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Random walks on DNA

Scientists have revealed how a bacterial enzyme has evolved an energy-efficient method to move long distances along DNA. The findings, published in Science, present further insight into the coupling of chemical and mechanical energy by a class of enzymes called helicases, a widely-distributed group of proteins, which in human cells are implicated in some cancers.

The team studied a helicase found in bacteria that moves along viral (bacteriophage) DNA. The work demonstrated that, surprisingly, the enzyme only consumed ATP at the start of the reaction in order to change conformation. Thereafter long-range movement along the DNA was driven by thermal motion; in other words by collisions with the surrounding water molecules. This produces a characteristic one-dimensional “random walk” (see picture), where the protein is just as likely to move backwards as forwards.

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