| Summary: | <p>Abstract</p> <p>The bacterial transposon <it>Tn7 </it>is distinguished by its ability to recognize a specific site called <it>attTn7</it>, and insert just downstream of the highly conserved chromosomal <it>glmS </it>gene. TnsD is one of four transposon-encoded polypeptides (TnsABC+D) required for site-specific insertion of Tn<it>7 </it>into <it>attTn7</it>, and is the target site-selector that binds to a highly conserved sequence in the end of the <it>glmS </it>protein coding region. In this study, we identified important nucleotides within this region that are crucial for TnsD-<it>attTn7 </it>interaction. We also probed the regions of TnsD that interact with <it>attTn7 </it>and found that there are important DNA-binding determinants throughout the entire length of the protein, including an amino-terminal CCCH zinc-finger motif. A key role of TnsD is to recruit the non-sequence specific DNA-binding protein TnsC to <it>attTn7</it>; TnsC also interacts with and controls both the TnsA and TnsB subunits of the Tn7 transposase. TnsC stimulates the binding of TnsD to <it>attTn7 in vivo</it>, and TnsCD and TnsD can also interact in the absence of DNA and localize their interaction domains to the N-terminal region of each protein.</p>
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