{
  "id": 10480119,
  "title": "Scientists Observe Enzymes Breaking Down DNA in Real Time",
  "url": "https://urgent.news/2026/09/28/scientists-observe-enzymes-breaking-down-dna-in-real-time",
  "topic": "science",
  "section": "Science",
  "published": "2026-09-28T15:30:34.000Z",
  "source": {
    "name": "GEN Biotechnology",
    "slug": "gen-biotechnology",
    "url": "https://www.genengnews.com/topics/omics/scientists-observe-enzymes-breaking-down-dna-in-real-time/"
  },
  "original_language": "en",
  "account": "Scientists at Japan's Nano Life Science Institute have captured high-speed footage of enzymes breaking down DNA in real-time. Utilizing advanced atomic force microscopy, the researchers observed enzymes repeatedly targeting vulnerable DNA regions before successfully cleaving them apart. Published in Nature Communications, the findings shed light on how DNA's structure influences its susceptibility to enzymatic degradation. This study provides a dynamic perspective on the fundamental question of why certain DNA regions are accessible to enzymes while others remain protected. The researchers utilized high-speed atomic force microscopy (HS-AFM) to directly visualize the interaction between individual nuclease enzymes and DNA. This technique allowed them to observe the enzymes' movements and interactions at the nanoscale without altering the biological samples. The HS-AFM movies revealed that the enzyme DNase I frequently targeted exposed DNA ends and regions with curved or locally bent DNA. By repeatedly returning to these restricted areas, DNase I increased the likelihood of successful fragmentation. The study also showed that the shape and higher-order organization of DNA significantly impacted where enzymes interacted with it. The researchers developed a conceptual framework called STORM (Scan–Target–Occupy–Rupture–Mobilize) to describe the complex interplay between DNA shape, enzyme engagement, and subsequent cleavage. This framework emphasizes the spatial and temporal correlations observed in the experiments rather than a fixed sequence of events. The findings suggest that DNA's physical organization, particularly when condensed by proteins like protamine, can provide protection from degradation. When protamine-bound DNA was examined, DNase I molecules rarely penetrated the compact structures, such as rod-like and toroidal configurations, which remained intact for extended periods. The study also found that loosening these condensed structures exposed DNA regions to enzymatic attack. Overall, the research provides new insights into the mechanisms governing DNA degradation and the role of DNA's structure in influencing enzymatic interactions.",
  "summary": "The research may be useful for the development of DNA-based therapeutics and gene-delivery systems. Packaging genetic material into structures that restrict nuclease access could potentially increase its resistance to degradation. The post Scientists Observe Enzymes Breaking Down DNA in Real Time appeared first on GEN - Genetic Engineering and Biotechnology News .",
  "key_points": [],
  "editors_take": null,
  "illustration": null,
  "coverage": {
    "outlets": 1,
    "also_reported_by": []
  },
  "ai_generated": true,
  "disclaimer": "Summaries, key points and the editor’s take are written by software from other outlets’ reporting and may contain errors — always check the linked original."
}