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Significance DNA transposons move by excision and reintegration mediated by the element-encoded transposase. Unlike most transposases, the transposonTn7 transposase is heteromeric, containing TnsB protein, which recognizes the transposon ends and mediates 3′ end breakage and joining, and TnsA protein, which mediates 5′ end breakage. We show that TnsA and TnsB interact and that TnsA can stimulate two key TnsB activities, end binding and end pairing. We also show that an end-pairing deficiency underlies the inability of aTn7 containing two left ends to transpose. These findings reveal new aspects of protein–protein and protein–DNA interactions that underlieTn7 transposition.

Direct interaction between the TnsA and TnsB subunits controls the heteromeric Tn7 transposase