Abstract
DNA transposons are responsible for transferring genetic information from one location to another and should provide a stable platform for use in human gene therapy. A multi-step process of DNA transposition is catalyzed by a transposase enzyme that should be sufficiently flexible to provide the catalytic site for each step of the reaction. Here we employ a combination of computational (minimal Distance Constraint Model) and experimental (Circular Dichroism spectroscopy) methods to investigate and compare the dynamics, the inter-residue couplings, and the role of DNA binding on the stability and flexibility of two representative members of Tc1/mariner family of transposases, the Sleeping Beauty (SB) and Mos1 transposases. To understand the link between dynamics and function, we further compare results for the original SB transposase and its hyperactive version SB100, which has a 100-fold increase in efficiency. Together, our data provide insights to how these transposases are structured and how they function.
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