A Versatile Method to Quantify DNA-Protein Interactions on Negatively Supercoiled DNA

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Publication date
DOI http://dx.doi.org/10.1016/j.bpj.2018.11.1182
Reference G.A. King, F. Burla, E.J.G. Peterman and G.J.L. Wuite, A Versatile Method to Quantify DNA-Protein Interactions on Negatively Supercoiled DNA, Biophys. J. 116, 3: 214a-214a (2019)
Group Biological Soft Matter (relocated to TUDelft)

Many genomic processes are regulated by torsional stress, resulting in a range of supercoiled DNA structures. In order to understand the effect of such structures on protein binding and activity, several single-molecule techniques are often employed. These include magnetic, micro-pipette and angular optical tweezers. However, two factors can limit the study of DNA-protein interactions on supercoiled DNA. First, it is challenging to combine DNA-torque control with fluorescence microscopy. Second, the DNA substrate is typically tethered to a surface, hindering rapid buffer exchange.