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A repair protein like RecG moves the stalled replication fork in thedirection from the zipped to the unzipped state of DNA. It is proposed herethat a softening of the zipped-unzipped interface at the fork results in thefront propagating towards the unzipped side. In this scenario, an ordinaryhelicase destabilizes the zipped state locally near the interface and the forkpropagates towards the zipped side. The softening of the interface can beproduced by the aromatic interaction, predicted from crystal structure, betweenRecG and the nascent broken base pairs at the Y-fork. A numerical analysis ofthe model also reveals the possibility of a stop and go type motion.

Interfacial instability and DNA fork reversal by repair proteins