DdrC, a DNA repair protein from Deinococcus radiodurans, recognises and stabilises DNA breaks by binding to both single-stranded and double-stranded lesions. It bridges and compacts DNA through a novel mechanism dependent on structural asymmetry, enhancing repair efficiency and supporting the bacterium’s exceptional resistance to DNA damage.
2024 August – Oxford Academic
Key takeaways
- DdrC stabilises DNA breaks, enhancing repair efficiency: DdrC binds to DNA at the sites of damage, particularly single-stranded and double-stranded breaks. This stabilisation prevents further DNA degradation and creates an environment conducive to effective repair processes. By ensuring the integrity of genetic material, such mechanisms are essential for longevity by countering the cumulative effects of DNA damage over time
- It bridges multiple DNA lesions, compacting damaged DNA into repair-ready structures: DdrC uniquely compacts DNA by binding to multiple lesions simultaneously, pulling them into close proximity. This compaction not only aids repair but also protects DNA from further environmental or intracellular stresses. The ability to efficiently manage and repair DNA damage is a cornerstone of maintaining cellular health and longevity
- Structural asymmetry in DdrC enables precise lesion recognition: The protein’s asymmetric structure plays a crucial role in identifying DNA lesions. This unique feature allows it to adapt to and recognise diverse DNA damage scenarios with remarkable precision, demonstrating the sophistication of the repair mechanisms that protect cellular functions over time
Robust DNA repair, such as that enabled by DdrC, helps maintain genomic stability. By countering the effects of DNA damage—a major contributor to cellular ageing and dysfunction—such mechanisms may offer insights into strategies for promoting longevity and healthy ageing in humans.
Read the article at: Szabla, Robert, et al. “DdrC, a Unique DNA Repair Factor from D. Radiodurans, Senses and Stabilizes DNA Breaks Through a Novel Lesion-Recognition Mechanism.” Nucleic Acids Research, vol. 52, no. 15, 2024, pp. 9282–9302. Oxford University Press, doi:10.1093/nar/gkae635.