Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

Restarting Stalled Replication Forks

Restarting Stalled Replication Forks

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,...

Single-Strand DNA Binding Proteins

Single-Strand DNA Binding Proteins

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...

DNA Damage can Stall the Cell Cycle

DNA Damage can Stall the Cell Cycle

In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...

Bacterial RNA Polymerase

Bacterial RNA Polymerase

Unlike eukaryotes, bacteria use a single RNA Polymerase (RNAP) to transcribe all genes. The different subunits of bacterial RNAPhave distinct functions. The multisubunit structure of the bacterial RNAP helps the enzyme to maintain catalytic function, facilitate assembly, interact with DNA and RNA, and self-regulate its activity.
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...

NF-κB-dependent Signaling Pathway

NF-κB-dependent Signaling Pathway

The transcription factor NF-κB was discovered in 1986 in the lab of Nobel laureate Professor David Baltimore, for its interaction with the immunoglobulin light chain enhancer in B-cells. After more than three decades of study, it is now evident that NF-κB regulates the expression of over 100 genes. Most of these genes play an essential role in the innate and adaptive immune responses as well as the inflammatory responses of animals.
NF-κB-dependent Signaling Mechanism
The...

Homologous Recombination

Homologous Recombination

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...

You might also read

Related Articles

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

Sort by

Same author

A unique poikilodermatous condition associated with a de novo heterozygous ATR missense variant.

Clinical and experimental dermatology·2026

Same author

Topological stress regulates replication fork dynamics in unperturbed S phase.

Nature communications·2026

Same author

Recessive loss of DIAPH1 function causes a progressive neurodevelopmental syndrome with variable immunological involvement.

Genetics in medicine : official journal of the American College of Medical Genetics·2026

Same author

CD73 restrains mutant β-catenin oncogenic activity in endometrial carcinomas.

JCI insight·2026

Same author

Differential roles of Rad18 in repressing carcinogen- and oncogene-driven mutagenesis <i>in vivo</i>.

NAR cancer·2026

Same author

REV7 associates with ATRIP and inhibits ATR kinase activity.

Nucleic acids research·2026

Same journal

Correction to 'scSuperAnnotator: A platform for benchmarking comparison and visualizing automated cellular annotation methods for scRNA-seq data'.

Nucleic acids research·2026

Same journal

Correction to 'Differentiable partition function calculation for RNA'.

Nucleic acids research·2026

Same journal

Deployment of non-canonical splicing in tunicate genomes is mediated by divergent U2AF function and changing m6A modification in U1 and U6 snRNA.

Nucleic acids research·2026

Same journal

Bacillus subtilis DnaB forms multiple protein-protein interactions essential for DNA replication initiation.

Nucleic acids research·2026

Same journal

Multiple forms of protein-protein and DNA binding are exhibited by BrxC from the BREX phage restriction system.

Nucleic acids research·2026

Same journal

Biosynthesis of glycosylated 5-hydroxycytosine in the DNA of diverse viruses.

Nucleic acids research·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 9, 2025

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry

Published on: January 17, 2025

PCNA-binding activity separates RNF168 functions in DNA replication and DNA double-stranded break signaling.

Yang Yang¹, Deepika Jayaprakash^1,2, Satpal S Jhujh³

¹Department of Pathology and Laboratory Medicine, University of North Carolina at Chapel Hill, 614 Brinkhous-Bullitt Building, 160 Medical Drive, Chapel Hill, NC 27599, USA.

Nucleic Acids Research

|October 24, 2024

Summary

This summary is machine-generated.

RNF168 protein plays a dual role in DNA repair and replication. Researchers found a new mechanism where RNF168 supports DNA replication independently of its DNA damage response functions.

More Related Videos

Visualization of DNA Repair Proteins Interaction by Immunofluorescence

Visualization of DNA Repair Proteins Interaction by Immunofluorescence

Published on: June 26, 2020

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids

Published on: September 21, 2017

Related Experiment Videos

Last Updated: Jun 9, 2025

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry

Published on: January 17, 2025

Visualization of DNA Repair Proteins Interaction by Immunofluorescence

Visualization of DNA Repair Proteins Interaction by Immunofluorescence

Published on: June 26, 2020

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids

Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids

Published on: September 21, 2017

Area of Science:

Molecular Biology
DNA Replication
DNA Damage Response

Background:

RNF168 is known for its role in DNA double-strand break (DSB) repair by recruiting factors like 53BP1.
Its involvement in DNA replication fork progression is suggested but not fully understood.

Purpose of the Study:

To elucidate the precise role of RNF168 in DNA replication.
To investigate the mechanism of RNF168 recruitment to replication factories.
To determine if RNF168's functions in replication and DSB signaling are linked.

Main Methods:

Investigated RNF168 recruitment to replication factories independently of ATM/RNF8.
Identified a degenerate PCNA-interacting peptide (DPIP) motif and MIU domain in RNF168.
Utilized an RNF168 mutant (ΔDPIP/ΔMIU1) deficient in PCNA interaction.
Assessed the mutant's ability to support DNA replication and rescue 53BP1 foci formation in RNF168-/- cells.

Main Results:

RNF168 is recruited to replication factories via interaction with mono-ubiquitylated PCNA through its DPIP motif and MIU domain.
RNF168 recruitment to replication factories is independent of the canonical DSB response pathway.
The RNF168 ΔDPIP/ΔMIU1 mutant fails to support DNA replication but fully rescues DSB-induced 53BP1 foci formation.
RNF168's functions in DNA replication and DSB signaling are separable.

Conclusions:

RNF168 promotes DNA replication through a novel mechanism involving PCNA interaction.
This replication function is distinct from its established role in DNA double-strand break signaling.
The study defines separable functions for RNF168 in maintaining genome stability during replication and repair.