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Related Experiment Videos

Torque-limited RecA polymerization on dsDNA.

Thijn van der Heijden1, John van Noort, Hendrikje van Leest

  • 1Kavli Institute of Nanoscience, Delft University of Technology Lorentzweg 1, 2628 CJ Delft, The Netherlands.

Nucleic Acids Research
|April 13, 2005
PubMed
Summary
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RecA protein assembly on DNA is stalled by DNA bending and twisting. Releasing DNA tension allows full RecA filament formation, revealing insights into DNA repair mechanisms.

Area of Science:

  • Molecular Biology
  • Biophysics
  • Biochemistry

Background:

  • RecA protein is crucial for DNA repair and recombination.
  • Understanding RecA-DNA interactions under force is key to cellular processes.

Purpose of the Study:

  • To investigate RecA filament assembly on torsionally constrained DNA in real-time.
  • To determine the effect of stretching force on RecA-DNA assembly dynamics.

Main Methods:

  • Utilized magnetic tweezers to apply controlled stretching forces to DNA.
  • Monitored RecA-DNA filament formation in real-time.

Main Results:

  • RecA assembly stalled due to plectoneme formation at forces up to 3.6 pN.
  • Higher forces (>3.6 pN) stalled assembly due to induced DNA twist, with a maximum torsion of 10.1 ± 0.7 k(b)T.

Related Experiment Videos

  • DNA rotation released plectonemes, enabling complete RecA coverage.

    • Conclusions:

    • RecA assembly dynamics are force-dependent, influenced by DNA supercoiling and plectoneme formation.
    • The built-up torsion during RecA filamentation may play roles in replication fork regression and DNA decondensation in vivo.