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The bacterial transposon  Tn7  is distinguished by its ability to recognize a specific site called  attTn7 , and insert just downstream of the highly conserved chromosomal  glmS  gene. TnsD is one of four transposon-encoded polypeptides (TnsABC+D) required for site-specific insertion of Tn 7  into  attTn7 , and is the target site-selector that binds to a highly conserved sequence in the end of the  glmS  protein coding region. In this study, we identified important nucleotides within this region that are crucial for TnsD- attTn7  interaction. We also probed the regions of TnsD that interact with  attTn7  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  attTn7 ; TnsC also interacts with and controls both the TnsA and TnsB subunits of the Tn7 transposase. TnsC stimulates the binding of TnsD to  attTn7 in vivo , 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.

Characterization of the TnsD-attTn7 complex that promotes site-specific insertion of Tn7