Saha, P.; Saravanan, Y.; Marchesi, A.; Valotteau, C.; Revy, P.; Paull, T. T.; Assenza, S.; Hopfner, K.-P.; Modesti, M.; Rico, F.

Coiled coils are structural motifs in proteins that play diverse functions. In MRE11-RAD50 (MR) complexes, ATP-driven changes in coiled coils are essential for DNA break sensing. However, coiled coil dynamics and its modulation by protein conformational changes remain unclear, partly due to the lack of quantitative tools. Here, we used high-speed atomic force microscopy (HS-AFM) for real-time visualization of the coiled coil conformational dynamics of individual MR complexes from bacteria and human homologs, and a biomedically relevant variant. The mean square deviation of the end-to-end distance of the coiled coils revealed a power-law scaling with time, conserved across conformational states, homologs, and variants, suggesting a universal dynamic scaling. Coiled coils behave as semi-flexible filaments with strong internal friction, leading to relaxation times that were seconds-long and varied among conformational states and variants. Molecular dynamics simulations indicated that strong friction arose from long-lifetime contacts between coils. Our results suggest that MR complexes modulate the coiled coil dynamics to mediate long-range allosteric and allodynamic communication during DNA repair.