Fig. 1: The eukaryotic Hermes transposon system. | Nature Communications

Fig. 1: The eukaryotic Hermes transposon system.

From: Zinc-finger BED domains drive the formation of the active Hermes transpososome by asymmetric DNA binding

Fig. 1

a The “cut-and-paste” transposition mechanism and Hermes transposon chemistry. The red arrows describe nucleophilic attacks on phosphate groups. TS target site. TSD target site duplication. b Schematic of the Hermes DNA transposon. The transposon has a left- and right-end (LE and RE, respectively) capped by two imperfect terminal inverted repeats (TIRs) that differ from one another by two swapped base pairs marked in italics. The ends flank the gene that encodes for the Hermes transposase (tnp). c Top: schematic of the domain organization of the Hermes transposase. DD dimerization domain. Bottom: octameric quaternary structure (tetramer of dimers) of BED-truncated (Δ-BED) Hermes in complex with the left-end terminal inverted repeat (LE-TIR) DNA (PDB: 4D1Q)11.

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