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PreprintCC BY-NC-NDbioRxiv

Defense-associated reverse transcriptases synthesize DNA in a telomerase-like manner

  • H. Zhang1
  • S. Chen
  • S. Zhang1
  • Y. Zhang1
  • P. Fu
  • T. Mao
  • Y. Zhan
  • J. Han
  • Z. Liu
  • Z. Shan
  • Z. Yuan
  • Y. Yu
1 more authors
  • H. Yin
  1. 1TianJin Medical University
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Abstract

Defense-associated reverse transcriptases (DRTs) constitute an emerging class of bacterial defense systems that harness reverse-transcriptase activity to generate cDNA products and counter phage infection. A distinct subset of DRT10 systems evolutionarily related to telomerase generates tandem-repeat DNA to confer antiphage immunity. Here, we biochemically characterize the reverse transcription activity of DRT10 and determine cryo-EM structures of DRT10-ncRNA complex in three functional states, revealing an unanticipated 2:1 RT:ncRNA assembly mode. Two DRT10 protomers dimerize through a central pair of interlocked {beta}-hairpins and are further embraced by a single ncRNA. This architecture distinguishes DRT10 from previously characterized DRT complexes, which either lack an ncRNA component or exhibit an equivalent stoichiometry of RT:ncRNA. Strikingly, despite the nearly identical conformations of the two DRT10 protomers, cDNA product density was resolved in only one catalytic pocket, revealing different product occupancy within the dimer. Moreover, along with flanking linkers, the stem loops of the ncRNA as fixed points to supply steric barriers help define the template boundary. These findings reveal a distinctive ncRNA-mediated DRT10 dimeric assembly and establish a mechanistic framework for protein-primed reverse transcription constrained by the length of the RNA flanking linker.

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Cite

BibTeXRIS
BibTeX
@misc{zhang2026defenseassociated,
  title = {{Defense-associated reverse transcriptases synthesize DNA in a telomerase-like manner}},
  author = {H. Zhang and S. Chen and S. Zhang and Y. Zhang and P. Fu and T. Mao and Y. Zhan and J. Han and Z. Liu and Z. Shan and Z. Yuan and Y. Yu and H. Yin},
  howpublished = {bioRxiv},
  year = {2026},
  month = oct,
  doi = {10.64898/2026.10.08.757509},
  url = {https://www.biorxiv.org/content/10.64898/2026.10.08.757509v1},
  note = {CC BY-NC-ND},
}
RIS
TY  - UNPB
TI  - Defense-associated reverse transcriptases synthesize DNA in a telomerase-like manner
AU  - H. Zhang
AU  - S. Chen
AU  - S. Zhang
AU  - Y. Zhang
AU  - P. Fu
AU  - T. Mao
AU  - Y. Zhan
AU  - J. Han
AU  - Z. Liu
AU  - Z. Shan
AU  - Z. Yuan
AU  - Y. Yu
AU  - H. Yin
PY  - 2026
DA  - 2026/10/08
PB  - bioRxiv
DO  - 10.64898/2026.10.08.757509
UR  - https://www.biorxiv.org/content/10.64898/2026.10.08.757509v1
AB  - Defense-associated reverse transcriptases (DRTs) constitute an emerging class of bacterial defense systems that harness reverse-transcriptase activity to generate cDNA products and counter phage infection. A distinct subset of DRT10 systems evolutionarily related to telomerase generates tandem-repeat DNA to confer antiphage immunity. Here, we biochemically characterize the reverse transcription activity of DRT10 and determine cryo-EM structures of DRT10-ncRNA complex in three functional states, revealing an unanticipated 2:1 RT:ncRNA assembly mode. Two DRT10 protomers dimerize through a central pair of interlocked {beta}-hairpins and are further embraced by a single ncRNA. This architecture distinguishes DRT10 from previously characterized DRT complexes, which either lack an ncRNA component or exhibit an equivalent stoichiometry of RT:ncRNA. Strikingly, despite the nearly identical conformations of the two DRT10 protomers, cDNA product density was resolved in only one catalytic pocket, revealing different product occupancy within the dimer. Moreover, along with flanking linkers, the stem loops of the ncRNA as fixed points to supply steric barriers help define the template boundary. These findings reveal a distinctive ncRNA-mediated DRT10 dimeric assembly and establish a mechanistic framework for protein-primed reverse transcription constrained by the length of the RNA flanking linker.
ER  -