GoKawiilBacterial defense protein DRT10 makes DNA repeats like telomerase
Researchers identified DRT10, a bacterial antiviral defense system in which a reverse transcriptase binds a noncoding RNA to repeatedly copy a defined RNA template into long tandem-repeat DNA. Cryo-EM structures show two reverse transcriptase molecules attached to opposite sides of the RNA, though only one produces the repeating DNA product, with stem-loop structures marking the boundaries of the copied region.
GoKawiil's interpretation of the reporting above, not reported fact.
The study suggests that this repeat-generating mechanism closely mirrors how eukaryotic telomerase extends chromosome ends, and phylogenetic analysis places telomerase and these bacterial defense reverse transcriptases in the same evolutionary lineage, hinting at a shared ancestral origin for repeat-building DNA synthesis. This could reshape understanding of how telomerase-like activity evolved and how bacteria repurpose reverse transcription for antiviral defense.
- DRT10 is a newly characterized bacterial antiviral system using an RNA-guided reverse transcriptase.
- Its 2:1 protein-to-RNA structure allows one subunit to generate repetitive DNA bounded by RNA stem-loops.
- Phylogenetic evidence links this mechanism to eukaryotic telomerase, implying a common evolutionary origin.
Source: nature.com — Tang, 2026-10-12
Published there as: “Antiviral immunity via telomerase-like reverse transcription in bacteria”
Read the original report → The summary and analysis above are GoKawiil's own, written from reporting by the source above. Facts and quotes belong to the original publisher.