Structural insights into the assembly and function of Retron Ec78 PtuAB

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.

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Publication Details

Journal
Communications Biology
Published
2026-05-09
DOI
https://doi.org/10.1038/s42003-026-10199-8
Primary Topic
Boron Compounds in Chemistry
Type
article
Field-Weighted Citation Impact
0.00

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article

Structural insights into the assembly and function of Retron Ec78 PtuAB

Qingguo Gong, Kaiming Zhang, Leyuan Duan, Xiao Yun Li et al.
Communications Biology
Boron Compounds in Chemistry
article

Structural insights into the assembly and function of Retron Ec78 PtuAB

Qingguo Gong, Kaiming Zhang, Leyuan Duan, Xiao Yun Li, Shanshan Li, Lu Chen, Qian Hu
article en

Abstract

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.

Communications Biology
University of Science and Technology of China (CN)
National Natural Science Foundation of China
Openalex Percentile: Top 7%
Boron Compounds in Chemistry
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