverse transcriptase (DRT) systems provide an ...Bacteria defend themselves from viral predation using diverse immune systems, many of which target foreign DNA for degradation. Defence-associated reverse transcriptase (DRT) systems provide an intriguing counterpoint to this strategy by using DNA synthesis instead. We and others recently showed that DRT2 systems use an RNA template to assemble a de novo gene that encodes the antiviral effector protein Neo. It remains unclear whether similar mechanisms of defence are used by other related DRT families. Here, we show that DRT9 systems defend against phage using DNA homopolymer synthesis. Viral infection triggers polydeoxyadenylate (poly-dA) accumulation in the cell, driving abortive infection and population-level immunity. Cryo-electron microscopy structures reveal how a non-coding RNA serves as both a structural scaffold and reverse transcription template to direct hexameric complex assembly and poly-dA synthesis. Notably, biochemical and functional experiments identify tyrosine residues within the reverse transcriptase itself that probably prime DNA synthesis, leading to the formation of protein-DNA covalent adducts. Synthesis of poly-dA by DRT9 in vivo is regulated by the competing activities of phage-encoded triggers and host-encoded silencers. Collectively, our study identifies a nucleic-acid-driven defence system that expands the paradigm of bacterial immunity and broadens the known functions of reverse transcriptases.
External linksNature / PubMed:40436039 / PubMed Central
MethodsEM (single particle)
Resolution2.6 - 3.2 Å
Structure data

49523

9nlv

EMDB-49523, PDB-9nlv:
Cryo-EM structure of hexameric SenDRT9 RT-ncRNA complex
Method: EM (single particle) / Resolution: 2.6 Å

49525

9nlx

EMDB-49525, PDB-9nlx:
Cryo-EM structure of the trimeric SenDRT9 RT-ncRNA complex (GST fusion)
Method: EM (single particle) / Resolution: 3.2 Å

Source
  • salmonella enterica (bacteria)
  • escherichia coli (E. coli)
KeywordsIMMUNE SYSTEM / DRT9 / Polymerase / Complex

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