Genome duplication is an inherently accurate process that relies on a close interplay between the DNA replication and repair machinery.This interplay arises because the replication machinery frequently encounters roadblocks that have the potential to stall or collapse a replication fork.The RecG DNA helicase catalyzes stalled replication fork rescue in an ATP-dependent manner, leading to the formation of a Holliday Junctiontype (HJ) structure that is then processed by RuvAB.Recent studies suggest that the activity of RecG in the early stages of fork rescue is enhanced and controlled by the single-stranded DNA binding protein (SSB).To understand how this occurs, we used two separate single molecule studies: atomic force microscopy (AFM) to visualize directly the interaction of RecG with a fork DNA in the presence of SSB and, a combination of optical and magnetic tweezers to understand how RecG catalyzes fork regression.