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- 🚀 100,000× faster evolution?!
🚀 100,000× faster evolution?!
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Anthony Ao
August 11, 2025
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Orthogonal T7 “evolution engine” turbocharges protein design ~100,000×, hitting 5,000× enzyme gains in days
Scripps Research reports T7-ORACLE, an orthogonal DNA replication system that installs a bacteriophage T7 replisome in E. coli to continuously hypermutate plasmid-encoded target genes while leaving the host genome intact.
The engineered T7 DNA polymerase reaches an in-vivo mutation rate of ~1.7×10⁻⁵ substitutions per base—~100,000-fold above the genomic rate.
In a proof-of-concept, the platform expanded the substrate scope of TEM-1 β-lactamase and boosted its activity ~5,000-fold against monobactam and cephalosporin antibiotics in <1 week.
The team emphasizes that the approach fits standard E. coli workflows and, per the accompanying press coverage, could speed therapeutic protein engineering and help predict resistance mutations. The study appeared in Science on August 7, 2025; the press summary ran August 8, 2025.
Why it matters
By safely cranking mutation rates on selectable targets while protecting the cell’s genome, T7-ORACLE offers a general, lab-friendly accelerator for directed evolution—potentially shrinking timelines for designing proteins and mapping drug-resistance pathways.
ELI5 Summary
Scientists built a safe “second DNA copier” inside bacteria that only scrambles the one gene you want to improve—leaving the rest of the cell alone. That turbo-copier makes changes about 100,000× faster than normal, so you can quickly test tons of protein versions and keep the best ones. In a demo, they evolved an enzyme that breaks down antibiotics so it could handle about 5,000× higher doses in under a week. In plain terms: it’s a fast-forward button for making better proteins.
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Anthony Ao
The PhDLevel Team
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