Formation of the active Hermes transpososome is driven by asymmetric DNA binding of BED domains
L. Lannes, C. M. Furman, A. B. Hickman, F. Dyda
The paper investigates how the Hermes transposase forms an active tetramer and shows that it binds asymmetrically to the transposon ends, with stronger interaction at the left-end through BED domains.
bioRxiv · Sep 16, 2022 · PreprintBiochemistry