The study, led by Richard Wong and his team, focused on nucleases like DNase I, which are responsible for clearing damaged or unwanted DNA. Using high-speed atomic force microscopy, the researchers bypassed the need for chemical staining or crystallization, allowing them to watch the interaction within a liquid environment. These observations confirmed that enzymes do not target DNA randomly; instead, they preferentially congregate around curved or bent segments. To categorize these behaviors, the team proposed the STORM framework—Scan, Target, Occupy, Rupture, and Mobilize—to describe the lifecycle of enzymatic interaction.
Scientists capture enzymes dismantling DNA in real-time
Researchers at Kanazawa University have utilized high-speed atomic force microscopy to observe enzymes in the act of fragmenting DNA molecules. By tracking individual proteins, the team discovered that enzymes repeatedly revisit specific, vulnerable regions of the DNA structure before initiating a break, revealing how physical shape dictates genetic degradation.
Beyond basic degradation, the researchers investigated how physical packaging protects genetic material. When DNA was condensed by protamine into compact, rod-like or ring-shaped toroids, it became remarkably resilient to enzymatic attack. DNase I molecules were observed gathering around these structures without success, as the physical density provided a barrier that the enzymes could not easily penetrate. Only when these compact structures were loosened did the DNA become susceptible to fragmentation again. These findings offer new insights into how cells preserve genetic integrity and suggest potential strategies for improving the stability of DNA-based therapeutics.
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