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

5.9K
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...
5.9K
Mismatch Repair01:36

Mismatch Repair

42.9K
Overview
42.9K
Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

16.1K
For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
16.1K
DNA Helicases00:55

DNA Helicases

23.3K
DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
23.3K
Homologous Recombination02:31

Homologous Recombination

60.0K
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...
60.0K
The DNA Replication Fork01:02

The DNA Replication Fork

39.2K
An organism’s genome needs to be duplicated in an efficient and error-free manner for its growth and survival. The replication fork is a Y-shaped active region where two strands of DNA are separated and replicated continuously. The coupling of DNA unzipping and complementary strand synthesis is a characteristic feature of a replication fork.   Organisms with small circular DNA, such as E. coli, often have a single origin of replication; therefore, they have only two replication...
39.2K

You might also read

Related Articles

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

Sort by
Same author

DHX36 is a regulatory switch in the interferon-mediated antiviral response.

Science advances·2026
Same author

The Zuo1 C-terminal domain stabilizes DNA guanosine quadruplex (G4) structures located on Chromosome IX in Saccharomyces cerevisiae.

Nucleic acids research·2025
Same author

Poly (ADP-ribose) polymerase in yeasts: characterization and involvement in telomere maintenance.

Nucleic acids research·2025
Same author

The Shu complex interacts with the replicative helicase to prevent mutations and aberrant recombination.

The EMBO journal·2025
Same author

Viral hijacking of hnRNPH1 unveils a G-quadruplex-driven mechanism of stress control.

Cell host & microbe·2024
Same author

In-gel staining methods of G4 DNA and RNA structures.

Methods in enzymology·2024

Related Experiment Video

Updated: Nov 28, 2025

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
05:37

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

Published on: April 4, 2025

1.0K

Mgs1 function at G-quadruplex structures during DNA replication.

Katrin Paeschke1, Peter Burkovics2

  • 1Department of Oncology, Hematology and Rheumatology, University Hospital Bonn, Bonn, Germany. kpaeschk@uni-bonn.de.

Current Genetics
|November 25, 2020
PubMed
Summary

Mgs1 protein aids DNA replication at difficult G-quadruplex (G4) DNA sites. Its binding, partly reliant on Pif1 helicase, is crucial for preventing genomic instability and chromosomal rearrangements.

Keywords:
G-quadruplexGenome stabilityMgs1Replication

More Related Videos

Author Spotlight: Characterizing DNA G-Quadruplex by Bis-3-Chloropiperidine Based Chemical Mapping
05:32

Author Spotlight: Characterizing DNA G-Quadruplex by Bis-3-Chloropiperidine Based Chemical Mapping

Published on: May 12, 2023

1.6K
Tools to Study the Role of Architectural Protein HMGB1 in the Processing of Helix Distorting, Site-specific DNA Interstrand Crosslinks
12:19

Tools to Study the Role of Architectural Protein HMGB1 in the Processing of Helix Distorting, Site-specific DNA Interstrand Crosslinks

Published on: November 10, 2016

8.5K

Related Experiment Videos

Last Updated: Nov 28, 2025

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
05:37

Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes

Published on: April 4, 2025

1.0K
Author Spotlight: Characterizing DNA G-Quadruplex by Bis-3-Chloropiperidine Based Chemical Mapping
05:32

Author Spotlight: Characterizing DNA G-Quadruplex by Bis-3-Chloropiperidine Based Chemical Mapping

Published on: May 12, 2023

1.6K
Tools to Study the Role of Architectural Protein HMGB1 in the Processing of Helix Distorting, Site-specific DNA Interstrand Crosslinks
12:19

Tools to Study the Role of Architectural Protein HMGB1 in the Processing of Helix Distorting, Site-specific DNA Interstrand Crosslinks

Published on: November 10, 2016

8.5K

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • DNA replication encounters challenges at difficult genomic sites, including G-quadruplex (G4) DNA structures.
  • G4 structures are stable DNA secondary structures implicated in gene regulation and telomere maintenance.
  • Replication fork progression can be hindered by G4s, leading to genomic instability such as deletions, mutations, and recombination.

Purpose of the Study:

  • To investigate the role of Mgs1 protein in DNA replication at G4-forming regions.
  • To understand the interaction between Mgs1, Pif1 helicase, and G4 structures during replication.
  • To elucidate the contribution of Mgs1 to maintaining genome stability.

Main Methods:

  • In vitro binding assays to assess Mgs1's affinity for G4 DNA.
  • Chromosomal analysis to determine Mgs1 association with G4 regions in vivo.
  • Analysis of gross chromosomal rearrangement (GCR) rates in yeast strains with deletions in Mgs1 and Pif1.

Main Results:

  • Mgs1 preferentially binds to G4 DNA structures in vitro.
  • Mgs1 is found in vivo at chromosomal regions predicted to form G4 structures.
  • Mgs1 binding to G4 motifs in vivo is partially dependent on the Pif1 helicase.
  • Deletion of Mgs1 leads to elevated GCR rates, similar to the effect of Pif1 deletion.

Conclusions:

  • Mgs1 plays a significant role in supporting DNA replication at G4-forming regions.
  • The findings suggest a functional interplay between Mgs1 and Pif1 in managing G4 structures during replication.
  • Mgs1 is essential for preventing gross chromosomal rearrangements, thereby contributing to genome stability.