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Related Experiment Videos

Pulling apart catalytically active Tn5 synaptic complexes using magnetic tweezers.

Christian D Adams1, Bernhard Schnurr, John F Marko

  • 1Department of Biochemistry, University of Wisconsin at Madison, WI 53706, USA.

Journal of Molecular Biology
|January 30, 2007
PubMed
Summary

The Tn5 transposase protein binds DNA and forms loops, but its DNA cleavage activity is highly sequence-specific. This finding impacts understanding of how transposition is regulated in cells.

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • DNA transposition is a fundamental genetic mobility mechanism.
  • Transposase proteins mediate the movement of DNA sequences (transposons).
  • The Tn5 transposase system is a well-studied model for transposition.

Purpose of the Study:

  • To investigate the sequence-specificity of DNA binding and looping by the Tn5 transposase.
  • To determine the energy barriers involved in Tn5 transposase-DNA complex disassembly.
  • To understand how sequence-sensitivity relates to catalytic activity in transposition.

Main Methods:

  • Single-DNA micromanipulation experiments were employed.
  • The energy barrier for disassembling catalytically active synaptic complexes was measured.

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  • DNA looping and binding by Tn5 transposase at various DNA sequences were analyzed.

    • Main Results:

    • The energy barrier to disassemble active Tn5 synaptic complexes is 16 kcal mol(-1).
    • DNA looping by Tn5 transposase is less sequence-dependent than previously assumed.
    • Non-transposon end sequences can form stable loops (14 kcal mol(-1) barrier) but do not lead to DNA cleavage.

    Conclusions:

    • Tn5 transposase exhibits lower sequence-sensitivity for DNA binding and looping compared to DNA cleavage.
    • These findings suggest mechanisms for in vivo regulation of transposition.
    • The results provide insights into the cis-transposition bias of Tn5 transposase.