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  11. Asymmetric Loading Of Tnse Regulates Tn7 Targeting Of Dna Replication Structures

Asymmetric loading of TnsE regulates Tn7 targeting of DNA replication structures

Shreya S Krishnan1,2, Yao Shen1,2, Treasa B O'Hagan1,2

  • 1Department of Biochemistry, McGill University, Montreal, QC H3G 0B1, Canada.

Nucleic Acids Research
|June 11, 2025

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View abstract on PubMed

Summary
This summary is machine-generated.

The Tn7 transposable element uses the TnsE protein to identify DNA replication sites for insertion. This study reveals how TnsE forms specific complexes with DNA, guiding transposition for genetic element spread.

Area of Science:

  • Molecular Biology
  • Genetics
  • Structural Biology

Background:

  • Tn7 transposable elements exhibit complex target selection for insertion.
  • The mechanism for Tn7 targeting DNA replication sites is poorly understood, unlike the well-studied chromosomal attTn7 site.

Purpose of the Study:

  • To elucidate the mechanism by which the Tn7-encoded protein TnsE recognizes DNA replication sites.
  • To understand the structural basis of TnsE-DNA interactions.

Main Methods:

  • Integrative structural biology approach.
  • Native mass spectrometry to analyze TnsE:DNA complexes.
  • Structural characterization of TnsE-DNA interactions.

Main Results:

  • TnsE forms 1:1 and 2:1 complexes with 3'-recessed DNA.

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  • Gain-of-function TnsE variants show a preference for 2:1 complexes.
  • The C-terminal domain of TnsE binds DNA duplex, while the N-terminal domain dictates substrate specificity and recruits transposition machinery.

    • Conclusions:

    • TnsE-mediated target selection involves asymmetric TnsE:DNA complex formation.
    • This complex formation is crucial for recruiting the Tn7 transposase to DNA replication structures.