It’s also worth noting that Drt3b has fascinating parallels, as well as mechanistic differences, with nucleotidyltransferases that append sequence-specific tails to RNA, including the CCA-adding enzyme and the poly(UG)-adding RDE-3. These enzymes are structurally quite distinct from RTs. (5/6)
All in all, it’s quite remarkable how creative bacterial defense systems can be! (6/6)
Great summary by @philipcball.bsky.social! Our findings certainly don’t invalidate the central dogma, but rather demonstrate an unexpected (and cool!) structural mechanism by which a sequence-specific DNA is created in a cell. (1/6)
1/9 New preprint from the Sternberg Lab in collaboration with the Nishimasu Lab! We uncover how the DRT3 antiphage immune system pairs two reverse transcriptases, one RNA-templated and one protein-templated, to build a double-stranded DNA effector. doi.org/10.64898/202...
Congratulations to the amazing team of co-first authors @poppy-pujuan-deng.bsky.social, @hyunbinlee0221.bsky.social, and Carlo Armijo!