AI Article Synopsis
- The stalling of DNA replication forks due to DNA damage poses a significant challenge for cells, necessitating effective repair mechanisms.
- RecG protein plays a vital role in managing stalled replication forks by reversing them past the damaged site, forming a four-way junction that permits template switching and bypass of lesions.
- The crystal structure of RecG bound to a DNA model of a stalled replication fork reveals its mechanism for recognizing junctions and suggests differences between the two largest helicase superfamilies in terms of their function and mechanism.
Article Abstract
The stalling of DNA replication forks that occurs as a consequence of encountering DNA damage is a critical problem for cells. RecG protein is involved in the processing of stalled replication forks, and acts by reversing the fork past the damage to create a four-way junction that allows template switching and lesion bypass. We have determined the crystal structure of RecG bound to a DNA substrate that mimics a stalled replication fork. The structure not only reveals the elegant mechanism used by the protein to recognize junctions but has also trapped the protein in the initial stage of fork reversal. We propose a mechanism for how forks are processed by RecG to facilitate replication fork restart. In addition, this structure suggests that the mechanism and function of the two largest helicase superfamilies are distinct.
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| http://dx.doi.org/10.1016/s0092-8674(01)00501-3 | DOI Listing |
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