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 Concept Videos

Mismatch Repair01:20

Mismatch Repair

6.0K
Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...
6.0K
Mismatch Repair01:36

Mismatch Repair

43.0K
Overview
43.0K
Homologous Recombination02:31

Homologous Recombination

60.8K
The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...
60.8K
Homologous Recombination02:31

Homologous Recombination

5.7K
5.7K
Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

6.1K
DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
6.1K
Fixing Double-strand Breaks02:04

Fixing Double-strand Breaks

13.9K
The double-stranded structure of DNA has two major advantages. First, it serves as a safe repository of genetic information where one strand serves as the back-up in case the other strand is damaged. Second, the double-helical structure can be wrapped around proteins called histones to form nucleosomes, which can then be tightly wound to form chromosomes. This way, DNA chains up to 2 inches long can be contained within microscopic structures in a cell. A double-stranded break not only damages...
13.9K

You might also read

Related Articles

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

Sort by
Same author

The local mechanostructural properties of protein cargoes regulate nucleocytoplasmic transport.

Nature physics·2026
Same author

Improved method for the generation of double Holliday junction DNAs.

Analytical biochemistry·2026
Same author

A dihydrouracil CRBN ligand mitigates IMiD associated safety liabilities in heterobifunctional targeted protein degrader.

Nature communications·2026
Same author

An intrinsically disordered region mediates RNA-binding selectivity and cellular activities of LARP6.

Nature communications·2026
Same author

Integrase anchors viral RNA to the HIV-1 capsid interior.

Nature·2026
Same author

Discovery of AZD9750, an Orally Bioavailable Androgen Receptor Degrader for the Treatment of Prostate Cancer.

Journal of medicinal chemistry·2026

Related Experiment Video

Updated: Dec 4, 2025

Visualization of DNA Repair Proteins Interaction by Immunofluorescence
07:55

Visualization of DNA Repair Proteins Interaction by Immunofluorescence

Published on: June 26, 2020

10.8K

MutSβ Stimulates Holliday Junction Resolution by the SMX Complex.

Sarah J Young1, Marie Sebald1, Rajvee Shah Punatar1

  • 1The Francis Crick Institute, 1 Midland Road, London NW1 1AT, UK.

Cell Reports
|October 21, 2020
PubMed
Summary

MutSβ, a DNA repair complex, interacts with SLX4 to resolve DNA Holliday junctions, a process crucial for preventing genomic instability and diseases like Huntington's.

Keywords:
DNA recombinationDNA repairHolliday junctionMUS81-EME1SLX1-SLX4SMX trinucleasegenome stabilityresolution

More Related Videos

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein
11:01

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein

Published on: March 31, 2010

18.5K
Single-Molecule Förster Resonance Energy Transfer Methods for Real-Time Investigation of the Holliday Junction Resolution by GEN1
11:27

Single-Molecule Förster Resonance Energy Transfer Methods for Real-Time Investigation of the Holliday Junction Resolution by GEN1

Published on: September 18, 2019

9.8K

Related Experiment Videos

Last Updated: Dec 4, 2025

Visualization of DNA Repair Proteins Interaction by Immunofluorescence
07:55

Visualization of DNA Repair Proteins Interaction by Immunofluorescence

Published on: June 26, 2020

10.8K
Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein
11:01

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein

Published on: March 31, 2010

18.5K
Single-Molecule Förster Resonance Energy Transfer Methods for Real-Time Investigation of the Holliday Junction Resolution by GEN1
11:27

Single-Molecule Förster Resonance Energy Transfer Methods for Real-Time Investigation of the Holliday Junction Resolution by GEN1

Published on: September 18, 2019

9.8K

Area of Science:

  • Molecular Biology
  • Genetics
  • DNA Repair Mechanisms

Background:

  • MutSα and MutSβ are key players in DNA mismatch repair, implicated in hereditary cancers and degenerative diseases.
  • MutSβ, composed of MSH2 and MSH3, is known for its role in trinucleotide repeat expansion disorders.

Purpose of the Study:

  • To investigate the role of MutSβ in DNA repair pathways beyond mismatch repair.
  • To elucidate the interaction between MutSβ and the SLX1-SLX4-MUS81-EME1-XPF-ERCC1 (SMX) complex in resolving DNA structures.

Main Methods:

  • Co-immunoprecipitation to assess protein-protein interactions between MutSβ and SLX4.
  • In vitro assays to measure the stimulation of Holliday junction resolution by SLX1-SLX4 and SMX complexes.
  • Analysis of MSH3-depleted cells to observe effects on sister chromatid exchanges and homologous recombination ultrafine bridges (HR-UFBs).

Main Results:

  • MutSβ directly binds to SLX4, a scaffold protein for the SMX complex.
  • MutSβ stimulates the resolution of Holliday junctions (HJs) by SLX1-SLX4 and SMX, dependent on MutSβ-SLX4 interaction.
  • MutSα does not exhibit a similar stimulatory effect on HJ resolution.
  • MSH3 depletion leads to reduced sister chromatid exchanges and increased HR-UFBs during mitosis, indicating impaired processing of recombination intermediates.

Conclusions:

  • MutSβ has a novel function in promoting the resolution of DNA Holliday junctions, in addition to its known role in trinucleotide repeat instability.
  • This function of MutSβ is mediated through its interaction with SLX4 and contributes to maintaining genomic stability.
  • Defects in MutSβ's role in HJ resolution may contribute to the pathogenesis of diseases linked to DNA repair deficiencies.