Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Human Rad51 filaments on double- and single-stranded DNA: correlating regular and irregular forms with recombination

Dejan Ristic1, Mauro Modesti, Thijn van der Heijden

  • 1Department of Cell Biology and Genetics, Erasmus Medical Center PO Box 1738, 3000 DR Rotterdam, The Netherlands.

Nucleic Acids Research
|June 10, 2005
PubMed
Summary

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Devising a divisome for synthetic cells.

Nature reviews. Chemistry·2026
Same author

Topological Investigation of Protein Folding and Intrinsic Disorder.

The journal of physical chemistry. B·2026
Same author

Terminal Conjugation Enables Nanopore Sequencing of Peptides.

Journal of the American Chemical Society·2026
Same author

Two CTCF motifs impede cohesin-mediated DNA loop extrusion.

Molecular cell·2025
Same author

Modulation of Archaeal Hypernucleosome Structure and Stability by Mg<sup>2</sup>.

Journal of molecular biology·2025
Same author

Long-read nucleosome mapping of single chromatin fibers using DNA methylation and nanopore sequencing.

Biophysical journal·2025

Human recombinase Rad51 forms dynamic filaments on DNA. Regular filament structures on double-stranded DNA correlate with recombination activity, suggesting dynamic rearrangements drive strand exchange.

Area of Science:

  • Molecular Biology
  • Biophysics
  • Genetics

Background:

  • Homologous recombination is crucial for DNA repair and genetic diversity.
  • Recombinase proteins, like human Rad51, form helical filaments on DNA, acting as the catalytic core.
  • Eukaryotic recombinase activity is sensitive to reaction conditions, implying nucleotide cofactor status affects function and filament structure.

Purpose of the Study:

  • To analyze the structure and dynamics of human Rad51 nucleoprotein filaments under various conditions.
  • To investigate the relationship between filament structure, DNA substrate, and recombination activity.
  • To elucidate the role of filament dynamics in driving DNA strand exchange.

Main Methods:

  • Scanning force microscopy (SFM) to visualize Rad51 filaments on double-stranded and single-stranded DNA.

Related Experiment Videos

  • Single-molecule force spectroscopy using magnetic tweezers to study Rad51 filament assembly and disassembly kinetics.
  • Analysis of protein association and dissociation dynamics.

    • Main Results:

    • Regular Rad51 filaments on extended double-stranded DNA correlated with active in vitro recombination.
    • Filaments formed readily on single-stranded DNA but were rarely regular, indicating dynamic Rad51 monomers.
    • Single-molecule force spectroscopy revealed dynamic protein association/dissociation kinetics, distinct from RecA.

    Conclusions:

    • The dynamic rearrangements of proteins and DNA within Rad51 nucleoprotein filaments are likely key events driving strand exchange in homologous recombination.
    • Filament regularity on double-stranded DNA may stabilize DNA products, enhancing recombination efficiency.
    • Rad51 filament structure is highly dynamic, particularly on single-stranded DNA, suggesting transient regular structures are important for function.