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

Nucleotide Excision Repair

Nucleotide Excision Repair

Nucleotide Excision Repair

Nucleotide Excision Repair

DNA Distortion and Damage
Cells are regularly exposed to mutagens—factors in the environment that can damage DNA and generate mutations. UV radiation is one of the most common mutagens and is estimated to introduce a significant number of changes in DNA. These include bends or kinks in the structure, which can block DNA replication or transcription. If these errors are not fixed, the damage can cause mutations, which in turn can result in cancer or disease depending on which sequences are...

Nucleotide Excision Repair

Nucleotide Excision Repair

Base Excision Repair

Base Excision Repair

One of the common DNA damages is the chemical alteration of single bases by alkylation, oxidation, or deamination. The altered bases cause mispairing and strand breakage during replication. This type of damage causes minimal change to the DNA double helix structure and can be repaired by the base excision repair (BER) pathways. BER corrects damaged DNA sequences by removing the damaged base and restoring the original base sequence using the complementary strand as a template.
The first step of...

Base Excision Repair

Base Excision Repair

One of the common DNA damages is the chemical alteration of single bases by alkylation, oxidation, or deamination. The altered bases cause mispairing and strand breakage during replication. This type of damage causes minimal change to the DNA double helix structure and can be repaired by the base excision repair (BER) pathways. BER corrects damaged DNA sequences by removing the damaged base and restoring the original base sequence using the complementary strand as a template.
The first step of...

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

Comparative evaluation of stability, efficacy, and sterility in five repackaged intravitreal anti-vascular endothelial growth factor medications.

Scientific reports·2026

Same author

Distinct quaternary states, intermediates, and autoinhibition during loading of the DnaB-replicative helicase by the phage λP helicase loader.

Nucleic acids research·2025

Same author

Wss1 and Ddi1 DNA-Protein crosslink repair proteases protect Saccharomyces cerevisiae and Candida albicans against oxidative stress.

Scientific reports·2025

Same author

DnaB and DciA: mechanisms of helicase loading and translocation on ssDNA.

Nucleic acids research·2025

Same author

Distinct Quaternary States, Intermediates, and Autoinhibition During Loading of the DnaB-Replicative Helicase by the Phage λP Helicase Loader.

bioRxiv : the preprint server for biology·2025

Same author

A disordered linker in the Polycomb protein Polyhomeotic tunes phase separation and oligomerization.

Molecular cell·2025

Search research articles

Related Experiment Video

Updated: Jun 24, 2026

Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair

Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair

Published on: May 24, 2017

A structural model for the damage-sensing complex in bacterial nucleotide excision repair.

Danaya Pakotiprapha¹, Yi Liu, Gregory L Verdine

¹Department of Molecular and Cellular Biology, Harvard University, Cambridge, MA 02138, USA.

The Journal of Biological Chemistry

|March 17, 2009

Summary

Bacterial DNA repair uses the UvrA.UvrB complex to detect diverse DNA damage. Researchers determined the structure of this complex, revealing its damage-sensing mechanism.

More Related Videos

Visualizing and Quantifying Endonuclease-Based Site-Specific DNA Damage

Visualizing and Quantifying Endonuclease-Based Site-Specific DNA Damage

Published on: August 21, 2021

Related Experiment Videos

Last Updated: Jun 24, 2026

Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair

Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair

Published on: May 24, 2017

Visualizing and Quantifying Endonuclease-Based Site-Specific DNA Damage

Visualizing and Quantifying Endonuclease-Based Site-Specific DNA Damage

Published on: August 21, 2021

Area of Science:

Molecular biology
Biochemistry
Structural biology

Background:

Nucleotide excision repair (NER) is a crucial DNA repair pathway.
NER can fix a wide variety of DNA lesions.
In bacteria, the UvrA.UvrB complex initiates DNA damage recognition.

Purpose of the Study:

To determine the structure of the UvrA and UvrB interaction domains.
To understand how these domains facilitate the formation of the DNA damage-sensing complex.

Main Methods:

X-ray crystallography to obtain the complex structure.
Biochemical analyses to confirm functional interactions.

Main Results:

The crystal structure of the UvrA and UvrB interaction domains was determined.
These domains are essential and sufficient for UvrA and UvrB association.
A model for the complete DNA damage-sensing complex was proposed.

Conclusions:

The UvrA.UvrB interaction domains are key to forming the bacterial NER damage-sensing complex.
Structural insights provide a foundation for understanding NER mechanisms.