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

Mismatch Repair

Mismatch Repair

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...

Mismatch Repair

Mismatch Repair

Mismatch Repair

Mismatch Repair

Fixing Double-strand Breaks

Fixing Double-strand Breaks

The double-stranded structure of DNA has two major advantages. First, it serves as a safe repository of genetic information where one strand serves as the back-up in case the other strand is damaged. Second, the double-helical structure can be wrapped around proteins called histones to form nucleosomes, which can then be tightly wound to form chromosomes. This way, DNA chains up to 2 inches long can be contained within microscopic structures in a cell. A double-stranded break not only damages...

Fixing Double-strand Breaks

Fixing Double-strand Breaks

The double-stranded structure of DNA has two major advantages. First, it serves as a safe repository of genetic information where one strand serves as the back-up in case the other strand is damaged. Second, the double-helical structure can be wrapped around proteins called histones to form nucleosomes, which can then be tightly wound to form chromosomes. This way, DNA chains up to 2 inches long can be contained within microscopic structures in a cell. A double-stranded break not only damages...

Long-patch Base Excision Repair

Long-patch Base Excision Repair

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:

You might also read

Related Articles

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

Sort by

Same author

Perceptions of Professional Responsibility When Caring for Older People in Home Care in Sweden.

Journal of community health nursing·2020

Same author

Anatomy and resilience of the global production ecosystem.

Nature·2019

Same author

Immune-regulatory genes as possible modifiers of familial pityriasis rubra pilaris - lessons from a family with PRP and psoriasis.

Journal of the European Academy of Dermatology and Venereology : JEADV·2018

Same author

A novel TRPS1 mutation in a Moroccan family with Tricho-rhino-phalangeal syndrome type III: case report.

BMC medical genetics·2017

Same author

Exome sequencing identifies mutations in KIF14 as a novel cause of an autosomal recessive lethal fetal ciliopathy phenotype.

Clinical genetics·2013

Same author

Cytomegalovirus seropositivity is negatively associated with multiple sclerosis.

Multiple sclerosis (Houndmills, Basingstoke, England)·2013

Search research articles

Related Experiment Video

Updated: Jun 16, 2026

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein

Published on: March 31, 2010

MutSbeta exceeds MutSalpha in dinucleotide loop repair.

J Kantelinen¹, M Kansikas, M K Korhonen

¹Department of Biological and Environmental Sciences, University of Helsinki, Viikinkaari 5, Helsinki, Finland.

British Journal of Cancer

|February 18, 2010

Summary

MutSalpha and MutSbeta exhibit functional redundancy in DNA repair, particularly for insertion/deletion loops. MutSbeta plays a key role in repairing specific DNA repeats, offering clinical insights into MSH3 deficiency in tumors.

More Related Videos

Proofreading and DNA Repair Assay Using Single Nucleotide Extension and MALDI-TOF Mass Spectrometry Analysis

Proofreading and DNA Repair Assay Using Single Nucleotide Extension and MALDI-TOF Mass Spectrometry Analysis

Published on: June 19, 2018

The Lambda Select cII Mutation Detection System

The Lambda Select cII Mutation Detection System

Published on: April 26, 2018

Related Experiment Videos

Last Updated: Jun 16, 2026

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein

Application of Stopped-flow Kinetics Methods to Investigate the Mechanism of Action of a DNA Repair Protein

Published on: March 31, 2010

Proofreading and DNA Repair Assay Using Single Nucleotide Extension and MALDI-TOF Mass Spectrometry Analysis

Proofreading and DNA Repair Assay Using Single Nucleotide Extension and MALDI-TOF Mass Spectrometry Analysis

Published on: June 19, 2018

The Lambda Select cII Mutation Detection System

The Lambda Select cII Mutation Detection System

Published on: April 26, 2018

Area of Science:

Molecular Biology
Genetics
Cancer Research

Background:

MutSalpha (MSH2+MSH6) and MutSbeta (MSH2+MSH3) are key DNA mismatch repair factors.
Their functional redundancy and clinical significance in mismatch repair (MMR)-deficient tumors remain incompletely understood.
Tumor microsatellite instability (MSI) type correlates with the affected MMR gene and its substrate specificities.

Purpose of the Study:

To investigate the substrate specificities and functional redundancy of MutSalpha and MutSbeta in vitro.
To clarify the roles of these factors in repairing different types of DNA mismatches and insertion/deletion loops (IDLs).

Main Methods:

In vitro mismatch repair (MMR) assay.
Utilized three substrate constructs: GT mismatch, 1-nucleotide IDLs, and 2-nucleotide IDLs.
Assays were performed in three different cell lines.

Main Results:

MutSalpha demonstrated primary responsibility for GT mismatch and 1-nucleotide IDL repair.
Both MutSalpha and MutSbeta showed functional redundancy in repairing 2-nucleotide IDLs.
MutSbeta appeared to have a more significant role than MutSalpha in 2-nucleotide IDL repair, contrary to previous findings.

Conclusions:

MutSbeta's significant role in 2-nucleotide IDL repair has clinical relevance.
This suggests that MSH3 deficiency in tumors may present with low dinucleotide and absent mononucleotide repeat instability.