Helicases on crowded DNA

In physiological settings, all nucleic acids motor proteins must travel along substrates that are crowded with other proteins. However, the physical basis for how motor proteins behave in these highly crowded environments remains unknown. I used real-time single molecule imaging, kinetic Monte Carlo simulations and Molecular dynamics simulations to determine how the ATP-dependent translocase RecBCD travels along DNA occupied by obstacle proteins. I demonstrated that RecBCD forces each protein into its nearest adjacent neighbor, causing rapid disruption of underlying protein-nucleic acid interface.

References:

Sequential eviction of crowded nucleoprotein complexes by the RecBCD molecular motor

Terakawa T, Redding S, Silverstein TD, Greene EC

bioRxiv (2017)