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Updated: May 9, 2025

Bacterial Artificial Chromosomes: A Functional Genomics Tool for the Study of Positive-strand RNA Viruses
Published on: December 29, 2015
Bacterial reverse transcriptase synthesizes long poly(A)-rich cDNA for antiphage defense.
Xin-Yi Song1, Yushan Xia1, Jun-Tao Zhang1
1Department of Biochemistry, SUSTech Homeostatic Medicine Institute, School of Medicine, Southern University of Science and Technology, Shenzhen, China.
Prokaryotic defense-associated reverse transcriptases (DRTs) activate antiphage defense by forming complexes that arrest cell growth. DRT9 synthesizes cDNA to disrupt phage propagation, revealing novel antiviral mechanisms.
Area of Science:
- Microbiology
- Molecular Biology
- Structural Biology
Background:
- Prokaryotic defense-associated reverse transcriptases (DRTs) possess antiviral functions, but their mechanisms are not fully understood.
- DRTs represent a diverse class of enzymes involved in microbial defense systems.
Purpose of the Study:
- To elucidate the functional mechanism of DRT9 in antiphage defense.
- To determine the structural basis of DRT9-ncRNA complex formation and activity.
Main Methods:
- Cryo-electron microscopy to determine the structure of the DRT9-ncRNA hexamer complex.
- Biochemical assays to analyze DRT9 activity and interaction with phage components.
Main Results:
- DRT9 forms a hexameric complex with non-coding RNA (ncRNA) to mediate antiphage defense.
- Activated DRT9 synthesizes long, poly-A-rich single-stranded cDNA, sequestering phage SSB protein and inducing abortive infection.
- The cryo-EM structure provides mechanistic insights into DRT9's cDNA synthesis.
Conclusions:
- DRT9 utilizes a novel mechanism involving cDNA synthesis for antiphage defense.
- These findings expand the known repertoire of reverse transcriptase-based antiviral strategies.
- The structural data can inform the development of DRT9-based biotechnological tools.
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