Nature published a mechanism that links bacterial antiviral defense to the repeat-writing logic of telomerase. DRT10 pairs a reverse transcriptase with a noncoding RNA and makes a long tandem-repeat DNA product from that RNA template. Cryo-electron microscopy shows two reverse-transcriptase monomers on opposite sides of a pseudo-symmetric RNA, but only one makes the long repeat. Two flanking stem-loop anchors delimit the template.
The paper’s phylogeny places telomerase in a monophyletic clade with the DRT family, supporting a common origin for their DNA-polymerization activity. That is stronger than an analogy between two enzymes; it is still not proof that a DRT10-like system directly became modern human telomerase by one simple step.
Columbia says the lab has already used DRT10 to synthesize human telomeric repeat DNA in human cells. The next claims remain open: whether it can lengthen chromosomes safely, prevent cellular senescence or help engineered T cells persist. There is a patent application and relevant investigator company interests, which matter when the work moves from mechanism toward application.
Nature — “Antiviral immunity via telomerase-like reverse transcription in bacteria,” October 12
Columbia University explanation