Abstract
A repair protein like RecG moves the stalled replication fork in the direction from thezipped to the unzipped state of DNA. It is proposed here that a softening of thezipped–unzipped interface at the fork results in the front propagating towards the unzippedside. In this scenario, an ordinary helicase destabilizes the zipped state locally near theinterface and the fork propagates towards the zipped side. The softening of the interfacecan be produced by the aromatic interaction, predicted from the crystal structure,between RecG and the nascent broken base pairs at the Y-fork. A numericalanalysis of the model also reveals the possibility of a stop and go type motion.
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