Transposition of a reconstructed Harbinger element in human cells and functional homology with two transposon-derived cellular genes

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Item Type:	Article
Title:	Transposition of a reconstructed Harbinger element in human cells and functional homology with two transposon-derived cellular genes
Creators Name:	Sinzelle, L., Kapitonov, V.V., Grzela, D.P., Jursch, T., Jurka, J., Izsvak, Z. and Ivics, Z.
Abstract:	Ancient, inactive copies of transposable elements of the PIF/Harbinger superfamily have been described in vertebrates. We reconstructed components of the Harbinger3_DR transposon in zebrafish, including a transposase and a second, transposon-encoded protein that has a Myb-like trihelix domain. The reconstructed Harbinger transposon shows efficient cut-and-paste transposition in human cells and preferentially inserts into a 15-bp consensus target sequence. The Myb-like protein is required for transposition and physically interacts with the N-terminal region of the transposase via its C-terminal domain. The Myb-like protein enables transposition in part by promoting nuclear import of the transposase, by directly binding to subterminal regions of the transposon, and by recruiting the transposase to the transposon ends. We investigated the functions of two transposon-derived human proteins: HARBI1, a domesticated transposase-derived protein, and NAIF1, which contains a trihelix motif similar to that described in the Myb-like protein. Physical interaction, subcellular localization, and DNA-binding activities of HARBI1 and NAIF1 suggest strong functional homologies between the Harbinger3_DR system and their related, host-encoded counterparts. The Harbinger transposon will serve as a useful experimental system for transposon biology and for investigating the enzymatic functions of domesticated, transposon-derived cellular genes.
Keywords:	Molecular Domestication, Myb Domain, Nuclear Import, Transposase, DNA Binding, Animals, Zebrafish
Source:	Proceedings of the National Academy of Sciences of the United States of America
ISSN:	0027-8424
Publisher:	National Academy of Sciences
Volume:	105
Number:	12
Page Range:	4715-4720
Date:	25 March 2008
Official Publication:	https://doi.org/10.1073/pnas.0707746105
PubMed:	View item in PubMed

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