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Peer-reviewedCC BY-NC-ND 4.0Nature Communications

Molecular basis of DNA polymerase ζ’s reverse transcriptase activity

  • Radhika Malik1
  • Robert E. Johnson2
  • Louise Prakash2
  • Satya Prakash2
  • Aneel K. Aggarwal1
  1. 1Department of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai, New York, NY USA
  2. 2Department of Biochemistry and Molecular Biology, University of Texas Medical Branch, Galveston, TX USA
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Abstract

DNA polymerase ζ (Polζ) has emerged as a key reverse transcriptase in RNA-templated double-strand break repair (RT-DSBR), beyond its canonical role in translesion DNA synthesis (TLS). We present here the cryo-EM structure of yeast Polζ (including Rev1) in the act of reverse transcription, wherein the polymerase molds the replicative end of the bound RNA:DNA hybrid into B-like conformation and retains most contacts seen with DNA:DNA. Critically, the polymerase adopts the same conformation as with DNA:DNA, indicating its inherent versatility in accommodating both DNA:DNA and RNA:DNA substrates to preserve genome stability.

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Cite

BibTeXRIS
BibTeX
@article{malik2026molecular,
  title = {{Molecular basis of DNA polymerase ζ’s reverse transcriptase activity}},
  author = {Radhika Malik and Robert E. Johnson and Louise Prakash and Satya Prakash and Aneel K. Aggarwal},
  journal = {Nature Communications},
  year = {2026},
  month = sep,
  doi = {10.1038/s41467-026-78032-8},
  url = {https://doi.org/10.1038/s41467-026-78032-8},
  note = {CC BY-NC-ND 4.0},
}
RIS
TY  - JOUR
TI  - Molecular basis of DNA polymerase ζ’s reverse transcriptase activity
AU  - Radhika Malik
AU  - Robert E. Johnson
AU  - Louise Prakash
AU  - Satya Prakash
AU  - Aneel K. Aggarwal
PY  - 2026
DA  - 2026/09/25
JO  - Nature Communications
DO  - 10.1038/s41467-026-78032-8
UR  - https://doi.org/10.1038/s41467-026-78032-8
AB  - DNA polymerase ζ (Polζ) has emerged as a key reverse transcriptase in RNA-templated double-strand break repair (RT-DSBR), beyond its canonical role in translesion DNA synthesis (TLS). We present here the cryo-EM structure of yeast Polζ (including Rev1) in the act of reverse transcription, wherein the polymerase molds the replicative end of the bound RNA:DNA hybrid into B-like conformation and retains most contacts seen with DNA:DNA. Critically, the polymerase adopts the same conformation as with DNA:DNA, indicating its inherent versatility in accommodating both DNA:DNA and RNA:DNA substrates to preserve genome stability.
SN  - 2041-1723
ER  -