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Molecular and Cellular Biology, September 2004, p. 8301-8311, Vol. 24, No. 18
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.18.8301-8311.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Early Intermediates of mariner Transposition: Catalysis without Synapsis of the Transposon Ends Suggests a Novel Architecture of the Synaptic Complex

Karen Lipkow ,^1,, Nicolas Buisine,^1, David J. Lampe,² and Ronald Chalmers^1*

Department of Biochemistry, University of Oxford, Oxford, United Kingdom,¹ Department of Biological Sciences, Duquesne University, Pittsburgh, Pennsylvania²

Received 2 February 2004/ Returned for modification 3 March 2004/ Accepted 9 June 2004

The mariner family is probably the most widely distributed family of transposons in nature. Although these transposons are related to the well-studied bacterial insertion elements, there is evidence for major differences in their reaction mechanisms. We report the identification and characterization of complexes that contain the Himar1 transposase bound to a single transposon end. Titrations and mixing experiments with the native transposase and transposase fusions suggested that they contain different numbers of transposase monomers. However, the DNA protection footprints of the two most abundant single-end complexes are identical. This indicates that some transposase monomers may be bound to the transposon end solely by protein-protein interactions. This would mean that the Himar1 transposase can dimerize independently of the second transposon end and that the architecture of the synaptic complex has more in common with V(D)J recombination than with bacterial insertion elements. Like V(D)J recombination and in contrast to the case for bacterial elements, Himar1 catalysis does not appear to depend on synapsis of the transposon ends, and the single-end complexes are active for nicking and probably for cleavage. We discuss the role of this single-end activity in generating the mutations that inactivate the vast majority of mariner elements in eukaryotes.

K.L. and N.B. contributed equally to this work.

Present address: Department of Anatomy, University of Cambridge, Cambridge CB2 3DY, United Kingdom.

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