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 Dmc1 protein binds DNA as an octameric ring.

S I Passy1, X Yu, Z Li

  • 1Department of Biology, Rensselaer Polytechnic Institute, 425 Jordan Road, Troy, NY 12180, USA.

Proceedings of the National Academy of Sciences of the United States of America
|September 15, 1999
PubMed
Summary
This summary is machine-generated.

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

Decadal biodiversity trends in rivers reveal recent community rearrangements.

The Science of the total environment·2022
Same author

Practice variation in the diagnosis of acute rejection among pediatric heart transplant centers: An analysis of the pediatric heart transplant society (PHTS) registry.

The Journal of heart and lung transplantation : the official publication of the International Society for Heart Transplantation·2021
Same author

Cost-effectiveness of pediatric heart transplantation across a positive crossmatch for high waitlist urgency candidates.

American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons·2015
Same author

Structural plasticity of helical nanotubes based on coiled-coil assemblies.

Structure (London, England : 1993)·2015
Same author

Practical design and performance of the stressed-lap polishing tool.

Applied optics·2010
Same author

Optical metrology for two large highly aspheric telescope mirrors.

Applied optics·2010

Human Dmc1 (hDmc1) forms octameric rings, unlike bacterial RecA. This meiosis-specific recombinase binds DNA within its ring structure, suggesting a conserved functional mechanism in genetic recombination.

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • The bacterial RecA protein is central to homologous genetic recombination and shares structural similarities with F1-ATPase and helicases.
  • RecA forms a hexameric ring structure, a motif also observed in F1-ATPases and ring helicases.

Purpose of the Study:

  • To investigate the structural and functional characteristics of the human meiosis-specific recombinase, hDmc1.
  • To compare the oligomeric state and DNA-binding properties of hDmc1 with its bacterial homolog, RecA.

Main Methods:

  • Structural analysis of human Dmc1 (hDmc1) protein.
  • DNA-binding assays to determine the active conformation of hDmc1.

Main Results:

  • Human Dmc1 (hDmc1) forms octameric rings, distinct from the hexameric rings of RecA.

Related Experiment Videos

  • Unlike RecA and Rad51, hDmc1 does not form helical filaments.
  • The hDmc1 ring structure binds DNA in its central channel, indicating this is likely the active conformation.

    • Conclusions:

    • The RecA-like ring structure is conserved from bacteria to humans.
    • Some RecA homologs, like hDmc1, may function exclusively as rings, while others can form both rings and filaments.