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

The Replisome03:01

The Replisome

DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with the...
The Replisome03:01

The Replisome

DNA replication is carried out by a large complex of proteins that act in a coordinated matter to achieve high-fidelity DNA replication. Together this complex is known as the DNA replication machinery or the replisome.
The synthesis of the leading and lagging strands is a highly coordinated process. To explain this, the “Trombone model” was proposed by Bruce Alberts in 1980. The DNA loop formation starts when a primer is synthesized on the parent lagging strand. The loop grows with the...
Restarting Stalled Replication Forks02:37

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, a...
The DNA Replication Fork01:02

The DNA Replication Fork

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 forks, one in...
The DNA Replication Fork01:02

The DNA Replication Fork

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 forks, one in...
Homologous Recombination02:31

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

Orchestrated metal ion repositioning defines the dynamic catalytic strategy of the essential DNA repair nuclease APE1.

bioRxiv : the preprint server for biology·2026
Same author

Subsets of adjacent nodes (SOAN): A fast method for computing suboptimal paths in protein dynamic networks.

Molecular physics·2026
Same author

Ranking exercise interventions by their effectiveness in the management of polycystic ovary syndrome: a systematic review and network meta-analysis.

Reproductive biology and endocrinology : RB&E·2026
Same author

Mitochondrial genome assembly, comparative analysis of two caprifoliaceae species, and insights into adaptive evolution.

BMC plant biology·2026
Same author

The interaction of XPG with TFIIH through p62 and XPD is required for the completion of nucleotide excision repair.

Nucleic acids research·2026
Same author

Successful Re-Pigmentation of IPL-Induced Hypopigmentation Using Topical Bimatoprost.

Journal of cosmetic dermatology·2025
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

Related Experiment Video

Updated: May 15, 2026

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry
08:07

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry

Published on: January 17, 2025

A new structural framework for integrating replication protein A into DNA processing machinery.

Chris A Brosey1, Chunli Yan, Susan E Tsutakawa

  • 1Department of Biochemistry, Center for Structural Biology, Vanderbilt University, Nashville, TN 37232, USA.

Nucleic Acids Research
|January 11, 2013
PubMed
Summary
This summary is machine-generated.

Replication protein A (RPA) compacts and becomes less dynamic when binding single-stranded DNA (ssDNA). This study reveals RPA undergoes two binding transitions, not three, challenging previous models of DNA processing.

More Related Videos

Strand-Specific Analysis of Proteins at Replicating DNA Strands by Enrichment and Sequencing of Protein-Associated Nascent DNA Method
08:53

Strand-Specific Analysis of Proteins at Replicating DNA Strands by Enrichment and Sequencing of Protein-Associated Nascent DNA Method

Published on: May 2, 2025

Imaging Replicative Domains in Ultrastructurally Preserved Chromatin by Electron Tomography
14:56

Imaging Replicative Domains in Ultrastructurally Preserved Chromatin by Electron Tomography

Published on: May 20, 2022

Related Experiment Videos

Last Updated: May 15, 2026

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry
08:07

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry

Published on: January 17, 2025

Strand-Specific Analysis of Proteins at Replicating DNA Strands by Enrichment and Sequencing of Protein-Associated Nascent DNA Method
08:53

Strand-Specific Analysis of Proteins at Replicating DNA Strands by Enrichment and Sequencing of Protein-Associated Nascent DNA Method

Published on: May 2, 2025

Imaging Replicative Domains in Ultrastructurally Preserved Chromatin by Electron Tomography
14:56

Imaging Replicative Domains in Ultrastructurally Preserved Chromatin by Electron Tomography

Published on: May 20, 2022

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Replication protein A (RPA) is crucial for DNA processing, protecting single-stranded DNA (ssDNA) and recruiting other factors.
  • The coordination of RPA's eight domains during DNA binding and processing remains poorly understood.

Purpose of the Study:

  • To investigate the structural dynamics and DNA-binding mechanism of RPA's core domains.
  • To elucidate how RPA's architecture changes upon binding to ssDNA.

Main Methods:

  • Small-angle X-ray scattering (SAXS) and small-angle neutron scattering (SANS).
  • All-atom molecular dynamics (MD) simulations.
  • Integration of scattering data with MD simulations to model RPA structure and dynamics.

Main Results:

  • DNA binding induces compaction in RPA, transitioning from a mobile, multi-state ensemble to a more condensed, less dynamic structure.
  • RPA binding to ssDNA involves two distinct transitions, contradicting models that propose a three-stage process with a discrete intermediate.
  • The study provides a revised framework for RPA's interaction with ssDNA.

Conclusions:

  • RPA's structural flexibility is key to its function in DNA processing.
  • The findings offer a new perspective on RPA's role in coordinating DNA repair and replication pathways.
  • Understanding RPA's dynamic behavior is essential for comprehending DNA maintenance mechanisms.