Structural highlights
Function
A0AAD2V6K7_ECOLX
Publication Abstract from PubMed
Reverse transcriptases (RTs) have well-established roles in the replication and spread of retroviruses and retrotransposons. However, recent evidence suggests that RTs have been conscripted by cells for diverse roles in antiviral defense. Here we determine structures of a type I-A retron, which explain how RNA, DNA, RT, HNH-nuclease and four molecules of an SMC-family ATPase assemble into a 364 kDa complex that provides phage defense. We show that phage-encoded nucleases trigger degradation of the retron-associated DNA, leading to disassembly of the retron and activation of the HNH nuclease. The HNH nuclease cleaves tRNA (Ser) , stalling protein synthesis and arresting viral replication. Taken together, these data reveal diverse and paradoxical roles for RTs in the perpetuation and elimination of genetic parasites.
Structural basis of antiphage defense by an ATPase-associated reverse transcriptase.,George JT, Burman N, Wilkinson RA, de Silva S, McKelvey-Pham Q, Buyukyoruk M, Dale A, Landman H, Graham A, DeLuca SZ, Wiedenheft B bioRxiv [Preprint]. 2025 Mar 26:2025.03.26.645336. doi: , 10.1101/2025.03.26.645336. PMID:40196496[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ George JT, Burman N, Wilkinson RA, de Silva S, McKelvey-Pham Q, Buyukyoruk M, Dale A, Landman H, Graham A, DeLuca SZ, Wiedenheft B. Structural basis of antiphage defense by an ATPase-associated reverse transcriptase. bioRxiv [Preprint]. 2025 Mar 26:2025.03.26.645336. PMID:40196496 doi:10.1101/2025.03.26.645336