Detection of ATP hydrolysis through motion of nanoconfined DNA

Confinement of DNA to nanochannels with a cross-section of 100$\times$100 nm$^2$ and hundreds of micrometer long has previously been used to investigate the equilibrium binding properties of proteins to DNA. Here we report on the observation that a range of proteins which catalyze a modification of DNA, and that do so by hydrolyzing ATP, cause a net directed motion of nanochannel-confined DNA. We present a model for this observation that does not require any motor-like action of the protein and that is purely dependent on the catalytic properties.