ArticleNucleic acids research2016
Crystal structure of endonuclease G in complex with DNA reveals how it nonspecifically degrades DNA as a homodimer.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 17 citations in OpenAlex.
- Human Endonuclease G Preferentially Cleaves Oxidatively Damaged DNA.Biochemistry · 2026Article
- Discovery of an Endonuclease G-inhibitory Ku80-peptide protecting against leukemogenic rearrangements at the MLL breakpoint cluster.Nature communications · 2026Article
- Integrative Multi-Omics Mendelian Randomization Reveals Oxidative Stress Mechanisms in Major Depressive Disorder, Bipolar Disorder, and Schizophrenia.Antioxidants (Basel, Switzerland) · 2026Article
- Design of a halogen bond catalyzed DNA endonuclease.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Mitochondrial exonuclease EXOG supports DNA integrity by the removal of single-stranded DNA flaps.Nucleic acids research · 2025Article
- The CD4/CD8 ratio is associated with T lymphocyte functions in long-term virally suppressed patients with HIV.BMC infectious diseases · 2025Article
- Transmembrane nuclease NUMEN/ENDOD1 regulates DNA repair pathway choice at the nuclear periphery.Nature cell biology · 2023Article
- Structural adaptation of vertebrate endonuclease G for 5-hydroxymethylcytosine recognition and function.Nucleic acids research · 2020Article
- Origin of programmed cell death from antiviral defense?Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- A unique exonuclease ExoG cleaves between RNA and DNA in mitochondrial DNA replication.Nucleic acids research · 2019Article
- Structural insights into nanoRNA degradation by human Rexo2.RNA (New York, N.Y.) · 2019Article
- Structure-based domain assignment in Leishmania infantum EndoG: characterization of a pH-dependent regulatory switch and a C-terminal extension that largely dictates DNA substrate preferences.Nucleic acids research · 2017Article
- Protein-nucleic acids interactions: new ways of connecting structure, dynamics and function.Biophysical reviews · 2017Article
- Article
- Nucleases as a barrier to gene silencing in the cotton boll weevil, Anthonomus grandis.PloS one · 2017Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endonuclease G (EndoG) is an evolutionarily conserved mitochondrial protein in eukaryotes that digests nucleus chromosomal DNA during apoptosis and paternal mitochondrial DNA during embryogenesis. Under oxidative stress, homodimeric EndoG becomes oxidized and converts to monomers with diminished nuclease activity. However, it remains unclear why EndoG has to function as a homodimer in DNA degradation. Here, we report the crystal structure of the Caenorhabditis elegans EndoG homologue, CPS-6, in complex with single-stranded DNA at a resolution of 2.3 Å. Two separate DNA strands are bound at the ββα-metal motifs in the homodimer with their nucleobases pointing away from the enzyme, explaining why CPS-6 degrades DNA without sequence specificity. Two obligatory monomeric CPS-6 mutants (P207E and K131D/F132N) were constructed, and they degrade DNA with diminished activity due to poorer DNA-binding affinity as compared to wild-type CPS-6. Moreover, the P207E mutant exhibits predominantly 3'-to-5' exonuclease activity, indicating a possible endonuclease to exonuclease activity change. Thus, the dimer conformation of CPS-6 is essential for maintaining its optimal DNA-binding and endonuclease activity. Compared to other non-specific endonucleases, which are usually monomeric enzymes, EndoG is a unique dimeric endonuclease, whose activity hence can be modulated by oxidation to induce conformational changes.
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