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


ABSTRACT: 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-Tgf2TPase). Two truncated recombinant Tgf2 transposases with deletions in the N-terminal zinc finger domain, S1- and S2-Tgf2TPase, were expressed in bacteria from goldfish cDNAs. Both truncated Tgf2TPases lost their DNA-binding ability in vitro, specifically at the ends of Tgf2 transposon than native L-Tgf2TPase. Consequently, S1- and S2-Tgf2TPases mediated gene transfer in the zebrafish genome in vivo at a significantly (p?

SUBMITTER: Jiang XY 

PROVIDER: S-EPMC4890040 | biostudies-literature | 2016 Jun

REPOSITORIES: biostudies-literature

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

Jiang Xia-Yun XY   Hou Fei F   Shen Xiao-Dan XD   Du Xue-Di XD   Xu Hai-Li HL   Zou Shu-Ming SM  

Scientific reports 20160602


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-Tgf2TPase). Two truncated recombinant Tgf2 transposases with deletions  ...[more]

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