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Related Concept Videos

Base Excision Repair01:54

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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.
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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...
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Related Experiment Video

Updated: Apr 4, 2026

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

Susan P Lees-Miller1

  • 1Departments of Biochemistry &Molecular Biology and Oncology, Robson DNA Science Centre, Southern Alberta Cancer Research Institute, Cumming School of Medicine, University of Calgary, Calgary, Alberta, T2N 4N1, Canada.

Nature Cell Biology
|August 29, 2015
PubMed
Summary

Fumarase, an enzyme for energy production, is newly found to aid DNA repair. It moves to DNA damage sites, producing fumarate to block histone demethylation and help fix double-strand breaks.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Fumarase is a key metabolic enzyme in the mitochondria, primarily involved in the citric acid cycle and ATP production.
  • DNA double-strand breaks (DSBs) are severe forms of DNA damage that require efficient repair mechanisms to maintain genomic integrity.
  • Histone modifications play crucial roles in regulating DNA repair processes, including chromatin accessibility and the recruitment of repair factors.

Purpose of the Study:

  • To investigate a novel role for the metabolic enzyme fumarase beyond its canonical function in energy metabolism.
  • To determine if fumarase participates in cellular responses to DNA damage.
  • To elucidate the mechanism by which fumarase might influence DNA repair pathways.

Main Methods:

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  • Utilized cell-based assays to detect fumarase localization in response to DNA damage induction.
  • Employed biochemical methods to measure fumarate production at DNA damage sites.
  • Investigated the impact of fumarase activity on histone demethylation using specific inhibitors and genetic manipulation.
  • Assessed the effect of fumarase on DNA double-strand break repair efficiency.

    • Main Results:

    • Fumarase is recruited from the mitochondria to sites of DNA damage within the nucleus.
    • Recruited fumarase actively produces fumarate at DNA damage foci.
    • Fumarate generated by fumarase inhibits histone demethylation, specifically targeting H3K27me3.
    • Inhibition of histone demethylation by fumarase promotes the repair of DNA double-strand breaks.

    Conclusions:

    • Fumarase exhibits a dual role, functioning both in cellular metabolism and in DNA damage response.
    • The recruitment of fumarase to DNA damage sites and subsequent fumarate production represent a novel regulatory mechanism in DNA repair.
    • Targeting fumarase or its product fumarate may offer new therapeutic strategies for enhancing DNA repair and genome stability.