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TitleNon-coding RNA mediates the defense-associated reverse transcriptase (DRT) anti-phage oligomerization transition.
Journal, issue, pagesEMBO J, Vol. 44, Issue 19, Page 5429-5442, Year 2025
Publish dateAug 20, 2025
AuthorsJie Han / Bin Liu / Jingjing Tang / Shuqin Zhang / Xiaoshen Wang / Xuzichao Li / Qian Zhang / Zhikun Liu / Wanyao Wang / Yingcan Liu / Ruimin Zhou / Hang Yin / Yong Wei / Zhuang Li / Minjie Zhang / Zengqin Deng / Heng Zhang /
PubMed AbstractDefense-associated reverse transcriptase (DRT) systems are implicated in prokaryotic resistance to viral infections, yet the molecular mechanisms underlying their functionality remain largely unknown. ...Defense-associated reverse transcriptase (DRT) systems are implicated in prokaryotic resistance to viral infections, yet the molecular mechanisms underlying their functionality remain largely unknown. Here, we characterize a two-component DRT9 system, composed of a reverse transcriptase (RT) and a non-coding RNA (ncRNA), which exhibits a protein-primed DNA synthesis activity upon phage infection. We also determine its cryo-electron microscopy (cryo-EM) structures in different functional states. DRT9 RT binds to ncRNA, forming a dimer of dimers configuration that assembles into a trimer of dimers upon substrate binding. This oligomerization transition, crucial for DRT9-mediated anti-phage defense, is facilitated by a ncRNA cooperative self-assembly manner. Furthermore, substrate binding induces large conformational movements around the catalytic pocket of DRT9 RT, revealing a "lock-switch" mechanism for enzymatic activation. Notably, phylogenetic analysis and functional assays identify a unique N-terminal helix extension required for ncRNA stabilization and enzymatic activity, distinct from previously reported reverse transcriptase systems. Overall, our findings illuminate the molecular basis of DRT9-mediated antiviral defense and expand the functional and mechanistic diversity of the DRT family.
External linksEMBO J / PubMed:40836036 / PubMed Central
MethodsEM (single particle)
Resolution3.46 - 3.49 Å
Structure data

65143

9vku

EMDB-65143, PDB-9vku:
Cryo-EM structure of DRT9 tetramer complex
Method: EM (single particle) / Resolution: 3.49 Å

65181

9vma

EMDB-65181, PDB-9vma:
Cryo-EM structure of substrate-bound DRT9 hexamer complex
Method: EM (single particle) / Resolution: 3.46 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-DTP:
2'-DEOXYADENOSINE 5'-TRIPHOSPHATE

Source
  • escherichia coli (E. coli)
KeywordsANTIVIRAL PROTEIN/RNA / a protein complex / ANTIVIRAL PROTEIN-RNA complex / ANTIVIRAL PROTEIN/RNA/DNA / complex / ANTIVIRAL PROTEIN-RNA-DNA complex

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