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Nucleic Acids Research 2005 33(6):1982-1992; doi:10.1093/nar/gki348
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Published online 6 April 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

Cyclic changes in the affinity of protein–DNA interactions drive the progression and regulate the outcome of the Tn10 transposition reaction

Danxu Liu, Paul Crellin and Ronald Chalmers*

Department of Biochemistry, University of Oxford South Parks Road, Oxford OX1 3QU, UK

*To whom correspondence should be addressed. Tel: +44 01865 275307; Fax: +44 01865 275297; Email: rqh12{at}yahoo.co.uk

Received February 22, 2005. Revised March 21, 2005. Accepted March 21, 2005.

The Tn10 transpososome is a DNA processing machine in which two transposon ends, a transposase dimer and the host protein integration host factor (IHF), are united in an asymmetrical complex. The transitions that occur during one transposition cycle are not limited to chemical cleavage events at the transposon ends, but also involve a reorganization of the protein and DNA components. Here, we demonstrate multiple pathways for Tn10 transposition. We show that one series of events is favored over all others and involves cyclic changes in the affinity of IHF for its binding site. During transpososome assembly, IHF is bound with high affinity. However, the affinity for IHF drops dramatically after cleavage of the first transposon end, leading to IHF ejection and unfolding of the complex. The ejection of IHF promotes cleavage of the second end, which is followed by restoration of the high affinity state which in turn regulates target interactions.


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