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. 1993 Mar 26;72(6):931-43.
doi: 10.1016/0092-8674(93)90581-a.

Tn7 transposition: target DNA recognition is mediated by multiple Tn7-encoded proteins in a purified in vitro system

R J Bainton  1 , K M Kubo, J N Feng, N L Craig
Affiliations

Tn7 transposition: target DNA recognition is mediated by multiple Tn7-encoded proteins in a purified in vitro system

R J Bainton et al. Cell. .

Abstract

We have reconstituted the transposition of the bacterial transposon Tn7 into its specific insertion site attTn7 with four purified Tn7-encoded proteins, TnsA+TnsB+TnsC+TnsD, and ATP. TnsA+TnsB+TnsC form a "core" recombination machine that recognizes the transposon ends and executes DNA breakage and joining; TnsD specifically recognizes attTn7. TnsA+TnsB+TnsC are specifically targeted to attTn7 through the TnsD-dependent interaction of TnsC, a nonspecific DNA-binding protein, with attTn7. Recombination appears to be activated by the assembly of a nucleoprotein complex containing the DNA substrates and Tns proteins. We suggest that TnsC plays a central role in communication between the transposon and the target DNA, particularly in directing insertion away from DNAs already containing a copy of Tn7.

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