Endonuclease G is an apoptotic DNase when released from mitochondria
Abstract
Nucleosomal fragmentation of DNA is a hallmark of apoptosis (programmed cell death), and results from the activation of nucleases in cells undergoing apoptosis. One such nuclease, DNA fragmentation factor (DFF, a caspase-activated deoxyribonuclease (CAD) and its inhibitor (ICAD)), is capable of inducing DNA fragmentation and chromatin condensation after cleavage by caspase-3 (refs 2,3,4). However, although transgenic mice lacking DFF45 or its caspase cleavage site have significantly reduced DNA fragmentation, these mice still show residual DNA fragmentation and are phenotypically normal. Here we report the identification and characterization of another nuclease that is specifically activated by apoptotic stimuli and is able to induce nucleosomal fragmentation of DNA in fibroblast cells from embryonic mice lacking DFF. This nuclease is endonuclease G (endoG), a mitochondrion-specific nuclease that translocates to the nucleus during apoptosis. Once released from mitochondria, endoG cleaves chromatin DNA into nucleosomal fragments independently of caspases. Therefore, endoG represents a caspase-independent apoptotic pathway initiated from the mitochondria.
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The actual contribution of ENDOG to RCD in mammals has been questioned by generation of Endog−/− mice, whose cells display normal sensitivity to multiple lethal triggers.
“the actual contribution of ENDOG to RCD in mammals [675] has been questioned by the generation of Endog−/− mice, whose cells display normal sensitivity to multiple lethal triggers [676, 677].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [675]
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- Authors
- Li, L. Y., Luo, X., & Wang, X.
- Affiliations
- Howard Hughes Medical Institute (US)
- Corresponding author
- Wang, Xiaodong
- Venue
- Nature
- Published
- 2001-07-05
- Volume
- 412
- Issue
- 6842
- Pages
- 95-99
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W1480948328
- Cited by
- 1,787
- References
- 32
- Citations by year
- 2026: 21 · 2025: 22 · 2024: 30 · 2023: 34 · 2022: 37 · 2021: 44 · 2020: 47 · 2019: 35 · 2018: 60 · 2017: 42 · 2016: 60 · 2015: 66 · 2014: 66 · 2013: 73 · 2012: 74
- FWCI
- 46.36
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature (publishedVersion)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- endonuclease G, apoptosis, DNA fragmentation, nucleosomal DNA fragmentation, DFF45, chromatin condensation, mitochondrial translocation, fibroblasts
- MeSH terms
- Animals, Cytochrome c Group, DNA, Endodeoxyribonucleases, Humans, Mitochondria, Liver, Proteins, Recombinant Proteins, Ultraviolet Rays, Apoptosis, Caspases, Apoptosis Regulatory Proteins, Mice, Caspase 8, Caspase 9, In Vitro Techniques
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