PUBLICATION
Transposition of a reconstructed Harbinger element in human cells and functional homology with two transposon-derived cellular genes
- Authors
- Sinzelle, L., Kapitonov, V.V., Grzela, D.P., Jursch, T., Jurka, J., Izsvák, Z., and Ivics, Z.
- ID
- ZDB-PUB-080326-17
- Date
- 2008
- Source
- Proceedings of the National Academy of Sciences of the United States of America 105(12): 4715-4720 (Journal)
- Registered Authors
- Ivics, Zoltan, Izsvák, Zsuzsa, Kapitonov, Vladimir
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Protein Binding
- Subcellular Fractions
- Mutagenesis, Insertional
- Proto-Oncogene Proteins c-myb/metabolism
- Protein Transport
- Animals
- Base Sequence
- Repetitive Sequences, Nucleic Acid/genetics
- DNA Transposable Elements/genetics*
- Consensus Sequence
- Humans
- Molecular Sequence Data
- Nuclear Proteins/chemistry
- Nuclear Proteins/genetics*
- Zebrafish
- Transposases/chemistry
- Transposases/genetics*
- Base Pairing
- Cell Nucleus/metabolism
- Sequence Homology, Amino Acid*
- Active Transport, Cell Nucleus
- Apoptosis Regulatory Proteins/chemistry
- Apoptosis Regulatory Proteins/genetics*
- HeLa Cells
- PubMed
- 18339812 Full text @ Proc. Natl. Acad. Sci. USA
Citation
Sinzelle, L., Kapitonov, V.V., Grzela, D.P., Jursch, T., Jurka, J., Izsvák, Z., and Ivics, Z. (2008) Transposition of a reconstructed Harbinger element in human cells and functional homology with two transposon-derived cellular genes. Proceedings of the National Academy of Sciences of the United States of America. 105(12):4715-4720.
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 terminal domain. The Myb-like protein enables transposition in part by promoting nuclear import of the transposase, by directly binding to subterminhe 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.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping