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Nucleic Acids Research, 2001, Vol. 29, No. 4 1005-1011
© 2001 Oxford University Press

Arrayed transposase-binding sequences on the ends of transposon Tn5090/Tn402

Masood Kamali-Moghaddam and Lars Sundström*

Department of Pharmaceutical Biosciences, Division of Microbiology, Uppsala University, PO Box 581 BMC, S-751 23 Uppsala, Sweden

The transposon Tn5090/Tn402 encodes a 559 amino acid transposase, TniA, with a DDE motif. Gel mobility shifting and cleavage protection analysis with DNase I and hydroxyl radical probes revealed that TniA binds to multiple repeat sequences on either terminus of Tn5090/Tn402. Four of these TniA-binding 19mers occurred on the left-hand (t) end and two on the right-hand (i) end. Hydroxyl radical cleavage protection demonstrated the presence of 3–6 bp contact sequences on one face of the DNA helix. The binding pattern and organisation of repeats suggested parallels between Tn5090/Tn402 and Mu, which controls its transpositional activity in the assembly step of a higher order transpososome complex. The complex terminal structure and genes of transposase and nucleotide-binding proteins in tandem are hallmarks of the handful of Mu-like elements that are known to date.

* To whom correspondence should be addressed. Tel: +46 18 4714115; Fax: +46 18 502790; Email: lars.sundstrom{at}farmbio.uu.se


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