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Active  Hobo/Activator/Tam3 (hAT)  transposable elements are rarely found in vertebrates. Previously, goldfish  Tgf2  was found to be an autonomously active vertebrate transposon that is efficient at gene-transfer in teleost fish. However, little is known about  Tgf2  functional domains required for transposition. To explore this, we first predicted  in silico  a zinc finger domain in the N-terminus of full length  Tgf2  transposase (L- Tgf2 TPase). Two truncated recombinant  Tgf2  transposases with deletions in the N-terminal zinc finger domain, S1- and S2- Tgf2 TPase, were expressed in bacteria from goldfish cDNAs. Both truncated  Tgf2 TPases lost their DNA-binding ability  in vitro , specifically at the ends of  Tgf2  transposon than native L- Tgf2 TPase. Consequently, S1- and S2- Tgf2 TPases mediated gene transfer in the zebrafish genome  in vivo  at a significantly ( p  < 0.01) lower efficiency (21%–25%), in comparison with L- Tgf2 TPase (56% efficiency). Compared to L- Tgf2 TPase, truncated  Tgf2 TPases catalyzed imprecise excisions with partial deletion of TE ends and/or plasmid backbone insertion/deletion. The gene integration into the zebrafish genome mediated by truncated  Tgf2 TPases was imperfect, creating incomplete 8-bp target site duplications at the insertion sites. These results indicate that the zinc finger domain in  Tgf2  transposase is involved in binding to  Tgf2  terminal sequences, and loss of those domains has effects on TE transposition.

The N-terminal zinc finger domain of Tgf2 transposase contributes to DNA binding and to transposition activity