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| Item Type: | Article |
|---|---|
| Title: | Involvement of a bifunctional, paired-like DNA-binding domain and a transpositional enhancer in Sleeping Beauty transposition |
| Creators Name: | Izsvak, Z. and Khare, D. and Behlke, J. and Heinemann, U. and Plasterk, R.H. and Ivics, Z. |
| Abstract: | Sleeping Beauty (SB) is the most active Tc1/mariner-like transposon in vertebrate species. Each of the terminal inverted repeats (IRs) of SB contains two transposase-binding sites (DRs). This feature, termed the IR/DR structure, is conserved in a group of Tcl-like transposons. The DNA-binding region of SB transposase, similar to the paired domain of Pax proteins, consists of two helix-turn-helix subdomains (PAI + RED = PAIRED). The N-terminal PAI subdomain was found to play a dominant role in contacting the DRs. Transposase was able to bind to mutant sites retaining the 3′ part of the DRs; thus, primary DNA binding is not sufficient to determine the specificity of the transposition reaction. The PAI subdomain was also found to bind to a transpositional enhancer-like sequence within the left IR of SB, and to mediate protein-protein interactions between transposase subunits. A tetrameric form of the transposase was detected in solution, consistent with an interaction between the IR/DR structure and a transposase tetramer. We propose a model in which the transpositional enhancer and the PAI subdomain stabilize complexes formed by a transposase tetramer bound at the IR/DR. These interactions may result in enhanced stability of synaptic complexes, which might explain the efficient transposition of Sleeping Beauty in vertebrate cells. |
| Keywords: | Binding Sites, Dimerization, DNA, DNA Transposable Elements, DNA-Binding Proteins, Enhancer Elements, Hela Cells, Transposases |
| Source: | Journal of Biological Chemistry |
| ISSN: | 0021-9258 |
| Publisher: | American Society for Biochemistry and Molecular Biology |
| Volume: | 277 |
| Number: | 37 |
| Page Range: | 34581-34588 |
| Date: | 13 September 2002 |
| Official Publication: | https://doi.org/10.1074/jbc.M204001200 |
| PubMed: | View item in PubMed |
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