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

Long-patch Base Excision Repair01:02

Long-patch Base Excision Repair

8.3K
Since the discovery of the two BER pathways, there has been a debate about how a cell chooses one pathway over the other and the factors determining this selection. Numerous in vitro experiments have pointed out multiple determinants for the sub-pathway selection. These are:
8.3K
Nucleotide Excision Repair01:08

Nucleotide Excision Repair

42.5K
Overview
42.5K
Nucleotide Excision Repair01:08

Nucleotide Excision Repair

14.0K
14.0K
Nucleotide Excision Repair01:38

Nucleotide Excision Repair

5.8K
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...
5.8K
Base Excision Repair01:54

Base Excision Repair

28.3K
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...
28.3K
DNA Helicases00:55

DNA Helicases

25.0K
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...
25.0K

You might also read

Related Articles

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

Sort by
Same author

Connecting fragmented aging research through the European Federation for Aging Research.

Nature aging·2026
Same author

Interactions between rare variants in DNA repair genes and cardiometabolic risk explain more variability in cognitive function.

GeroScience·2026
Same author

Control of mitochondrial dynamics by the metabolic regulator dPGC1 limits Yorkie-induced oncogenic growth in Drosophila.

PLoS biology·2025
Same author

Adapting health, economic and social policies to address population aging in China.

Nature aging·2025
Same author

The Predictive Role of C-Reactive Protein, Leukocyte Cell Count, and Soluble Urokinase Plasminogen Activator Receptor for Pulmonary Sequelae in Hospitalized COVID-19 Survivors: A Prospective Single-Center Cohort Study.

Journal of clinical medicine·2025
Same author

Deep learning reveals diverging effects of altitude on aging.

GeroScience·2025

Related Experiment Video

Updated: Apr 7, 2026

A Fluorescence-based Exonuclease Assay to Characterize DmWRNexo, Orthologue of Human Progeroid WRN Exonuclease, and Its Application to Other Nucleases
06:10

A Fluorescence-based Exonuclease Assay to Characterize DmWRNexo, Orthologue of Human Progeroid WRN Exonuclease, and Its Application to Other Nucleases

Published on: December 23, 2013

5.7K

Human exonuclease 1 (EXO1) activity characterization and its function on flap structures.

Guido Keijzers1, Vilhelm A Bohr2, Lene Juel Rasmussen1

  • 1Center for Healthy Aging, Department of Cellular and Molecular Medicine, University of Copenhagen, Denmark lenera@sund.ku.dk guido@sund.ku.dk.

Bioscience Reports
|July 17, 2015
PubMed
Summary

Human exonuclease 1 (EXO1) enzyme activity and stability are temperature-dependent. This DNA repair protein shows strong double-stranded DNA degradation and modest flap endonuclease activity, suggesting a role in strand displacement.

Keywords:
EXO1double stranded breaksflap activitystrand displacementthreadingtracking

More Related Videos

Author Spotlight: Optimizing Affinity Chromatography for His-Tagged FEN1 Protein
07:19

Author Spotlight: Optimizing Affinity Chromatography for His-Tagged FEN1 Protein

Published on: April 26, 2024

4.3K
Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair
10:59

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

Published on: May 24, 2017

10.2K

Related Experiment Videos

Last Updated: Apr 7, 2026

A Fluorescence-based Exonuclease Assay to Characterize DmWRNexo, Orthologue of Human Progeroid WRN Exonuclease, and Its Application to Other Nucleases
06:10

A Fluorescence-based Exonuclease Assay to Characterize DmWRNexo, Orthologue of Human Progeroid WRN Exonuclease, and Its Application to Other Nucleases

Published on: December 23, 2013

5.7K
Author Spotlight: Optimizing Affinity Chromatography for His-Tagged FEN1 Protein
07:19

Author Spotlight: Optimizing Affinity Chromatography for His-Tagged FEN1 Protein

Published on: April 26, 2024

4.3K
Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair
10:59

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

Published on: May 24, 2017

10.2K

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Human exonuclease 1 (EXO1) is crucial for DNA repair and replication.
  • Previous research primarily focused on yeast EXO1 functions.
  • The biochemical properties of full-length human EXO1 require detailed characterization.

Purpose of the Study:

  • To biochemically characterize full-length human EXO1.
  • To investigate factors affecting EXO1 stability and enzymatic activity.
  • To elucidate EXO1's mechanism in processing DNA flap structures.

Main Methods:

  • Purification and biochemical assays of full-length human EXO1.
  • Thermodynamic stability studies under varying temperatures.
  • Enzymatic activity assays using diverse DNA flap substrates.

Main Results:

  • EXO1's enzymatic activity and DNA binding stability are modulated by temperature.
  • EXO1 exhibits robust double-stranded DNA degradation capabilities.
  • EXO1 demonstrates modest endonuclease and 5' flap activities.
  • EXO1 preferentially cleaves DNA one nucleotide into the double-stranded region of flap substrates.

Conclusions:

  • Human EXO1's function is influenced by temperature.
  • EXO1 possesses significant DNA degradation and flap processing abilities.
  • The cleavage pattern suggests a potential role for EXO1 in strand displacement during DNA metabolism.