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Related Concept Videos

Mismatch Repair01:20

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 Repair01:36

Mismatch Repair

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Single-Molecule Fluorescence Visualization of DNA Polymerase Dynamics at G-Quadruplexes
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G-quadruplex recognition activities of E. Coli MutS.

Edward A Ehrat1, Bradley R Johnson, Jonathan D Williams

  • 1School of Biological Sciences, Illinois State University, Normal, IL 61790-4120, USA.

BMC Molecular Biology
|July 4, 2012
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E. coli MutS binds to guanine quadruplex (G4 DNA) structures, independent of mismatch repair activation. This suggests a role for mismatch repair factors in cellular responses to genomic instability caused by G4 DNA.

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A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1
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A G-quadruplex DNA-affinity Approach for Purification of Enzymatically Active G4 Resolvase1

Published on: March 18, 2017

Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Guanine quadruplex (G4 DNA) structures are formed from guanine-rich sequences and are implicated in genome instability.
  • The precise cellular mechanisms and factors involved in G4 DNA metabolism remain largely undefined.
  • Mismatch repair (MMR) factors, including MutS homologs, exhibit high affinity for non-B DNA forms, suggesting a potential role in G4 DNA recognition.

Purpose of the Study:

  • To investigate the ability of E. coli MutS and a specific mutant (MutS F36A) to recognize and bind G4 DNA.
  • To determine if MutS binding to G4 DNA triggers canonical mismatch repair pathway activation.
  • To explore the in vivo relevance of MutS-G4 DNA interactions in the context of cellular responses to genomic elements.

Main Methods:

  • Electrophoretic mobility shift assays (EMSA) were employed to assess the binding affinity of E. coli MutS and MutS F36A to G4 DNA and G-T heteroduplexes.
  • Nucleotide binding assays were performed to evaluate the effect on MutS-G4 DNA complex stability.
  • Bacteriophage M13 infection assays in wild-type and MutS-deficient E. coli strains were used to assess the functional consequences of G4 DNA presence.

Main Results:

  • E. coli MutS demonstrated high-affinity binding to G4 DNA, exceeding its affinity for G-T heteroduplexes.
  • The MutS F36A mutant, defective in heteroduplex recognition, retained the ability to bind G4 DNA.
  • Nucleotide binding did not induce dissociation of MutS or MutS F36A from G4 DNA, indicating a lack of canonical mismatch repair activation.
  • MutS-deficient E. coli strains exhibited reduced M13 phage infection rates when the phage DNA contained G4-forming sequences, suggesting a biological role for MutS in managing G4 DNA.

Conclusions:

  • E. coli MutS possesses specific binding activity towards non-B form G4 DNA.
  • This G4 DNA binding by MutS is independent of the activation mechanisms typical for canonical heteroduplex repair.
  • Mismatch repair factors may play a functional role in cellular responses to G4 DNA-associated genomic instability.