Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding. The Hermes DNA transposon is a member of the eukaryotic hAT superfamily, and its transposase forms a ring-shaped tetramer of dimers. Our investigation, combining biochemical, crystallography and cryo-electron microscopy, and in-cell assays, shows that the full-length Hermes octamer extensively interacts with its transposon left-end through multiple BED domains of three Hermes protomers... Authors: Laurie Lannes, Christopher M Furman, Alison B Hickman, Fred Dyda. Nat Commun. 2023 Jul 25;14(1):4470. doi: 10.1038/s41467-023-40210-3. Previous Science Highlights
