The Retron system is a crucial prokaryotic anti-phage defense mechanism, composed of a noncoding RNA, reverse transcriptase, and effector proteins, which synthesizes multicopy single-stranded DNA to trigger immune responses. While Retron Ec86's anti-phage mechanism has been elucidated, other Retron types remain poorly understood. Here, we investigate Retron Ec78, a Type I-A system encoding effector proteins PtuA (ATPase) and PtuB (HNH nuclease). Structural analysis reveals that PtuA hexameric complex putatively bound to PtuB, with ATP playing a key role in hexamer assembly. Beyond its known role in abortive infection via tRNA degradation, we demonstrate that the PtuAB complex also exhibits DNA-cleaving activity. These findings provide novel insights into the assembly and dual functionality of the Retron Ec78 system, advancing our understanding of prokaryotic immune mechanisms against phage infection.
Duan et al. (2026) studied this question.
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